Bile acid and bile salt metabolism (Homo sapiens)

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6, 14, 26, 416048, 5248, 5233, 563523, 50, 6419, 20, 44261, 3, 16, 31, 58...60388262821264, 552623, 50, 64282, 3810, 37, 4224, 40636053, 599, 15, 22, 25, 30...2613, 6128171723, 50, 64602, 382, 38, 462612, 17, 472653, 5918, 517, 392, 382, 386010, 37, 422923342, 38, 462, 382, 384, 552810, 37, 425, 49, 6323, 50, 649, 22, 25, 30, 36...2, 38, 4632262, 3823, 50, 64267, 3914, 41, 4533, 562648, 52262143212823, 50, 6423, 50, 64602610, 37, 4233, 56342623, 50, 64262827, 622, 38, 46112626212, 384, 55nucleoplasmGolgi lumencytosolmitochondrial matrixendoplasmic reticulum lumennucleoplasmendoplasmic reticulum lumennucleoplasmendoplasmic reticulum lumenendoplasmic reticulum lumenperoxisomal matrixendoplasmic reticulum lumencytosolcytosolmitochondrial matrixcytosolendoplasmic reticulum lumenO2NADP+H2O5beta-cholestan-3alpha,7alpha,12alpha,24(S)-tetrolCYP27A1TCCA NCOA1 5bCHOL3a,7a,12a,27-tetrolTHCANADPHH+NADP+5beta-cholestan-3alpha,7alpha-diol25(R) DHCA-CoAH+H2ONADP+CCA 3,7,24THCASLC27A2H2OPI4PH2O2H+H+CCA H2O5beta-cholestan-3alpha,7alpha,12alpha,27-tetrolNa+PI4PCDCA 5beta-cholestan-3alpha,7alpha,12alpha,24(S)-tetrolH2OCholest-5-ene-3beta,7alpha,27-triolNADP+GCCA NADHLCHA O2DCA NCOA1,2:RXRA:NR1H4:DCA,CDCA,LCHAO23alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-27-alpropionyl CoACYP27A1CoA-SHOSBPL3 NADPHCytochrome P450(CYP7B1 based)GCCA ATPNADPHbile salts and acidscomplexed withalbuminNCOA2H2ONR1H4CYP27A1Cytochrome P450(CYP8B1 based)CoA-SHCDCA glycocholate 7alpha-hydroxycholesterolCHOLH+CH25H (Fe2+cofactor)NADP+DCA,CDCA,LCHACHOLNADPH3alpha,7alpha,24(S)-trihydroxy-5beta-cholestan-27-alACOX2 TCDCA H2OH+H+NADP+SLCO1A25beta-cholestan-7alpha,12alpha,24(S)-triol-3-oneH+AMP5beta-cholestan-7alpha,27-diol-3-oneTCCA SLC10A1Fe2+ GCDCA H+CYP27A1O2H+24OH-CHOLGCDCA RXRAOSBPL2 BAATPTGIS AKR1C2 TCCA RXRA H+ADPtaurochenodeoxycholate CCA FABP6 HSD3B7Cytochrome P450(CYP8B1 based)CCA NCOA1cholateSLC27A5CH25H H+H2ONADHNADP+NADP+choloyl-CoA NADPHCDCA H2ONADP+H2ONCOA2 NCOA1 O2H+3alpha,7alpha-dihydroxy-5beta-cholest-24-one-CoAAKR1C3 bile salts25(R) TetraHCA-CoAPTGIS CYP39A125(S)3alpha,7alpha-dihydroxy-5beta-cholest-24-enoyl-CoAGCDCA cholate bile saltsH2OABCB11FAD 25(S) THCA-CoANADP+AKR1C1 TCDCA NADPHNR1H4:DCA,CDCA,LCHAAKR1D1ALB:(GCCA, TCCA)5beta-cholesten-7alpha, 12alpha-diol-3-oneNR1H4 DCA H+27HCHOLAKR1C2 Pialbumin:bile saltcomplexNAD+NAD+ALB 5beta-cholestan-7alpha-ol-3-oneSLC27A5H2OSTARD5 CDCA bile saltsH2OCYP7B1 NADPHNADP+4CHOL7a,12aDONEDHCAOSBPL7 GCDCA taurocholate LCHA 5beta-cholestan-7alpha,12alpha,27-triol-3-oneSLC27A2(24R,25R)3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoANADPHNADPH5bCHOL3a,7a,24(s)-triolDHCAH+LCA24OH-CHOLSTARD525(S) DHCA-CoAO2NADPHO2GCDCA TCDCA H2OGCCA H+NADPHCYP7A1 bile salts and acids(OATP-A)CHOL7a,24(S)DIOLATPCYP8B1 HSD17B4(2-736) H2O3alpha,7alpha,12alpha,24(S)-tetrahydroxy-5beta-cholestan-27-alBAAT3,7,24THCA-CoAOSBPsbile salts and acidsO2O24CHOL7a,24(S)DONENCOA2 3,7,24THCAbile saltsATPAKR1C3 AMACRNR1H4 NADPHALBLCHA 3alpha,7alpha-dihydroxy-5beta-cholestan-26-alGCCA Aldo-keto reductasefamilyO2TCCA DCA GCCA CYP27A1CoA-SHCYP8B1 TCCA CHOLPPiGCCA NADP+5beta-cholestan-3alpha,7alpha,12alpha,24(S),27-pentolTCCA CDCA GCCA, TCCAOSBPL6 ABCC3NAD+chenodeoxycholoyl-CoA LCA glycochenodeoxycholate CYP46A1GCCA choloyl-CoA;chenodeoxycholoyl-CoANa+CYP7A1 24OH-CHOLALB TAU NADP+TCCA CYP27A1FABP6CDCA NAD+CDCA THCANCOA1 NADP+ALB NADPHO2AKR1C4 NCOA1,2:RXRA:NR1H4:DCA,CDCA,LCHAAMP25OH-CHOLCoA-SHNADPHCYP7B1 STARD5:DCA,LCATCDCA 5beta-cholestan-3alpha,7alpha,26-triolCDCA CDCA CDCA albumin:bile saltand acid (OATP-A)complexH+H2ONADPHH+25OH-CHOLH2OTetraHCAAKR1C4 HSD3B7O2GCCA DCA glycocholate ATP5beta-cholestan-7alpha,24(S)-diol-3-oneH2ONADP+27OH-CHOL4CHOL7a,12a,27TONEAKR1D1NR1H4 NCOA1,2:RXRA:NR1H4:DCA,CDCA,LCHANADHNADPHTetraHCASLC27A5O2Gly 3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-one-CoAAKR1C1 THCA-CoATCDCA NADP+CHOL3b,7a,25TRIOLglycine; taurineTCCA H2ONa+TCCA PPiglycochenodeoxycholate TCDCA bile salts andacids:FABP6ATPSLCO1B1taurochenodeoxycholate NADP+GCCA Cytochrome P450(CYP7A1 based)taurocholate PiPTGIS LCHA CoA-SHHSD17B4 dimerGly 3,7,24THCA-CoATCDCA (24R,25R)3alpha,7alpha,24-trihydroxy-5beta-cholestanoyl-CoAADPAKR1C1 CYP27A125(R) THCA-CoACHOLNa+GCCA TCCA 25(R) TetraHCA-CoAPPiAldo-keto reductasefamilyO2NADPHSLCO1B35bCHOL3a,7a,12a-triolNCOA2 H+CYP8B1 NADP+AMPH+25(R) THCA-CoA27OH-CHOLH+ALB bile saltsNADP+GCDCA CDCA 4CHOL7aOLONEOSBPL1A NADPHTCDCA SLC10A2NADPHOSBPAKR1D1Cytochrome P450(CYP8B1 based)Aldo-keto reductasefamilyNADHRXRA CYP7B1 SCP2-1TCDCA 5beta-cholestan-3alpha, 7alpha-diolCYP7A1 OSBPL9 CoA-SH5bCHOL3a,7a,24(s),27-tetrolGCDCA AKR1C2 H2OCCA H+4CHOL7a,27DONEACOX2:FADCCATAU DCACytochrome P450(CYP7B1 based)TCCA GCCA RXRA NAD+H+NADP+CoA-SHH+4CHOL7a,12a,24(S)TONEglycine; taurineLCHA 5beta-cholestan-3alpha,7alpha,24(S)-triolcholate;chenodeoxycholateO225OH-CHOLO25beta-cholestan-3alpha,7alpha,26-triolH+5beta-cholestan-3alpha,7alpha,12alpha-triolNADP+25OH-CHOL25(R) DHCA-CoAchenodeoxycholatebile saltsNADPHACOT8NADP+CCA AKR1C4 chenodeoxycholoyl-CoANADPHNR1H4 DCA choloyl-CoAHSD3B7NADPHH+DCA AKR1C3


Description

In a healthy adult human, about 500 mg of cholesterol is converted to bile salts daily. Newly synthesized bile salts are secreted into the bile and released into the small intestine where they emulsify dietary fats (Russell 2003). About 95% of the bile salts in the intestine are recovered and returned to the liver (Kullak-Ublick et al. 2004; Trauner and Boyer 2002). The major pathway for bile salt synthesis in the liver begins with the conversion of cholesterol to 7alpha-hydroxycholesterol. Bile salt synthesis can also begin with the synthesis of an oxysterol - 24-hydroxycholesterol or 27-hydroxycholesterol. In the body, the initial steps of these two pathways occur in extrahepatic tissues, generating intermediates that are transported to the liver and converted to bile salts via the 7alpha-hydroxycholesterol pathway. These extrahepatic pathways contribute little to the total synthesis of bile salts, but are thought to play important roles in extrahepatic cholesterol homeostasis (Javitt 2002). View original pathway at:Reactome.

Comments

Reactome-Converter 
Pathway is converted from Reactome ID: 194068
Reactome-version 
Reactome version: 61
Reactome Author 
Reactome Author: Jassal, Bijay

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Bibliography

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  1. Lütjohann D, Breuer O, Ahlborg G, Nennesmo I, Sidén A, Diczfalusy U, Björkhem I, Björkhem I.; ''Cholesterol homeostasis in human brain: evidence for an age-dependent flux of 24S-hydroxycholesterol from the brain into the circulation.''; PubMed Europe PMC Scholia
  2. Ferdinandusse S, Denis S, van Berkel E, Dacremont G, Wanders RJ.; ''Peroxisomal fatty acid oxidation disorders and 58 kDa sterol carrier protein X (SCPx). Activity measurements in liver and fibroblasts using a newly developed method.''; PubMed Europe PMC Scholia
  3. Olkkonen VM.; ''OSBP-Related Protein Family in Lipid Transport Over Membrane Contact Sites.''; PubMed Europe PMC Scholia
  4. Steinberg SJ, Mihalik SJ, Kim DG, Cuebas DA, Watkins PA.; ''The human liver-specific homolog of very long-chain acyl-CoA synthetase is cholate:CoA ligase.''; PubMed Europe PMC Scholia
  5. Hunt MC, Solaas K, Kase BF, Alexson SE.; ''Characterization of an acyl-coA thioesterase that functions as a major regulator of peroxisomal lipid metabolism.''; PubMed Europe PMC Scholia
  6. Trauner M, Boyer JL.; ''Bile salt transporters: molecular characterization, function, and regulation.''; PubMed Europe PMC Scholia
  7. Amery L, Fransen M, De Nys K, Mannaerts GP, Van Veldhoven PP.; ''Mitochondrial and peroxisomal targeting of 2-methylacyl-CoA racemase in humans.''; PubMed Europe PMC Scholia
  8. Yamamoto R, Kallen CB, Babalola GO, Rennert H, Billheimer JT, Strauss JF.; ''Cloning and expression of a cDNA encoding human sterol carrier protein 2.''; PubMed Europe PMC Scholia
  9. Cali JJ, Hsieh CL, Francke U, Russell DW.; ''Mutations in the bile acid biosynthetic enzyme sterol 27-hydroxylase underlie cerebrotendinous xanthomatosis.''; PubMed Europe PMC Scholia
  10. Ananthanarayanan M, Balasubramanian N, Makishima M, Mangelsdorf DJ, Suchy FJ.; ''Human bile salt export pump promoter is transactivated by the farnesoid X receptor/bile acid receptor.''; PubMed Europe PMC Scholia
  11. Javitt NB.; ''Cholesterol, hydroxycholesterols, and bile acids.''; PubMed Europe PMC Scholia
  12. Noé J, Stieger B, Meier PJ.; ''Functional expression of the canalicular bile salt export pump of human liver.''; PubMed Europe PMC Scholia
  13. Kurz M, Brachvogel V, Matter H, Stengelin S, Thüring H, Kramer W.; ''Insights into the bile acid transportation system: the human ileal lipid-binding protein-cholyltaurine complex and its comparison with homologous structures.''; PubMed Europe PMC Scholia
  14. Mihalik SJ, Steinberg SJ, Pei Z, Park J, Kim DG, Heinzer AK, Dacremont G, Wanders RJ, Cuebas DA, Smith KD, Watkins PA.; ''Participation of two members of the very long-chain acyl-CoA synthetase family in bile acid synthesis and recycling.''; PubMed Europe PMC Scholia
  15. Björkhem I, Lütjohann D, Diczfalusy U, Ståhle L, Ahlborg G, Wahren J.; ''Cholesterol homeostasis in human brain: turnover of 24S-hydroxycholesterol and evidence for a cerebral origin of most of this oxysterol in the circulation.''; PubMed Europe PMC Scholia
  16. Kullak-Ublick GA, Ismair MG, Stieger B, Landmann L, Huber R, Pizzagalli F, Fattinger K, Meier PJ, Hagenbuch B.; ''Organic anion-transporting polypeptide B (OATP-B) and its functional comparison with three other OATPs of human liver.''; PubMed Europe PMC Scholia
  17. Zelcer N, Saeki T, Bot I, Kuil A, Borst P.; ''Transport of bile acids in multidrug-resistance-protein 3-overexpressing cells co-transfected with the ileal Na+-dependent bile-acid transporter.''; PubMed Europe PMC Scholia
  18. Russell DW.; ''The enzymes, regulation, and genetics of bile acid synthesis.''; PubMed Europe PMC Scholia
  19. Ishida H, Noshiro M, Okuda K, Coon MJ.; ''Purification and characterization of 7 alpha-hydroxy-4-cholesten-3-one 12 alpha-hydroxylase.''; PubMed Europe PMC Scholia
  20. Vanhove GF, Van Veldhoven PP, Fransen M, Denis S, Eyssen HJ, Wanders RJ, Mannaerts GP.; ''The CoA esters of 2-methyl-branched chain fatty acids and of the bile acid intermediates di- and trihydroxycoprostanic acids are oxidized by one single peroxisomal branched chain acyl-CoA oxidase in human liver and kidney.''; PubMed Europe PMC Scholia
  21. Schwarz M, Wright AC, Davis DL, Nazer H, Björkhem I, Russell DW.; ''The bile acid synthetic gene 3beta-hydroxy-Delta(5)-C(27)-steroid oxidoreductase is mutated in progressive intrahepatic cholestasis.''; PubMed Europe PMC Scholia
  22. Johnson MR, Barnes S, Kwakye JB, Diasio RB.; ''Purification and characterization of bile acid-CoA:amino acid N-acyltransferase from human liver.''; PubMed Europe PMC Scholia
  23. Parks DJ, Blanchard SG, Bledsoe RK, Chandra G, Consler TG, Kliewer SA, Stimmel JB, Willson TM, Zavacki AM, Moore DD, Lehmann JM.; ''Bile acids: natural ligands for an orphan nuclear receptor.''; PubMed Europe PMC Scholia
  24. Kondo KH, Kai MH, Setoguchi Y, Eggertsen G, Sjöblom P, Setoguchi T, Okuda KI, Björkhem I.; ''Cloning and expression of cDNA of human delta 4-3-oxosteroid 5 beta-reductase and substrate specificity of the expressed enzyme.''; PubMed Europe PMC Scholia
  25. Ferdinandusse S, Denis S, Clayton PT, Graham A, Rees JE, Allen JT, McLean BN, Brown AY, Vreken P, Waterham HR, Wanders RJ.; ''Mutations in the gene encoding peroxisomal alpha-methylacyl-CoA racemase cause adult-onset sensory motor neuropathy.''; PubMed Europe PMC Scholia
  26. Cali JJ, Russell DW.; ''Characterization of human sterol 27-hydroxylase. A mitochondrial cytochrome P-450 that catalyzes multiple oxidation reaction in bile acid biosynthesis.''; PubMed Europe PMC Scholia
  27. Li-Hawkins J, Lund EG, Bronson AD, Russell DW.; ''Expression cloning of an oxysterol 7alpha-hydroxylase selective for 24-hydroxycholesterol.''; PubMed Europe PMC Scholia
  28. Schmitz W, Albers C, Fingerhut R, Conzelmann E.; ''Purification and characterization of an alpha-methylacyl-CoA racemase from human liver.''; PubMed Europe PMC Scholia
  29. Bodo A, Bakos E, Szeri F, Varadi A, Sarkadi B.; ''Differential modulation of the human liver conjugate transporters MRP2 and MRP3 by bile acids and organic anions.''; PubMed Europe PMC Scholia
  30. Weber-Boyvat M, Zhong W, Yan D, Olkkonen VM.; ''Oxysterol-binding proteins: functions in cell regulation beyond lipid metabolism.''; PubMed Europe PMC Scholia
  31. Hsiang B, Zhu Y, Wang Z, Wu Y, Sasseville V, Yang WP, Kirchgessner TG.; ''A novel human hepatic organic anion transporting polypeptide (OATP2). Identification of a liver-specific human organic anion transporting polypeptide and identification of rat and human hydroxymethylglutaryl-CoA reductase inhibitor transporters.''; PubMed Europe PMC Scholia
  32. Suchanek M, Hynynen R, Wohlfahrt G, Lehto M, Johansson M, Saarinen H, Radzikowska A, Thiele C, Olkkonen VM.; ''The mammalian oxysterol-binding protein-related proteins (ORPs) bind 25-hydroxycholesterol in an evolutionarily conserved pocket.''; PubMed Europe PMC Scholia
  33. Plass JR, Mol O, Heegsma J, Geuken M, Faber KN, Jansen PL, Müller M.; ''Farnesoid X receptor and bile salts are involved in transcriptional regulation of the gene encoding the human bile salt export pump.''; PubMed Europe PMC Scholia
  34. Lee FY, Lee H, Hubbert ML, Edwards PA, Zhang Y.; ''FXR, a multipurpose nuclear receptor.''; PubMed Europe PMC Scholia
  35. Gåfvels M, Olin M, Chowdhary BP, Raudsepp T, Andersson U, Persson B, Jansson M, Björkhem I, Björkhem I, Eggertsen G.; ''Structure and chromosomal assignment of the sterol 12alpha-hydroxylase gene (CYP8B1) in human and mouse: eukaryotic cytochrome P-450 gene devoid of introns.''; PubMed Europe PMC Scholia
  36. Dufort I, Labrie F, Luu-The V.; ''Human types 1 and 3 3 alpha-hydroxysteroid dehydrogenases: differential lability and tissue distribution.''; PubMed Europe PMC Scholia
  37. Lund EG, Guileyardo JM, Russell DW.; ''cDNA cloning of cholesterol 24-hydroxylase, a mediator of cholesterol homeostasis in the brain.''; PubMed Europe PMC Scholia
  38. Holt JA, Luo G, Billin AN, Bisi J, McNeill YY, Kozarsky KF, Donahee M, Wang DY, Mansfield TA, Kliewer SA, Goodwin B, Jones SA.; ''Definition of a novel growth factor-dependent signal cascade for the suppression of bile acid biosynthesis.''; PubMed Europe PMC Scholia
  39. Jiang LL, Kobayashi A, Matsuura H, Fukushima H, Hashimoto T.; ''Purification and properties of human D-3-hydroxyacyl-CoA dehydratase: medium-chain enoyl-CoA hydratase is D-3-hydroxyacyl-CoA dehydratase.''; PubMed Europe PMC Scholia
  40. Houten SM, Watanabe M, Auwerx J.; ''Endocrine functions of bile acids.''; PubMed Europe PMC Scholia
  41. Mesmin B, Bigay J, Moser von Filseck J, Lacas-Gervais S, Drin G, Antonny B.; ''A four-step cycle driven by PI(4)P hydrolysis directs sterol/PI(4)P exchange by the ER-Golgi tether OSBP.''; PubMed Europe PMC Scholia
  42. Hagenbuch B, Meier PJ.; ''Molecular cloning, chromosomal localization, and functional characterization of a human liver Na+/bile acid cotransporter.''; PubMed Europe PMC Scholia
  43. Charman M, Colbourne TR, Pietrangelo A, Kreplak L, Ridgway ND.; ''Oxysterol-binding protein (OSBP)-related protein 4 (ORP4) is essential for cell proliferation and survival.''; PubMed Europe PMC Scholia
  44. Zhang Y, Kast-Woelbern HR, Edwards PA.; ''Natural structural variants of the nuclear receptor farnesoid X receptor affect transcriptional activation.''; PubMed Europe PMC Scholia
  45. Lund EG, Kerr TA, Sakai J, Li WP, Russell DW.; ''cDNA cloning of mouse and human cholesterol 25-hydroxylases, polytopic membrane proteins that synthesize a potent oxysterol regulator of lipid metabolism.''; PubMed Europe PMC Scholia
  46. Noshiro M, Okuda K.; ''Molecular cloning and sequence analysis of cDNA encoding human cholesterol 7 alpha-hydroxylase.''; PubMed Europe PMC Scholia
  47. Pikuleva IA, Babiker A, Waterman MR, Björkhem I, Björkhem I.; ''Activities of recombinant human cytochrome P450c27 (CYP27) which produce intermediates of alternative bile acid biosynthetic pathways.''; PubMed Europe PMC Scholia
  48. Létourneau D, Lefebvre A, Lavigne P, LeHoux JG.; ''STARD5 specific ligand binding: comparison with STARD1 and STARD4 subfamilies.''; PubMed Europe PMC Scholia
  49. Steinberg SJ, Wang SJ, McGuinness MC, Watkins PA.; ''Human liver-specific very-long-chain acyl-coenzyme A synthetase: cDNA cloning and characterization of a second enzymatically active protein.''; PubMed Europe PMC Scholia
  50. Mast N, Norcross R, Andersson U, Shou M, Nakayama K, Bjorkhem I, Bjorkhem I, Pikuleva IA.; ''Broad substrate specificity of human cytochrome P450 46A1 which initiates cholesterol degradation in the brain.''; PubMed Europe PMC Scholia
  51. Jones JM, Nau K, Geraghty MT, Erdmann R, Gould SJ.; ''Identification of peroxisomal acyl-CoA thioesterases in yeast and humans.''; PubMed Europe PMC Scholia
  52. Kullak-Ublick GA, Stieger B, Meier PJ.; ''Enterohepatic bile salt transporters in normal physiology and liver disease.''; PubMed Europe PMC Scholia
  53. Falany CN, Johnson MR, Barnes S, Diasio RB.; ''Glycine and taurine conjugation of bile acids by a single enzyme. Molecular cloning and expression of human liver bile acid CoA:amino acid N-acyltransferase.''; PubMed Europe PMC Scholia
  54. Cheng JB, Jacquemin E, Gerhardt M, Nazer H, Cresteil D, Heubi JE, Setchell KD, Russell DW.; ''Molecular genetics of 3beta-hydroxy-Delta5-C27-steroid oxidoreductase deficiency in 16 patients with loss of bile acid synthesis and liver disease.''; PubMed Europe PMC Scholia
  55. Olkkonen VM, Li S.; ''Oxysterol-binding proteins: sterol and phosphoinositide sensors coordinating transport, signaling and metabolism.''; PubMed Europe PMC Scholia
  56. Makishima M, Okamoto AY, Repa JJ, Tu H, Learned RM, Luk A, Hull MV, Lustig KD, Mangelsdorf DJ, Shan B.; ''Identification of a nuclear receptor for bile acids.''; PubMed Europe PMC Scholia
  57. Wu Z, Martin KO, Javitt NB, Chiang JY.; ''Structure and functions of human oxysterol 7alpha-hydroxylase cDNAs and gene CYP7B1.''; PubMed Europe PMC Scholia
  58. Solaas K, Ulvestad A, Söreide O, Kase BF.; ''Subcellular organization of bile acid amidation in human liver: a key issue in regulating the biosynthesis of bile salts.''; PubMed Europe PMC Scholia
  59. Zeng H, Liu G, Rea PA, Kruh GD.; ''Transport of amphipathic anions by human multidrug resistance protein 3.''; PubMed Europe PMC Scholia
  60. Abe T, Kakyo M, Tokui T, Nakagomi R, Nishio T, Nakai D, Nomura H, Unno M, Suzuki M, Naitoh T, Matsuno S, Yawo H.; ''Identification of a novel gene family encoding human liver-specific organic anion transporter LST-1.''; PubMed Europe PMC Scholia
  61. Byrne JA, Strautnieks SS, Mieli-Vergani G, Higgins CF, Linton KJ, Thompson RJ.; ''The human bile salt export pump: characterization of substrate specificity and identification of inhibitors.''; PubMed Europe PMC Scholia
  62. Baumgart E, Vanhooren JC, Fransen M, Marynen P, Puype M, Vandekerckhove J, Leunissen JA, Fahimi HD, Mannaerts GP, van Veldhoven PP.; ''Molecular characterization of the human peroxisomal branched-chain acyl-CoA oxidase: cDNA cloning, chromosomal assignment, tissue distribution, and evidence for the absence of the protein in Zellweger syndrome.''; PubMed Europe PMC Scholia
  63. Wang C, JeBailey L, Ridgway ND.; ''Oxysterol-binding-protein (OSBP)-related protein 4 binds 25-hydroxycholesterol and interacts with vimentin intermediate filaments.''; PubMed Europe PMC Scholia
  64. Kullak-Ublick GA, Hagenbuch B, Stieger B, Schteingart CD, Hofmann AF, Wolkoff AW, Meier PJ.; ''Molecular and functional characterization of an organic anion transporting polypeptide cloned from human liver.''; PubMed Europe PMC Scholia
  65. Létourneau D, Lorin A, Lefebvre A, Frappier V, Gaudreault F, Najmanovich R, Lavigne P, LeHoux JG.; ''StAR-related lipid transfer domain protein 5 binds primary bile acids.''; PubMed Europe PMC Scholia

History

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CompareRevisionActionTimeUserComment
114948view16:47, 25 January 2021ReactomeTeamReactome version 75
113392view11:46, 2 November 2020ReactomeTeamReactome version 74
112597view15:57, 9 October 2020ReactomeTeamReactome version 73
104892view15:14, 23 June 2019EgonwReplaced a secondary ChEBI identifiers with a primary identifier.
101513view11:37, 1 November 2018ReactomeTeamreactome version 66
101049view21:19, 31 October 2018ReactomeTeamreactome version 65
100580view19:53, 31 October 2018ReactomeTeamreactome version 64
100129view16:38, 31 October 2018ReactomeTeamreactome version 63
99679view15:08, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
99272view12:45, 31 October 2018ReactomeTeamreactome version 62
93944view13:46, 16 August 2017ReactomeTeamreactome version 61
93534view11:26, 9 August 2017ReactomeTeamreactome version 61
86633view09:22, 11 July 2016ReactomeTeamreactome version 56
83139view10:08, 18 November 2015ReactomeTeamVersion54
81480view13:01, 21 August 2015ReactomeTeamVersion53
76958view08:24, 17 July 2014ReactomeTeamFixed remaining interactions
76663view12:03, 16 July 2014ReactomeTeamFixed remaining interactions
75992view10:05, 11 June 2014ReactomeTeamRe-fixing comment source
75695view11:03, 10 June 2014ReactomeTeamReactome 48 Update
75051view13:56, 8 May 2014AnweshaFixing comment source for displaying WikiPathways description
74695view08:46, 30 April 2014ReactomeTeamReactome46
44976view14:24, 6 October 2011MartijnVanIerselOntology Term : 'bile acid biosynthetic pathway' added !
42156view23:17, 4 March 2011MaintBotModified categories
42011view21:50, 4 March 2011MaintBotAutomatic update
39814view05:51, 21 January 2011MaintBotNew pathway

External references

DataNodes

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NameTypeDatabase referenceComment
(24R,

25R)

3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA
MetaboliteCHEBI:52050 (ChEBI)
(24R,

25R)

3alpha,7alpha,24-trihydroxy-5beta-cholestanoyl-CoA
MetaboliteCHEBI:27403 (ChEBI)
24OH-CHOLMetaboliteCHEBI:34310 (ChEBI)
25(R) DHCA-CoAMetaboliteCHEBI:15494 (ChEBI)
25(R) THCA-CoAMetaboliteCHEBI:37642 (ChEBI)
25(R) TetraHCA-CoAMetaboliteCHEBI:27458 (ChEBI)
25(S) 3alpha,7alpha-dihydroxy-5beta-cholest-24-enoyl-CoAMetaboliteCHEBI:27393 (ChEBI)
25(S) DHCA-CoAMetaboliteCHEBI:15494 (ChEBI)
25(S) THCA-CoAMetaboliteCHEBI:37643 (ChEBI)
25OH-CHOLMetaboliteCHEBI:42977 (ChEBI)
27HCHOLMetaboliteCHEBI:17703 (ChEBI)
27OH-CHOLMetaboliteCHEBI:17703 (ChEBI)
3,7,24THCA-CoAMetaboliteCHEBI:27403 (ChEBI)
3,7,24THCAMetaboliteCHEBI:27403 (ChEBI)
3alpha,7alpha,12alpha,24(S)-tetrahydroxy-5beta-cholestan-27-alMetaboliteCHEBI:63849 (ChEBI)
3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-one-CoAMetaboliteCHEBI:27379 (ChEBI)
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-27-alMetaboliteCHEBI:16466 (ChEBI)
3alpha,7alpha,24(S)-trihydroxy-5beta-cholestan-27-alMetaboliteCHEBI:63848 (ChEBI)
3alpha,7alpha-dihydroxy-5beta-cholest-24-one-CoAMetaboliteCHEBI:28533 (ChEBI)
3alpha,7alpha-dihydroxy-5beta-cholestan-26-alMetaboliteCHEBI:27428 (ChEBI)
4CHOL7a,12a,24(S)TONEMetaboliteCHEBI:63839 (ChEBI)
4CHOL7a,12a,27TONEMetaboliteCHEBI:48333 (ChEBI)
4CHOL7a,12aDONEMetaboliteCHEBI:28477 (ChEBI)
4CHOL7a,24(S)DONEMetaboliteCHEBI:63838 (ChEBI)
4CHOL7a,27DONEMetaboliteCHEBI:48825 (ChEBI)
4CHOL7aOLONEMetaboliteCHEBI:17899 (ChEBI)
5bCHOL3a,7a,12a,27-tetrolMetaboliteCHEBI:17278 (ChEBI)
5bCHOL3a,7a,12a-triolMetaboliteCHEBI:16496 (ChEBI)
5bCHOL3a,7a,24(s),27-tetrolMetaboliteCHEBI:63833 (ChEBI)
5bCHOL3a,7a,24(s)-triolMetaboliteCHEBI:63831 (ChEBI)
5beta-cholestan-3alpha, 7alpha-diolMetaboliteCHEBI:28047 (ChEBI)
5beta-cholestan-3alpha,7alpha,12alpha,24(S),27-pentolMetaboliteCHEBI:63835 (ChEBI)
5beta-cholestan-3alpha,7alpha,12alpha,24(S)-tetrolMetaboliteCHEBI:63834 (ChEBI)
5beta-cholestan-3alpha,7alpha,12alpha,27-tetrolMetaboliteCHEBI:17278 (ChEBI)
5beta-cholestan-3alpha,7alpha,12alpha-triolMetaboliteCHEBI:16496 (ChEBI)
5beta-cholestan-3alpha,7alpha,24(S)-triolMetaboliteCHEBI:63831 (ChEBI)
5beta-cholestan-3alpha,7alpha,26-triolMetaboliteCHEBI:28540 (ChEBI)
5beta-cholestan-3alpha,7alpha-diolMetaboliteCHEBI:28047 (ChEBI)
5beta-cholestan-7alpha,12alpha,24(S)-triol-3-oneMetaboliteCHEBI:63830 (ChEBI)
5beta-cholestan-7alpha,12alpha,27-triol-3-oneMetaboliteCHEBI:48834 (ChEBI)
5beta-cholestan-7alpha,24(S)-diol-3-oneMetaboliteCHEBI:63829 (ChEBI)
5beta-cholestan-7alpha,27-diol-3-oneMetaboliteCHEBI:48778 (ChEBI)
5beta-cholestan-7alpha-ol-3-oneMetaboliteCHEBI:2290 (ChEBI)
5beta-cholesten-7alpha, 12alpha-diol-3-oneMetaboliteCHEBI:2288 (ChEBI)
7 alpha-hydroxycholesterolMetaboliteCHEBI:17500 (ChEBI)
ABCB11ProteinO95342 (Uniprot-TrEMBL)
ABCC3ProteinO15438 (Uniprot-TrEMBL)
ACOT8ProteinO14734 (Uniprot-TrEMBL)
ACOX2 ProteinQ99424 (Uniprot-TrEMBL)
ACOX2:FADComplexR-HSA-192320 (Reactome)
ADPMetaboliteCHEBI:16761 (ChEBI)
AKR1C1 ProteinQ04828 (Uniprot-TrEMBL)
AKR1C2 ProteinP52895 (Uniprot-TrEMBL)
AKR1C3 ProteinP42330 (Uniprot-TrEMBL)
AKR1C4 ProteinP17516 (Uniprot-TrEMBL)
AKR1D1ProteinP51857 (Uniprot-TrEMBL)
ALB ProteinP02768 (Uniprot-TrEMBL)
ALB:(GCCA, TCCA)ComplexR-HSA-194104 (Reactome)
ALBProteinP02768 (Uniprot-TrEMBL)
AMACRProteinQ9UHK6 (Uniprot-TrEMBL)
AMPMetaboliteCHEBI:16027 (ChEBI)
ATPMetaboliteCHEBI:15422 (ChEBI)
Aldo-keto reductase familyComplexR-HSA-3229260 (Reactome) This CandidateSet contains sequences identified by William Pearson's analysis of Reactome catalyst entities. Catalyst entity sequences were used to identify analagous sequences that shared overall homology and active site homology. Sequences in this Candidate set were identified in an April 24, 2012 analysis.
BAATProteinQ14032 (Uniprot-TrEMBL)
CCA MetaboliteCHEBI:16359 (ChEBI)
CCAMetaboliteCHEBI:16359 (ChEBI)
CDCA MetaboliteCHEBI:16755 (ChEBI)
CH25H (Fe2+ cofactor)ComplexR-HSA-192180 (Reactome)
CH25H ProteinO95992 (Uniprot-TrEMBL)
CHOL3b,7a,25TRIOLMetaboliteCHEBI:37623 (ChEBI)
CHOL7a,24(S)DIOLMetaboliteCHEBI:37640 (ChEBI)
CHOLMetaboliteCHEBI:16113 (ChEBI)
CYP27A1ProteinQ02318 (Uniprot-TrEMBL)
CYP39A1ProteinQ9NYL5 (Uniprot-TrEMBL)
CYP46A1ProteinQ9Y6A2 (Uniprot-TrEMBL)
CYP7A1 ProteinP22680 (Uniprot-TrEMBL)
CYP7B1 ProteinO75881 (Uniprot-TrEMBL)
CYP8B1 ProteinQ9UNU6 (Uniprot-TrEMBL)
Cholest-5-ene-3beta,7alpha,27-triolMetaboliteCHEBI:18431 (ChEBI)
CoA-SHMetaboliteCHEBI:15346 (ChEBI)
Cytochrome P450 (CYP7A1 based)ComplexR-HSA-3219435 (Reactome) This CandidateSet contains sequences identified by William Pearson's analysis of Reactome catalyst entities. Catalyst entity sequences were used to identify analagous sequences that shared overall homology and active site homology. Sequences in this Candidate set were identified in an April 24, 2012 analysis.
Cytochrome P450 (CYP7B1 based)ComplexR-HSA-2975806 (Reactome) This CandidateSet contains sequences identified by William Pearson's analysis of Reactome catalyst entities. Catalyst entity sequences were used to identify analagous sequences that shared overall homology and active site homology. Sequences in this Candidate set were identified in an April 24, 2012 analysis.
Cytochrome P450 (CYP8B1 based)ComplexR-HSA-3229177 (Reactome) This CandidateSet contains sequences identified by William Pearson's analysis of Reactome catalyst entities. Catalyst entity sequences were used to identify analagous sequences that shared overall homology and active site homology. Sequences in this Candidate set were identified in an April 24, 2012 analysis.
DCA MetaboliteCHEBI:28834 (ChEBI)
DCA,CDCA,LCHAComplexR-ALL-5340249 (Reactome)
DCAMetaboliteCHEBI:28834 (ChEBI)
DHCAMetaboliteCHEBI:16577 (ChEBI)
FABP6 ProteinP51161 (Uniprot-TrEMBL)
FABP6ProteinP51161 (Uniprot-TrEMBL)
FAD MetaboliteCHEBI:16238 (ChEBI)
Fe2+ MetaboliteCHEBI:18248 (ChEBI)
GCCA MetaboliteCHEBI:17687 (ChEBI)
GCCA, TCCAComplexR-ALL-194097 (Reactome)
GCDCA MetaboliteCHEBI:36274 (ChEBI)
Gly MetaboliteCHEBI:57305 (ChEBI)
H+MetaboliteCHEBI:15378 (ChEBI)
H2O2MetaboliteCHEBI:16240 (ChEBI)
H2OMetaboliteCHEBI:15377 (ChEBI)
HSD17B4 dimerComplexR-HSA-389999 (Reactome)
HSD17B4(2-736) ProteinP51659 (Uniprot-TrEMBL)
HSD3B7ProteinQ9H2F3 (Uniprot-TrEMBL)
LCA MetaboliteCHEBI:16325 (ChEBI)
LCAMetaboliteCHEBI:16325 (ChEBI)
LCHA MetaboliteCHEBI:16325 (ChEBI)
NAD+MetaboliteCHEBI:15846 (ChEBI)
NADHMetaboliteCHEBI:16908 (ChEBI)
NADP+MetaboliteCHEBI:18009 (ChEBI)
NADPHMetaboliteCHEBI:16474 (ChEBI)
NCOA1 ProteinQ15788 (Uniprot-TrEMBL)
NCOA1,2:RXRA:NR1H4:DCA,CDCA,LCHAComplexR-HSA-5340274 (Reactome)
NCOA1ProteinQ15788 (Uniprot-TrEMBL)
NCOA2 ProteinQ15596 (Uniprot-TrEMBL)
NCOA2ProteinQ15596 (Uniprot-TrEMBL)
NR1H4 ProteinQ96RI1 (Uniprot-TrEMBL)
NR1H4:DCA,CDCA,LCHAComplexR-HSA-5340186 (Reactome)
NR1H4ProteinQ96RI1 (Uniprot-TrEMBL)
Na+MetaboliteCHEBI:29101 (ChEBI)
O2MetaboliteCHEBI:15379 (ChEBI)
OSBPL1A ProteinQ9BXW6 (Uniprot-TrEMBL)
OSBPL2 ProteinQ9H1P3 (Uniprot-TrEMBL)
OSBPL3 ProteinQ9H4L5 (Uniprot-TrEMBL)
OSBPL6 ProteinQ9BZF3 (Uniprot-TrEMBL)
OSBPL7 ProteinQ9BZF2 (Uniprot-TrEMBL)
OSBPL9 ProteinQ96SU4 (Uniprot-TrEMBL)
OSBPProteinP22059 (Uniprot-TrEMBL)
OSBPsComplexR-HSA-8868084 (Reactome)
PI4PMetaboliteCHEBI:17526 (ChEBI)
PPiMetaboliteCHEBI:29888 (ChEBI)
PTGIS ProteinQ16647 (Uniprot-TrEMBL)
PiMetaboliteCHEBI:18367 (ChEBI)
RXRA ProteinP19793 (Uniprot-TrEMBL)
RXRAProteinP19793 (Uniprot-TrEMBL)
SCP2-1ProteinP22307-1 (Uniprot-TrEMBL)
SLC10A1ProteinQ14973 (Uniprot-TrEMBL)
SLC10A2ProteinQ12908 (Uniprot-TrEMBL)
SLC27A2ProteinO14975 (Uniprot-TrEMBL)
SLC27A5ProteinQ9Y2P5 (Uniprot-TrEMBL)
SLCO1A2ProteinP46721 (Uniprot-TrEMBL)
SLCO1B1ProteinQ9Y6L6 (Uniprot-TrEMBL)
SLCO1B3ProteinQ9NPD5 (Uniprot-TrEMBL)
STARD5 ProteinQ9NSY2 (Uniprot-TrEMBL)
STARD5:DCA,LCAComplexR-HSA-8873894 (Reactome)
STARD5ProteinQ9NSY2 (Uniprot-TrEMBL)
TAU MetaboliteCHEBI:15891 (ChEBI)
TCCA MetaboliteCHEBI:28865 (ChEBI)
TCDCA MetaboliteCHEBI:16525 (ChEBI)
TCDCA MetaboliteCHEBI:9407 (ChEBI)
THCA-CoAMetaboliteCHEBI:27505 (ChEBI)
THCAMetaboliteCHEBI:18402 (ChEBI)
TetraHCAMetaboliteCHEBI:63824 (ChEBI)
albumin:bile salt

and acid (OATP-A)

complex
ComplexR-HSA-194110 (Reactome)
albumin:bile salt complexComplexR-HSA-194125 (Reactome)
bile salts and acids:FABP6ComplexR-HSA-194191 (Reactome)
bile salts and acids (OATP-A)ComplexR-ALL-194131 (Reactome)
bile salts and acids

complexed with

albumin
ComplexR-HSA-194165 (Reactome)
bile salts and acidsComplexR-ALL-192483 (Reactome)
bile saltsComplexR-ALL-193416 (Reactome)
bile saltsComplexR-ALL-193448 (Reactome)
bile saltsComplexR-ALL-193479 (Reactome)
chenodeoxycholate bile saltsComplexR-ALL-193453 (Reactome)
chenodeoxycholoyl-CoA MetaboliteCHEBI:28701 (ChEBI)
chenodeoxycholoyl-CoAMetaboliteCHEBI:28701 (ChEBI)
cholate bile saltsComplexR-ALL-193404 (Reactome)
cholate; chenodeoxycholateComplexR-ALL-194096 (Reactome)
cholateMetaboliteCHEBI:16359 (ChEBI)
choloyl-CoA MetaboliteCHEBI:15519 (ChEBI)
choloyl-CoA; chenodeoxycholoyl-CoAComplexR-ALL-194073 (Reactome)
choloyl-CoAMetaboliteCHEBI:15519 (ChEBI)
glycine; taurineComplexR-ALL-193463 (Reactome)
glycine; taurineComplexR-ALL-194069 (Reactome)
glycochenodeoxycholate MetaboliteCHEBI:36274 (ChEBI)
glycocholate MetaboliteCHEBI:17687 (ChEBI)
propionyl CoAMetaboliteCHEBI:15539 (ChEBI)
taurochenodeoxycholate MetaboliteCHEBI:16525 (ChEBI)
taurocholate MetaboliteCHEBI:28865 (ChEBI)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
(24R,

25R)

3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA
ArrowR-HSA-192331 (Reactome)
(24R,

25R)

3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA
ArrowR-HSA-193763 (Reactome)
(24R,

25R)

3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA
R-HSA-193455 (Reactome)
(24R,

25R)

3alpha,7alpha,24-trihydroxy-5beta-cholestanoyl-CoA
ArrowR-HSA-193535 (Reactome)
(24R,

25R)

3alpha,7alpha,24-trihydroxy-5beta-cholestanoyl-CoA
ArrowR-HSA-193736 (Reactome)
(24R,

25R)

3alpha,7alpha,24-trihydroxy-5beta-cholestanoyl-CoA
R-HSA-193508 (Reactome)
24OH-CHOLArrowR-HSA-192061 (Reactome)
24OH-CHOLArrowR-HSA-193767 (Reactome)
24OH-CHOLArrowR-HSA-193776 (Reactome)
24OH-CHOLR-HSA-192178 (Reactome)
24OH-CHOLR-HSA-193767 (Reactome)
24OH-CHOLR-HSA-193776 (Reactome)
25(R) DHCA-CoAArrowR-HSA-193407 (Reactome)
25(R) DHCA-CoAArrowR-HSA-193424 (Reactome)
25(R) DHCA-CoAArrowR-HSA-193482 (Reactome)
25(R) DHCA-CoAR-HSA-193452 (Reactome)
25(R) DHCA-CoAR-HSA-193482 (Reactome)
25(R) THCA-CoAArrowR-HSA-192137 (Reactome)
25(R) THCA-CoAArrowR-HSA-192325 (Reactome)
25(R) THCA-CoAArrowR-HSA-193401 (Reactome)
25(R) THCA-CoAR-HSA-192056 (Reactome)
25(R) THCA-CoAR-HSA-192325 (Reactome)
25(R) TetraHCA-CoAArrowR-HSA-193727 (Reactome)
25(R) TetraHCA-CoAArrowR-HSA-193761 (Reactome)
25(R) TetraHCA-CoAArrowR-HSA-193766 (Reactome)
25(R) TetraHCA-CoAR-HSA-193761 (Reactome)
25(R) TetraHCA-CoAR-HSA-193763 (Reactome)
25(S) 3alpha,7alpha-dihydroxy-5beta-cholest-24-enoyl-CoAArrowR-HSA-193369 (Reactome)
25(S) 3alpha,7alpha-dihydroxy-5beta-cholest-24-enoyl-CoAR-HSA-193535 (Reactome)
25(S) DHCA-CoAArrowR-HSA-193452 (Reactome)
25(S) DHCA-CoAR-HSA-193369 (Reactome)
25(S) THCA-CoAArrowR-HSA-192056 (Reactome)
25(S) THCA-CoAR-HSA-192335 (Reactome)
25OH-CHOLArrowR-HSA-191983 (Reactome)
25OH-CHOLArrowR-HSA-8867667 (Reactome)
25OH-CHOLArrowR-HSA-8868402 (Reactome)
25OH-CHOLR-HSA-192065 (Reactome)
25OH-CHOLR-HSA-8867667 (Reactome)
25OH-CHOLR-HSA-8868402 (Reactome)
27HCHOLArrowR-HSA-193801 (Reactome)
27HCHOLR-HSA-191972 (Reactome)
27OH-CHOLArrowR-HSA-192123 (Reactome)
27OH-CHOLArrowR-HSA-193812 (Reactome)
27OH-CHOLR-HSA-193801 (Reactome)
27OH-CHOLR-HSA-193812 (Reactome)
3,7,24THCA-CoAArrowR-HSA-193711 (Reactome)
3,7,24THCA-CoAArrowR-HSA-193743 (Reactome)
3,7,24THCA-CoAArrowR-HSA-193753 (Reactome)
3,7,24THCA-CoAR-HSA-193736 (Reactome)
3,7,24THCA-CoAR-HSA-193753 (Reactome)
3,7,24THCAArrowR-HSA-193737 (Reactome)
3,7,24THCAArrowR-HSA-193786 (Reactome)
3,7,24THCAR-HSA-193711 (Reactome)
3,7,24THCAR-HSA-193743 (Reactome)
3,7,24THCAR-HSA-193786 (Reactome)
3alpha,7alpha,12alpha,24(S)-tetrahydroxy-5beta-cholestan-27-alArrowR-HSA-193780 (Reactome)
3alpha,7alpha,12alpha,24(S)-tetrahydroxy-5beta-cholestan-27-alR-HSA-193713 (Reactome)
3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-one-CoAArrowR-HSA-193455 (Reactome)
3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-one-CoAR-HSA-192341 (Reactome)
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-27-alArrowR-HSA-192042 (Reactome)
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-27-alR-HSA-192054 (Reactome)
3alpha,7alpha,24(S)-trihydroxy-5beta-cholestan-27-alArrowR-HSA-193719 (Reactome)
3alpha,7alpha,24(S)-trihydroxy-5beta-cholestan-27-alR-HSA-193737 (Reactome)
3alpha,7alpha-dihydroxy-5beta-cholest-24-one-CoAArrowR-HSA-193508 (Reactome)
3alpha,7alpha-dihydroxy-5beta-cholest-24-one-CoAR-HSA-193533 (Reactome)
3alpha,7alpha-dihydroxy-5beta-cholestan-26-alArrowR-HSA-193497 (Reactome)
3alpha,7alpha-dihydroxy-5beta-cholestan-26-alR-HSA-193460 (Reactome)
4CHOL7a,12a,24(S)TONEArrowR-HSA-193709 (Reactome)
4CHOL7a,12a,24(S)TONER-HSA-193755 (Reactome)
4CHOL7a,12a,27TONEArrowR-HSA-193845 (Reactome)
4CHOL7a,12a,27TONER-HSA-193821 (Reactome)
4CHOL7a,12aDONEArrowR-HSA-192157 (Reactome)
4CHOL7a,12aDONER-HSA-192067 (Reactome)
4CHOL7a,24(S)DONEArrowR-HSA-193789 (Reactome)
4CHOL7a,24(S)DONER-HSA-193709 (Reactome)
4CHOL7a,24(S)DONER-HSA-193746 (Reactome)
4CHOL7a,27DONEArrowR-HSA-193816 (Reactome)
4CHOL7a,27DONER-HSA-193824 (Reactome)
4CHOL7a,27DONER-HSA-193845 (Reactome)
4CHOL7aOLONEArrowR-HSA-192097 (Reactome)
4CHOL7aOLONER-HSA-192033 (Reactome)
4CHOL7aOLONER-HSA-192157 (Reactome)
5bCHOL3a,7a,12a,27-tetrolArrowR-HSA-191999 (Reactome)
5bCHOL3a,7a,12a,27-tetrolArrowR-HSA-193832 (Reactome)
5bCHOL3a,7a,12a,27-tetrolR-HSA-192042 (Reactome)
5bCHOL3a,7a,12a-triolArrowR-HSA-192010 (Reactome)
5bCHOL3a,7a,12a-triolR-HSA-191999 (Reactome)
5bCHOL3a,7a,24(s),27-tetrolArrowR-HSA-193792 (Reactome)
5bCHOL3a,7a,24(s),27-tetrolR-HSA-193719 (Reactome)
5bCHOL3a,7a,24(s)-triolArrowR-HSA-193715 (Reactome)
5bCHOL3a,7a,24(s)-triolR-HSA-193792 (Reactome)
5beta-cholestan-3alpha, 7alpha-diolArrowR-HSA-193537 (Reactome)
5beta-cholestan-3alpha, 7alpha-diolR-HSA-193393 (Reactome)
5beta-cholestan-3alpha,7alpha,12alpha,24(S),27-pentolArrowR-HSA-193787 (Reactome)
5beta-cholestan-3alpha,7alpha,12alpha,24(S),27-pentolR-HSA-193780 (Reactome)
5beta-cholestan-3alpha,7alpha,12alpha,24(S)-tetrolArrowR-HSA-193774 (Reactome)
5beta-cholestan-3alpha,7alpha,12alpha,24(S)-tetrolArrowR-HSA-193781 (Reactome)
5beta-cholestan-3alpha,7alpha,12alpha,24(S)-tetrolR-HSA-193774 (Reactome)
5beta-cholestan-3alpha,7alpha,12alpha,24(S)-tetrolR-HSA-193787 (Reactome)
5beta-cholestan-3alpha,7alpha,12alpha,27-tetrolArrowR-HSA-193800 (Reactome)
5beta-cholestan-3alpha,7alpha,12alpha,27-tetrolR-HSA-193832 (Reactome)
5beta-cholestan-3alpha,7alpha,12alpha-triolArrowR-HSA-192036 (Reactome)
5beta-cholestan-3alpha,7alpha,12alpha-triolR-HSA-192010 (Reactome)
5beta-cholestan-3alpha,7alpha,24(S)-triolArrowR-HSA-193758 (Reactome)
5beta-cholestan-3alpha,7alpha,24(S)-triolR-HSA-193715 (Reactome)
5beta-cholestan-3alpha,7alpha,26-triolArrowR-HSA-193393 (Reactome)
5beta-cholestan-3alpha,7alpha,26-triolArrowR-HSA-193808 (Reactome)
5beta-cholestan-3alpha,7alpha,26-triolArrowR-HSA-193841 (Reactome)
5beta-cholestan-3alpha,7alpha,26-triolR-HSA-193497 (Reactome)
5beta-cholestan-3alpha,7alpha,26-triolR-HSA-193808 (Reactome)
5beta-cholestan-3alpha,7alpha-diolArrowR-HSA-192160 (Reactome)
5beta-cholestan-3alpha,7alpha-diolR-HSA-193537 (Reactome)
5beta-cholestan-7alpha,12alpha,24(S)-triol-3-oneArrowR-HSA-193755 (Reactome)
5beta-cholestan-7alpha,12alpha,24(S)-triol-3-oneR-HSA-193781 (Reactome)
5beta-cholestan-7alpha,12alpha,27-triol-3-oneArrowR-HSA-193821 (Reactome)
5beta-cholestan-7alpha,12alpha,27-triol-3-oneR-HSA-193800 (Reactome)
5beta-cholestan-7alpha,24(S)-diol-3-oneArrowR-HSA-193746 (Reactome)
5beta-cholestan-7alpha,24(S)-diol-3-oneR-HSA-193758 (Reactome)
5beta-cholestan-7alpha,27-diol-3-oneArrowR-HSA-193824 (Reactome)
5beta-cholestan-7alpha,27-diol-3-oneR-HSA-193841 (Reactome)
5beta-cholestan-7alpha-ol-3-oneArrowR-HSA-192033 (Reactome)
5beta-cholestan-7alpha-ol-3-oneR-HSA-192160 (Reactome)
5beta-cholesten-7alpha, 12alpha-diol-3-oneArrowR-HSA-192067 (Reactome)
5beta-cholesten-7alpha, 12alpha-diol-3-oneR-HSA-192036 (Reactome)
7 alpha-hydroxycholesterolArrowR-HSA-192051 (Reactome)
7 alpha-hydroxycholesterolR-HSA-192097 (Reactome)
ABCB11mim-catalysisR-HSA-193362 (Reactome)
ABCC3mim-catalysisR-HSA-194153 (Reactome)
ACOT8mim-catalysisR-HSA-193385 (Reactome)
ACOX2:FADmim-catalysisR-HSA-192335 (Reactome)
ACOX2:FADmim-catalysisR-HSA-193369 (Reactome)
ADPArrowR-HSA-193362 (Reactome)
ADPArrowR-HSA-194153 (Reactome)
AKR1D1mim-catalysisR-HSA-192033 (Reactome)
AKR1D1mim-catalysisR-HSA-192067 (Reactome)
AKR1D1mim-catalysisR-HSA-193746 (Reactome)
AKR1D1mim-catalysisR-HSA-193755 (Reactome)
AKR1D1mim-catalysisR-HSA-193821 (Reactome)
AKR1D1mim-catalysisR-HSA-193824 (Reactome)
ALB:(GCCA, TCCA)R-HSA-194079 (Reactome)
ALB:(GCCA, TCCA)R-HSA-194083 (Reactome)
ALBArrowR-HSA-194079 (Reactome)
ALBArrowR-HSA-194083 (Reactome)
ALBArrowR-HSA-194121 (Reactome)
ALBArrowR-HSA-194130 (Reactome)
ALBR-HSA-194153 (Reactome)
AMACRmim-catalysisR-HSA-192056 (Reactome)
AMACRmim-catalysisR-HSA-193452 (Reactome)
AMACRmim-catalysisR-HSA-193736 (Reactome)
AMACRmim-catalysisR-HSA-193763 (Reactome)
AMPArrowR-HSA-159425 (Reactome)
AMPArrowR-HSA-192137 (Reactome)
AMPArrowR-HSA-193401 (Reactome)
AMPArrowR-HSA-193407 (Reactome)
AMPArrowR-HSA-193424 (Reactome)
AMPArrowR-HSA-193711 (Reactome)
AMPArrowR-HSA-193727 (Reactome)
AMPArrowR-HSA-193743 (Reactome)
AMPArrowR-HSA-193766 (Reactome)
ATPR-HSA-159425 (Reactome)
ATPR-HSA-192137 (Reactome)
ATPR-HSA-193362 (Reactome)
ATPR-HSA-193401 (Reactome)
ATPR-HSA-193407 (Reactome)
ATPR-HSA-193424 (Reactome)
ATPR-HSA-193711 (Reactome)
ATPR-HSA-193727 (Reactome)
ATPR-HSA-193743 (Reactome)
ATPR-HSA-193766 (Reactome)
ATPR-HSA-194153 (Reactome)
Aldo-keto reductase familymim-catalysisR-HSA-192036 (Reactome)
Aldo-keto reductase familymim-catalysisR-HSA-192160 (Reactome)
Aldo-keto reductase familymim-catalysisR-HSA-193758 (Reactome)
Aldo-keto reductase familymim-catalysisR-HSA-193781 (Reactome)
Aldo-keto reductase familymim-catalysisR-HSA-193800 (Reactome)
Aldo-keto reductase familymim-catalysisR-HSA-193841 (Reactome)
BAATmim-catalysisR-HSA-159431 (Reactome)
BAATmim-catalysisR-HSA-192312 (Reactome)
BAATmim-catalysisR-HSA-193491 (Reactome)
CCAArrowR-HSA-193399 (Reactome)
CH25H (Fe2+ cofactor)mim-catalysisR-HSA-191983 (Reactome)
CHOL3b,7a,25TRIOLArrowR-HSA-192065 (Reactome)
CHOL7a,24(S)DIOLArrowR-HSA-192178 (Reactome)
CHOL7a,24(S)DIOLR-HSA-193789 (Reactome)
CHOLR-HSA-191983 (Reactome)
CHOLR-HSA-192051 (Reactome)
CHOLR-HSA-192061 (Reactome)
CHOLR-HSA-192123 (Reactome)
CYP27A1mim-catalysisR-HSA-191999 (Reactome)
CYP27A1mim-catalysisR-HSA-192042 (Reactome)
CYP27A1mim-catalysisR-HSA-192054 (Reactome)
CYP27A1mim-catalysisR-HSA-192123 (Reactome)
CYP27A1mim-catalysisR-HSA-193393 (Reactome)
CYP27A1mim-catalysisR-HSA-193460 (Reactome)
CYP27A1mim-catalysisR-HSA-193497 (Reactome)
CYP27A1mim-catalysisR-HSA-193713 (Reactome)
CYP27A1mim-catalysisR-HSA-193719 (Reactome)
CYP27A1mim-catalysisR-HSA-193737 (Reactome)
CYP27A1mim-catalysisR-HSA-193780 (Reactome)
CYP27A1mim-catalysisR-HSA-193787 (Reactome)
CYP27A1mim-catalysisR-HSA-193792 (Reactome)
CYP39A1mim-catalysisR-HSA-192178 (Reactome)
CYP46A1mim-catalysisR-HSA-192061 (Reactome)
Cholest-5-ene-3beta,7alpha,27-triolArrowR-HSA-191972 (Reactome)
Cholest-5-ene-3beta,7alpha,27-triolR-HSA-193816 (Reactome)
CoA-SHArrowR-HSA-159431 (Reactome)
CoA-SHArrowR-HSA-192312 (Reactome)
CoA-SHArrowR-HSA-193385 (Reactome)
CoA-SHArrowR-HSA-193491 (Reactome)
CoA-SHR-HSA-159425 (Reactome)
CoA-SHR-HSA-192137 (Reactome)
CoA-SHR-HSA-192341 (Reactome)
CoA-SHR-HSA-193401 (Reactome)
CoA-SHR-HSA-193407 (Reactome)
CoA-SHR-HSA-193424 (Reactome)
CoA-SHR-HSA-193533 (Reactome)
CoA-SHR-HSA-193711 (Reactome)
CoA-SHR-HSA-193727 (Reactome)
CoA-SHR-HSA-193743 (Reactome)
CoA-SHR-HSA-193766 (Reactome)
Cytochrome P450 (CYP7A1 based)mim-catalysisR-HSA-192051 (Reactome)
Cytochrome P450 (CYP7B1 based)mim-catalysisR-HSA-191972 (Reactome)
Cytochrome P450 (CYP7B1 based)mim-catalysisR-HSA-192065 (Reactome)
Cytochrome P450 (CYP8B1 based)mim-catalysisR-HSA-192157 (Reactome)
Cytochrome P450 (CYP8B1 based)mim-catalysisR-HSA-193709 (Reactome)
Cytochrome P450 (CYP8B1 based)mim-catalysisR-HSA-193845 (Reactome)
DCA,CDCA,LCHAR-HSA-5340195 (Reactome)
DCAR-HSA-8873850 (Reactome)
DHCAArrowR-HSA-193460 (Reactome)
DHCAArrowR-HSA-193519 (Reactome)
DHCAR-HSA-193407 (Reactome)
DHCAR-HSA-193424 (Reactome)
DHCAR-HSA-193519 (Reactome)
FABP6ArrowR-HSA-194153 (Reactome)
FABP6R-HSA-194187 (Reactome)
GCCA, TCCAArrowR-HSA-194079 (Reactome)
GCCA, TCCAArrowR-HSA-194083 (Reactome)
H+ArrowR-HSA-192042 (Reactome)
H+ArrowR-HSA-192097 (Reactome)
H+ArrowR-HSA-193455 (Reactome)
H+ArrowR-HSA-193497 (Reactome)
H+ArrowR-HSA-193508 (Reactome)
H+ArrowR-HSA-193789 (Reactome)
H+ArrowR-HSA-193816 (Reactome)
H+R-HSA-191972 (Reactome)
H+R-HSA-191983 (Reactome)
H+R-HSA-191999 (Reactome)
H+R-HSA-192033 (Reactome)
H+R-HSA-192036 (Reactome)
H+R-HSA-192051 (Reactome)
H+R-HSA-192054 (Reactome)
H+R-HSA-192061 (Reactome)
H+R-HSA-192065 (Reactome)
H+R-HSA-192067 (Reactome)
H+R-HSA-192123 (Reactome)
H+R-HSA-192157 (Reactome)
H+R-HSA-192160 (Reactome)
H+R-HSA-192178 (Reactome)
H+R-HSA-193393 (Reactome)
H+R-HSA-193460 (Reactome)
H+R-HSA-193709 (Reactome)
H+R-HSA-193713 (Reactome)
H+R-HSA-193719 (Reactome)
H+R-HSA-193737 (Reactome)
H+R-HSA-193746 (Reactome)
H+R-HSA-193755 (Reactome)
H+R-HSA-193758 (Reactome)
H+R-HSA-193780 (Reactome)
H+R-HSA-193781 (Reactome)
H+R-HSA-193787 (Reactome)
H+R-HSA-193792 (Reactome)
H+R-HSA-193800 (Reactome)
H+R-HSA-193821 (Reactome)
H+R-HSA-193824 (Reactome)
H+R-HSA-193841 (Reactome)
H+R-HSA-193845 (Reactome)
H2O2ArrowR-HSA-192335 (Reactome)
H2O2ArrowR-HSA-193369 (Reactome)
H2OArrowR-HSA-159425 (Reactome)
H2OArrowR-HSA-191972 (Reactome)
H2OArrowR-HSA-191983 (Reactome)
H2OArrowR-HSA-191999 (Reactome)
H2OArrowR-HSA-192051 (Reactome)
H2OArrowR-HSA-192054 (Reactome)
H2OArrowR-HSA-192061 (Reactome)
H2OArrowR-HSA-192065 (Reactome)
H2OArrowR-HSA-192123 (Reactome)
H2OArrowR-HSA-192157 (Reactome)
H2OArrowR-HSA-192178 (Reactome)
H2OArrowR-HSA-193393 (Reactome)
H2OArrowR-HSA-193460 (Reactome)
H2OArrowR-HSA-193709 (Reactome)
H2OArrowR-HSA-193711 (Reactome)
H2OArrowR-HSA-193713 (Reactome)
H2OArrowR-HSA-193719 (Reactome)
H2OArrowR-HSA-193727 (Reactome)
H2OArrowR-HSA-193737 (Reactome)
H2OArrowR-HSA-193743 (Reactome)
H2OArrowR-HSA-193766 (Reactome)
H2OArrowR-HSA-193780 (Reactome)
H2OArrowR-HSA-193787 (Reactome)
H2OArrowR-HSA-193792 (Reactome)
H2OArrowR-HSA-193845 (Reactome)
H2OR-HSA-192331 (Reactome)
H2OR-HSA-193362 (Reactome)
H2OR-HSA-193385 (Reactome)
H2OR-HSA-193535 (Reactome)
HSD17B4 dimermim-catalysisR-HSA-192331 (Reactome)
HSD17B4 dimermim-catalysisR-HSA-193455 (Reactome)
HSD17B4 dimermim-catalysisR-HSA-193508 (Reactome)
HSD17B4 dimermim-catalysisR-HSA-193535 (Reactome)
HSD3B7mim-catalysisR-HSA-192097 (Reactome)
HSD3B7mim-catalysisR-HSA-193789 (Reactome)
HSD3B7mim-catalysisR-HSA-193816 (Reactome)
LCAR-HSA-8873850 (Reactome)
NAD+R-HSA-192097 (Reactome)
NAD+R-HSA-193455 (Reactome)
NAD+R-HSA-193508 (Reactome)
NAD+R-HSA-193789 (Reactome)
NAD+R-HSA-193816 (Reactome)
NADHArrowR-HSA-192097 (Reactome)
NADHArrowR-HSA-193455 (Reactome)
NADHArrowR-HSA-193508 (Reactome)
NADHArrowR-HSA-193789 (Reactome)
NADHArrowR-HSA-193816 (Reactome)
NADP+ArrowR-HSA-191972 (Reactome)
NADP+ArrowR-HSA-191983 (Reactome)
NADP+ArrowR-HSA-191999 (Reactome)
NADP+ArrowR-HSA-192033 (Reactome)
NADP+ArrowR-HSA-192036 (Reactome)
NADP+ArrowR-HSA-192051 (Reactome)
NADP+ArrowR-HSA-192054 (Reactome)
NADP+ArrowR-HSA-192061 (Reactome)
NADP+ArrowR-HSA-192065 (Reactome)
NADP+ArrowR-HSA-192067 (Reactome)
NADP+ArrowR-HSA-192123 (Reactome)
NADP+ArrowR-HSA-192157 (Reactome)
NADP+ArrowR-HSA-192160 (Reactome)
NADP+ArrowR-HSA-192178 (Reactome)
NADP+ArrowR-HSA-193393 (Reactome)
NADP+ArrowR-HSA-193460 (Reactome)
NADP+ArrowR-HSA-193709 (Reactome)
NADP+ArrowR-HSA-193713 (Reactome)
NADP+ArrowR-HSA-193719 (Reactome)
NADP+ArrowR-HSA-193737 (Reactome)
NADP+ArrowR-HSA-193746 (Reactome)
NADP+ArrowR-HSA-193755 (Reactome)
NADP+ArrowR-HSA-193758 (Reactome)
NADP+ArrowR-HSA-193780 (Reactome)
NADP+ArrowR-HSA-193781 (Reactome)
NADP+ArrowR-HSA-193787 (Reactome)
NADP+ArrowR-HSA-193792 (Reactome)
NADP+ArrowR-HSA-193800 (Reactome)
NADP+ArrowR-HSA-193821 (Reactome)
NADP+ArrowR-HSA-193824 (Reactome)
NADP+ArrowR-HSA-193841 (Reactome)
NADP+ArrowR-HSA-193845 (Reactome)
NADP+R-HSA-192042 (Reactome)
NADP+R-HSA-193497 (Reactome)
NADPHArrowR-HSA-192042 (Reactome)
NADPHArrowR-HSA-193497 (Reactome)
NADPHR-HSA-191972 (Reactome)
NADPHR-HSA-191983 (Reactome)
NADPHR-HSA-191999 (Reactome)
NADPHR-HSA-192033 (Reactome)
NADPHR-HSA-192036 (Reactome)
NADPHR-HSA-192051 (Reactome)
NADPHR-HSA-192054 (Reactome)
NADPHR-HSA-192061 (Reactome)
NADPHR-HSA-192065 (Reactome)
NADPHR-HSA-192067 (Reactome)
NADPHR-HSA-192123 (Reactome)
NADPHR-HSA-192157 (Reactome)
NADPHR-HSA-192160 (Reactome)
NADPHR-HSA-192178 (Reactome)
NADPHR-HSA-193393 (Reactome)
NADPHR-HSA-193460 (Reactome)
NADPHR-HSA-193709 (Reactome)
NADPHR-HSA-193713 (Reactome)
NADPHR-HSA-193719 (Reactome)
NADPHR-HSA-193737 (Reactome)
NADPHR-HSA-193746 (Reactome)
NADPHR-HSA-193755 (Reactome)
NADPHR-HSA-193758 (Reactome)
NADPHR-HSA-193780 (Reactome)
NADPHR-HSA-193781 (Reactome)
NADPHR-HSA-193787 (Reactome)
NADPHR-HSA-193792 (Reactome)
NADPHR-HSA-193800 (Reactome)
NADPHR-HSA-193821 (Reactome)
NADPHR-HSA-193824 (Reactome)
NADPHR-HSA-193841 (Reactome)
NADPHR-HSA-193845 (Reactome)
NCOA1,2:RXRA:NR1H4:DCA,CDCA,LCHAArrowR-HSA-194187 (Reactome)
NCOA1,2:RXRA:NR1H4:DCA,CDCA,LCHAArrowR-HSA-5340251 (Reactome)
NCOA1,2:RXRA:NR1H4:DCA,CDCA,LCHATBarR-HSA-191972 (Reactome)
NCOA1,2:RXRA:NR1H4:DCA,CDCA,LCHATBarR-HSA-192051 (Reactome)
NCOA1,2:RXRA:NR1H4:DCA,CDCA,LCHATBarR-HSA-192065 (Reactome)
NCOA1R-HSA-5340251 (Reactome)
NCOA2R-HSA-5340251 (Reactome)
NR1H4:DCA,CDCA,LCHAArrowR-HSA-5340195 (Reactome)
NR1H4:DCA,CDCA,LCHAR-HSA-5340251 (Reactome)
NR1H4R-HSA-5340195 (Reactome)
Na+ArrowR-HSA-194121 (Reactome)
Na+ArrowR-HSA-194187 (Reactome)
Na+R-HSA-194121 (Reactome)
Na+R-HSA-194187 (Reactome)
O2R-HSA-191972 (Reactome)
O2R-HSA-191983 (Reactome)
O2R-HSA-191999 (Reactome)
O2R-HSA-192051 (Reactome)
O2R-HSA-192054 (Reactome)
O2R-HSA-192061 (Reactome)
O2R-HSA-192065 (Reactome)
O2R-HSA-192123 (Reactome)
O2R-HSA-192157 (Reactome)
O2R-HSA-192178 (Reactome)
O2R-HSA-192335 (Reactome)
O2R-HSA-193369 (Reactome)
O2R-HSA-193393 (Reactome)
O2R-HSA-193460 (Reactome)
O2R-HSA-193709 (Reactome)
O2R-HSA-193713 (Reactome)
O2R-HSA-193719 (Reactome)
O2R-HSA-193737 (Reactome)
O2R-HSA-193780 (Reactome)
O2R-HSA-193787 (Reactome)
O2R-HSA-193792 (Reactome)
O2R-HSA-193845 (Reactome)
OSBPmim-catalysisR-HSA-8868402 (Reactome)
OSBPsmim-catalysisR-HSA-8867667 (Reactome)
PI4PArrowR-HSA-8868402 (Reactome)
PI4PR-HSA-8868402 (Reactome)
PPiArrowR-HSA-159425 (Reactome)
PPiArrowR-HSA-192137 (Reactome)
PPiArrowR-HSA-193401 (Reactome)
PPiArrowR-HSA-193407 (Reactome)
PPiArrowR-HSA-193424 (Reactome)
PPiArrowR-HSA-193711 (Reactome)
PPiArrowR-HSA-193727 (Reactome)
PPiArrowR-HSA-193743 (Reactome)
PPiArrowR-HSA-193766 (Reactome)
PiArrowR-HSA-193362 (Reactome)
PiArrowR-HSA-194153 (Reactome)
R-HSA-159425 (Reactome) Cholate or chenodeoxycholate, coenzyme A, and ATP react to form their CoA conjugates, AMP, pyrophosphate and water. This reaction is catalyzed by SLC27A5 (BACS) associated with the endoplasmic reticulum membrane, but the substrates and products are cytosolic (Mihalik et al. 2002).
R-HSA-159431 (Reactome) Cytosolic bile acid-CoA conjugates (choloyl-CoA; chenodeoxycholoyl-CoA) react with the amino acids glycine and taurine, generating the corresponding bile salts and coenzyme A, catalyzed by BAAT (bile acid-CoA:amino acid N-acetyltransferase). In the body, this reaction occurs in hepatocytes and is the means by which bile acids recovered from the intestine are converted to bile salts before being released again into the bile (Kullak-Ublick et al. 2004; Trauner and Boyer 2002).
R-HSA-191971 (Reactome) THCA (3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoate) is translocated from the mitochondrial matrix to the cytosol. The transporter that mediates its passage across the inner mitochondrial membrane has not been identified. In particular, despite the structural and functional similarities between THCA and long chain fatty acids, searches for carnitine - THCA have failed (Russell 2003). VLCS (SLC27A2), one of the enzymes that catalyzes CoA conjugation of THCA may also be present in peroxisomes, and Mihalik et al. (2002) have hypothesized that THCA could be translocated unchanged from the mitochondrial matrix to the peroxisomal matrix and undergo conjugation there.
R-HSA-191972 (Reactome) 27-hydroxycholesterol, NADPH + H+, and O2 react to form cholest-5-ene-3beta,7alpha,27-triol, H2O, and NADP+. This reaction is catalyzed by CYP7B1 in the endoplasmic reticulum membrane. Defects in CYB7B1 are associated with failure of 7alpha-hydroxylation in vivo, and with liver damage, confirming both the function of the enzyme and the central role of the liver in this metabolic process (Setchell et al. 1998).
R-HSA-191983 (Reactome) The microsomal enzyme cholesterol 25-hydroxylase is a member of a lipid metabolizing enzyme family that utilizes oxygen and diiron-oxygen cofactor to hydroxylate, desaturate, epoxidate and acetylate substrates.
R-HSA-191999 (Reactome) CYP27A1, a mitochondrial matrix sterol hydroxylase, catalyses the 27-hydroxylation of side-chains of sterol intermediates (Cali et al. 1991). A specific reaction is the 27-hydroxylation of 5beta-cholestan-3alpha, 7alpha, 12alpha-triol (5bCHOL3a,7a,12a-triol) to form 5beta-cholestan-3alpha, 7alpha, 12alpha, 27-tetrol (5bCHOL3a,7a,12a, 27-tetrol) (Pikuleva et al. 1998). Defects in CYP27A1 can cause Cerebrotendinous xanthomatosis (CTX; MIM:213700), a rare sterol storage disorder characterised by progressive neurologic dysfunction, premature atherosclerosis and cataracts (Cali et al. 1991b).
R-HSA-192010 (Reactome) 5beta-cholestan-3alpha,7alpha,12alpha-triol is translocated from the cytosol to the mitochondrial matrix. The transporter that mediates its passage across the inner mitochondrial membrane is unknown: the StAR protein that performs this function for cholesterol at the start of steroid hormone biosynthesis is excluded as StAR is not expressed in liver. Other members of the START family of transporters are candidates, however (Russell 2003).
R-HSA-192033 (Reactome) 4-Cholesten-7alpha-ol-3-one, NADPH, and H+ react to form 5beta-cholestan-7alpha-ol-3-one and NADP+. This reaction is catalyzed by AKR1D1 (3-oxo-5-beta-steroid 4-dehydrogenase). AKR1D1 is localized to the cytosol, and in the course of the reaction its steroid substrate moves from the endoplasmic reticulum membrane to the cytosol. It is unclear whether this translocation results simply from its increased hydrophilicity or is mediated by the enzyme or another transport protein (Russell 2003).
R-HSA-192036 (Reactome) 5Beta-cholesten-7alpha,12alpha-diol-3-one and NADPH + H+ form 5beta-cholestan-3alpha,7alpha,12alpha-triol and NAPDP+. The reaction is catalyzed by 3alpha-hydroxysteroid dehydrogenase (AKR1C4), a cytosolic enzyme belonging to the aldo-keto reductase family (Dufort et al. 2001). Biochemical studies with rat proteins raise the possibility that other related enzymes may also carry out this reaction in vivo (Russell 2003).
R-HSA-192042 (Reactome) 5beta-cholestan-3alpha, 7alpha, 12alpha, 27-tetrol and NADP+ react to form 3alpha, 7alpha, 12alpha-trihydroxy-5beta-cholestan-27-al and NADPH + H+. This oxidation reaction occurs in the mitochondrial matrix, catalyzed by CYP27A1.
R-HSA-192051 (Reactome) Cholesterol, NADPH + H+, and O2 form 7alpha-cholesterol (5-cholesten-3beta, 7alpha-diol), NADP+,and H2O, in a reaction catalysed by CYP7A1 (cholesterol 7alpha-hydroylase) in the endoplasmic reticulum membrane. In the body, this enzyme is expressed only in liver, and its expression is tightly regulated at the level of transcription to determine the overall rate of bile acid and bile salt production (Noshiro et al. 1990).
R-HSA-192054 (Reactome) 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-27-al, NADPH + H+, and O2 react to form 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoate (THCA), NADP+, and H2O. This oxidation reaction occurs in the mitochondrial matrix, catalyzed by CYP27A1.
R-HSA-192056 (Reactome) The isomerization of 25(R) THCA-CoA to 25(S) THCA-CoA, catalyzed by 2-methylacyl-CoA racemase, occurs in the peroxisomal matrix.
R-HSA-192061 (Reactome) Cholesterol 24-hydroxylase (CYP46A1), an enzyme associated with the ER membrane, catalyses the 24-hydroxylation of cholesterol (CHOL) to 24-hydroxycholesterol (24OH-CHOL). In the body, this enzyme is expressed predominantly in the brain and is thought to play a major role in cholesterol turnover there (Lund et al. 1999, Mast et al. 2003).
R-HSA-192065 (Reactome) 25-hydroxycholesterol (25OH-CHOL) is 7alpha-hydroxylated to cholest-5-ene-3beta,7alpha,25-triol (CHOL3b,7a,25TRIOL) by CYP7B1 (cytochrome P450 7B1) (Wu et al. 1999).
R-HSA-192067 (Reactome) 4-Cholesten-7alpha, 12alpha-diol-3-one and NADPH + H+ react to form 5beta-cholesten-7alpha,12alpha-diol-3-one + NADP+. This reaction is catalyzed by AKR1D1 (3-oxo-5-beta-steroid 4-dehydrogenase). AKR1D1 is localized to the cytosol, and in the course of the reaction its steroid substrate moves from the endoplasmic reticulum membrane to the cytosol. It is unclear whether this translocation results simply from its increased hydrophilicity or is mediated by the enzyme or another transport protein (Russell 2003).
R-HSA-192097 (Reactome) 7alpha-hydroxycholesterol and NAD+ react to form 4-cholesten-7alpha-ol-3-one, NADH, and H+, in a reaction catalyzed by HSD3B7 (3 beta-hydroxysteroid dehydrogenase type 7) in the endoplasmic reticulum membrane. Its function in vivo has been confirmed in studies of patients with defects in bile acid synthesis (Schwarz et al. 2000).
R-HSA-192123 (Reactome) Cholesterol CHOL), NADPH + H+, and O2 react to form 27-hydroxycholesterol (27OH-CHOL), H2O, and NADP+, in the mitochondrial matrix, catalysed by CYP27A1. 27OH-CHOL is the most abundant oxysterol in human plasma. Its formation is thought to play a central role in the mobilization of CHOL from non-hepatic tissues (Cali et al. 1991).
R-HSA-192137 (Reactome) THCA (25(R) 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoate) , coenzyme A, and ATP react to form the CoA conjugate of 25(R) THCA, AMP, and pyrophosphate. This cytosolic reaction is catalyzed by SLC27A5 (BACS). SLC27A2 (VLCS) also catalyzes this reaction; the relative contributions of the two enzymes to de novo bile acid synthesis in vivo are not certain (Mihalik et al. 2002).
R-HSA-192157 (Reactome) Sterol 12alpha hydroxylase (CYP8B1), an enzyme associated with the endoplasmic reticulum membrane, catalyses the 12-alpha-hydroxylation of 7-Alpha-hydroxycholest-4-en-3-one (4CHOL7aOLONE) to 7-alpha,12-alpha-dihydroxycholest-4-en-3-one (4CHOL7a,12aDONE). While the human gene has been cloned (Gafvels et al. 1999), its protein product has not been characterised, and the enzymatic properties of human CYP8B1 protein are inferred from those of its well-characterised rabbit homolog (Ishida et al. 1992).
R-HSA-192160 (Reactome) 5Beta-cholesten-7alpha-ol-3-one and NADPH + H+ form 5beta-cholestan-3alpha,7alpha-diol and NAPDP+. The reaction is catalyzed by 3alpha-hydroxysteroid dehydrogenase (AKR1C4), a cytosolic enzyme belonging to the aldo-keto reductase family (Dufort et al. 2001). Biochemical studies with rat proteins raise the possibility that other related enzymes may also carry out this reaction in vivo (Russell 2003).
R-HSA-192178 (Reactome) 24-hydroxycholesterol 7-alpha-hydroxylase (CYP39A1), located on the ER membrane, 7-alpha-hydroxylates 24-hydroxycholesterol (24OH-CHOL) to cholest-5-ene-3beta,7alpha,24-triol (CHOL7a,24(S)DIOL). In the body, expression of CYP39A1 is restricted to the liver and is involved in bile acid metabolism (Li-Hawkins et al. 2000).
R-HSA-192312 (Reactome) Choloyl CoA reacts with glycine or taurine to form glycocholate or taurocholate, releasing CoASH. This reaction, which completes the de novo synthesis of bile salts from cholesterol in vivo, is catalyzed by BAAT (Bile acid CoA:amino acid N-acyltransferase - Falany et al. 1994) and occurs in the peroxisomal matrix (Solaas et al. 2000; Mihalik et al. 2002). In vivo, the relative amounts of glycocholate and taurocholate synthesized appear to be determined solely by the intracellular abundances of glycine and taurine (Russell 2003).
R-HSA-192315 (Reactome) The bile salts glycocholate, glycochenodeoxycholate, taurocholate, and taurochenodeoxycholate are translocated from the peroxisomal matrix to the cytosol. The transporter that mediates this process is unknown (Russell 2003).
R-HSA-192325 (Reactome) 25(R) THCA-CoA is transported from the cytosol into the peroxisome. Indirect evidence suggests that a member of the ABC class of transporters mediates this reaction.
R-HSA-192331 (Reactome) 3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA (THCA-CoA) is hydrated to form (24R, 25R) 3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA. This reaction, catalyzed by the peroxisomal D-bifunctional enzyme (Huyghe et al. 2006), occurs in the peroxisomal matrix.
R-HSA-192335 (Reactome) 25(S) THCA-CoA and O2 react to form 3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-enoyl-CoA (THCA-CoA) and H2O2. This dehydrogenation reaction occurs in the peroxisomal matrix. It is catalyzed by the FAD-containing peroxisomal enzyme branched chain acyl-CoA oxidase (ACOX2). The enzyme transfers electrons to molecular oxygen and hydrogen peroxide is produced as a byproduct.
R-HSA-192341 (Reactome) 3alpha,7alpha,12alpha-trihydroxy-5beta-cholan-24-one-CoA and CoASH react to form choloyl-CoA (3alpha,7alpha,12alpha-trihydroxy-5beta-cholan-24-one-CoA) and propionyl CoA. This reaction, in the peroxisomal matrix, is catalyzed by peroxisomal thiolase 2 (sterol carrier protein 2).
R-HSA-193362 (Reactome) A molecule of glycocholate, glycochenodeoxycholate, taurocholate, or taurochenodeoxycholate is transported from the cytosol to the extracellular space, coupled to the hydrolysis of a molecule of cytosolic ATP to ADP and orthophosphate. This reaction is mediated by ABCB11 (bile salt export pump). In the body, this reaction mediates the release of bile salts from the liver cells into the bile (Kullak-Ublick et al. 2004); the role of ABCB11 in the reaction is confirmed by the observed failure of bile salt export in patients in whom the transporter is defective (Noe et al. 2005).
R-HSA-193369 (Reactome) 25(S) DHCA-CoA and O2 react to form 25(S) 3alpha,7alpha-dihydroxy-5beta-cholest-24-enoyl-CoA and H2O2. This dehydrogenation reaction occurs in the peroxisomal matrix. It is catalyzed by the FAD-containing peroxisomal enzyme branched chain acyl-CoA oxidase (ACOX2). The enzyme transfers electrons to molecular oxygen and hydrogen peroxide is produced as a byproduct.
R-HSA-193385 (Reactome) Choloyl-CoA and water react to form cholate and CoASH. This reaction, catalyzed by acyl-coenzyme A thioesterase 8, occurs in the peroxisomal matrix (Jones et al. 1999; Hunt et al. 2002). While bile salts are the major product of the de novo biosynthetic pathway in the normal human liver, bile acids are major feedback regulators of this pathway and this hydrolysis reaction is thought to play a role in generating them (Russell 2003).
R-HSA-193393 (Reactome) 5beta-cholestan-3alpha, 7alpha-diol, NADPH + H+, and O2 react to form 5beta-cholestan-3alpha, 7alpha, 26-triol + NADP+ + H2O. This reaction occurs in the mitochondrial matrix, catalyzed by CYP27A1.
R-HSA-193399 (Reactome) Cholate is translocated from the peroxisomal matrix to the cytosol. The transporter that mediates this event is unknown.
R-HSA-193401 (Reactome) THCA (25(R) 3alpha,7alpha,12alpha-trihydroxy-5beta-cholestanoate), coenzyme A, and ATP react to form the CoA conjugate of 25(R) THCA, AMP, and pyrophosphate. This cytosolic reaction is catalyzed by SLC27A2 (VLCS). SLC27A5 (BACS) also catalyzes this reaction; the relative contributions of the two enzymes to de novo bile acid synthesis in vivo are not certain (Mihalik et al. 2002).
R-HSA-193407 (Reactome) DHCA (25(R) 3alpha,7alpha-dihydroxy-5beta-cholestanoate) , coenzyme A, and ATP react to form the CoA conjugate of 25(R) DHCA, AMP, and pyrophosphate. This cytosolic reaction is catalyzed by SLC27A5 (BACS). SLC27A2 (VLCS) also catalyzes this reaction; the relative contributions of the two enzymes to de novo bile acid synthesis in vivo are not certain (Mihalik et al. 2002).
R-HSA-193424 (Reactome) DHCA (25(R) 3alpha,7alpha-dihydroxy-5beta-cholestanoate), coenzyme A, and ATP react to form the CoA conjugate of 25(R) DHCA, AMP, and pyrophosphate. This cytosolic reaction is catalyzed by SLC27A2 (VLCS). SLC27A5 (BACS) also catalyzes this reaction; the relative contributions of the two enzymes to de novo bile acid synthesis in vivo are not certain (Mihalik et al. 2002).
R-HSA-193452 (Reactome) The isomerization of 25(R) DHCA-CoA to 25(S) DHCA-CoA, catalyzed by 2-methylacyl-CoA racemase, occurs in the peroxisomal matrix.
R-HSA-193455 (Reactome) (24R, 25R) 3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA and NAD+ react to form 3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-one-CoA, NADH, and H+. This oxidation reaction, catalyzed by the peroxisomal D-bifunctional enzyme (Huyghe et al. 2006), occurs in the peroxisomal matrix.
R-HSA-193460 (Reactome) 3alpha, 7alpha-dihydroxy-5beta-cholestan-26-al, NADPH + H+, and O2 react to form 3alpha, 7alpha-dihydroxy-5beta-cholestanoate (DHCA), NADP+ and H2O. This oxidation reaction occurs in the mitochondrial matrix, catalyzed by CYP27A1.
R-HSA-193482 (Reactome) 25(R) DHCA-CoA is transported from the cytosol into the peroxisome. Indirect evidence suggests that a member of the ABC class of transporters mediates this reaction.
R-HSA-193491 (Reactome) Chenodeoxycholoyl CoA reacts with glycine or taurine to form glycochenodeoxycholate or taurochenodeoxycholate, releasing CoASH. This reaction, which completes the de novo synthesis of bile salts from cholesterol in vivo, is catalyzed by BAAT (Bile acid CoA:amino acid N-acyltransferase - Falany et al. 1994) and occurs in the peroxisomal matrix (Solaas et al. 2000; Mihalik et al. 2002). In vivo, the relative amounts of glycochenodeoxycholate and taurochenodeoxycholate synthesized appear to be determined solely by the intracellular abundances of glycine and taurine (Russell 2003).
R-HSA-193497 (Reactome) 5beta-cholestan-3alpha, 7alpha, 26-triol and NADP+ react to form 3alpha, 7alpha-dihydroxy-5beta-cholestan-26-al and NADPH + H+. This oxidation reaction occurs in the mitochondrial matrix, catalyzed by CYP27A1.
R-HSA-193508 (Reactome) (24R, 25R) 3alpha,7alpha,24-trihydroxy-5beta-cholestanoyl-CoA and NAD+ react to form 3alpha,7alpha-dihydroxy-5beta-cholest-24-one-CoA, NADH, and H+. This oxidation reaction, catalyzed by the peroxisomal D-bifunctional enzyme (Huyghe et al. 2006), occurs in the peroxisomal matrix.
R-HSA-193519 (Reactome) DHCA (3alpha, 7alpha-dihydroxy-5beta-cholestanoate) is translocated from the mitochondrial matrix to the cytosol. The transporter that mediates its passage across the inner mitochondrial membrane has not been identified. In particular, despite the structural and functional similarities between DHCA and long chain fatty acids, searches for carnitine - DHCA have failed (Russell 2003). VLCS (SLC27A2), one of the enzymes that catalyzes CoA conjugation of DHCA, may also be present in peroxisomes, and Mihalik et al. (2002) have hypothesized that DHCA could be translocated unchanged from the mitochondrial matrix to the peroxisomal matrix and undergo conjugation there.
R-HSA-193533 (Reactome) 3alpha,7alpha-dihydroxy-5beta-cholan-24-one-CoA and CoASH react to form chenodeoxycholoyl-CoA (3alpha,7alpha-dihydroxy-5beta-cholan-24-one-CoA) and propionyl CoA. This reaction, in the peroxisomal matrix, is catalyzed by peroxisomal thiolase 2 (sterol carrier protein 2).
R-HSA-193535 (Reactome) 25(S) 3alpha,7alpha-dihydroxy-5beta-cholest-24-enoyl-CoA is hydrated to form (24R, 25R) 3alpha,7alpha,24-trihydroxy-5beta-cholestanoyl-CoA. This reaction, catalyzed by the peroxisomal D-bifunctional enzyme (Huyghe et al. 2006), occurs in the peroxisomal matrix.
R-HSA-193537 (Reactome) 5beta-cholestan-3alpha, 7alpha-diol is transported from the cytosol to the mitochondrial matrix. The transporter that mediates its passage across the inner mitochondrial membrane is unknown: the StAR protein that performs this function for cholesterol at the start of steroid hormone biosynthesis is excluded as StAR is not expressed in liver. Other members of the START family of transporters are candidates, however (Russell 2003).
R-HSA-193709 (Reactome) Sterol 12alpha hydroxylase (CYP8B1) catalyses the 12-alpha-hydroxylation of 4-cholesten-7alpha,24(S)-diol-3-one (4CHOL7a,24(S)DONE) to 4-cholesten-7-alpha,12-alpha,24(S)-triol-3-one (4CHOL7a,12a,24(S)TONE). While the human gene has been cloned (Gafvels et al. 1999), its protein product has not been characterised, and the enzymatic properties of human CYP8B1 protein are inferred from those of its well-characterised rabbit homolog (Ishida et al. 1992).
R-HSA-193711 (Reactome) 3,7,24THCA (25(R) 3alpha,7alpha,24(S)-trihydroxy-5beta-cholestanoate), coenzyme A, and ATP react to form the CoA conjugate of 3,7,24THCA, AMP, pyrophosphate and water. This cytosolic reaction is catalyzed by SLC27A5 (BACS). SLC27A2 (VLCS) also catalyzes this reaction; the relative contributions of the two enzymes to de novo bile acid synthesis in vivo are not certain (Mihalik et al. 2002).
R-HSA-193713 (Reactome) 3alpha,7alpha,12alpha,24(S)-tetrahydroxy-5beta-cholestan-27-al, NADPH + H+, and O2 react to form 3alpha,7alpha,12alpha,24(S)-tetrahydroxy-5beta-cholestanoate (TetraHCA), NADP+, and H2O. This oxidation reaction occurs in the mitochondrial matrix, catalyzed by CYP27A1.
R-HSA-193715 (Reactome) 5beta-cholestan-3alpha,7alpha,24(S)-triol is transported from the cytosol to the mitochondrial matrix. The transporter that mediates its passage across the inner mitochondrial membrane is unknown: the StAR protein that performs this function for cholesterol at the start of steroid hormone biosynthesis is excluded as StAR is not expressed in liver. Other members of the START family of transporters are candidates, however (Russell 2003).
R-HSA-193719 (Reactome) 5beta-cholestan-3alpha,7alpha,24(S),27-tetrol, NADPH + H+, and O2 react to form 3alpha,7alpha,24(S)-trihydroxy-5beta-cholestan-27-al, NADP+, and H2O. This oxidation reaction occurs in the mitochondrial matrix, catalyzed by CYP27A1.
R-HSA-193722 (Reactome) TetraHCA (3alpha,7alpha,12alpha,24(S)-tetrahydroxy-5beta-cholestanoate) is translocated from the mitochondrial matrix to the cytosol. The transporter that mediates its passage across the inner mitochondrial membrane has not been identified (Russell 2003). VLCS (SLC27A2), one of the enzymes that catalyzes CoA conjugation of TetraHCA, may also be present in peroxisomes, and Mihalik et al. (2002) have hypothesized that TetraHCA could be translocated unchanged from the mitochondrial matrix to the peroxisomal matrix and undergo conjugation there.
R-HSA-193727 (Reactome) TetraHCA (25(R) 3alpha,7alpha,12alpha,24(S)-tetrahydroxy-5beta-cholestanoate), coenzyme A, and ATP react to form the CoA conjugate of 25(R) TetraHCA, AMP, pyrophosphate and water. This cytosolic reaction is catalyzed by SLC27A2 (VLCS). SLC27A5 (BACS) also catalyzes this reaction; the relative contributions of the two enzymes to de novo bile acid synthesis in vivo are not certain (Mihalik et al. 2002).
R-HSA-193736 (Reactome) The isomerization of 3,7,24THCA-CoA to (24R, 25R) 3alpha,7alpha,24-trihydroxy-5beta-cholestanoyl-CoA, catalyzed by 2-methylacyl-CoA racemase, occurs in the peroxisomal matrix.
R-HSA-193737 (Reactome) 3alpha,7alpha,24(S)-trihydroxy-5beta-cholestan-27-al, NADPH + H+, and O2 react to form 3alpha,7alpha,24(S)-trihydroxy-5beta-cholestanoate (3,7,24THCA), NADP+, and H2O. This oxidation reaction occurs in the mitochondrial matrix, catalyzed by CYP27A1.
R-HSA-193743 (Reactome) 3,7,24THCA (25(R) 3alpha,7alpha,24(S)-trihydroxy-5beta-cholestanoate), coenzyme A, and ATP react to form the CoA conjugate of 3,7,24THCA, AMP, pyrophosphate and water. This cytosolic reaction is catalyzed by SLC27A2 (VLCS). SLC27A5 (BACS) also catalyzes this reaction; the relative contributions of the two enzymes to de novo bile acid synthesis in vivo are not certain (Mihalik et al. 2002).
R-HSA-193746 (Reactome) 4-Cholesten-7alpha,24(S)-diol-3-one, NADPH, and H+ react to form 5beta-cholestan-7alpha,24(S)-diol-3-one and NADP+. This reaction is catalyzed by AKR1D1 (3-oxo-5-beta-steroid 4-dehydrogenase). AKR1D1 is localized to the cytosol, and in the course of the reaction its steroid substrate moves from the endoplasmic reticulum membrane to the cytosol. It is unclear whether this translocation results simply from its increased hydrophilicity or is mediated by the enzyme or another transport protein (Russell 2003).
R-HSA-193753 (Reactome) 3,7,24THCA-CoA is transported from the cytosol into the peroxisome.
R-HSA-193755 (Reactome) 4-cholesten-7alpha,12alpha,24(S)-triol-3-one and NADPH + H+ react to form 5beta-cholesten-7alpha,12alpha,24(S)-triol-3-one and NADP+. This reaction is catalyzed by AKR1D1 (3-oxo-5-beta-steroid 4-dehydrogenase). AKR1D1 is localized to the cytosol, and in the course of the reaction its steroid substrate moves from the endoplasmic reticulum membrane to the cytosol. It is unclear whether this translocation results simply from its increased hydrophilicity or is mediated by the enzyme or another transport protein (Russell 2003).
R-HSA-193758 (Reactome) 5Beta-cholesten-7alpha,24(S)-diol-3-one and NADPH + H+ form 5beta-cholestan-3alpha,7alpha,24(S)-triol and NAPDP+. The reaction is catalyzed by 3alpha-hydroxysteroid dehydrogenase (AKR1C4), a cytosolic enzyme belonging to the aldo-keto reductase family (Dufort et al. 2001). Biochemical studies with rat proteins raise the possibility that other related enzymes may also carry out this reaction in vivo (Russell 2003).
R-HSA-193761 (Reactome) 25(R) TetraHCA-CoA is transported from the cytosol into the peroxisome.
R-HSA-193763 (Reactome) The isomerization of 25(R) TetraHCA-CoA to (24R, 25R) 3alpha,7alpha,12alpha,24-tetrahydroxy-5beta-cholestanoyl-CoA, catalyzed by 2-methylacyl-CoA racemase, occurs in the peroxisomal matrix.
R-HSA-193766 (Reactome) TetraHCA (25(R) 3alpha,7alpha,12alpha,24(S)-tetrahydroxy-5beta-cholestanoate), coenzyme A, and ATP react to form the CoA conjugate of 25(R) TetraHCA, AMP, pyrophosphate and water. This cytosolic reaction is catalyzed by SLC27A5 (BACS). SLC27A2 (VLCS) also catalyzes this reaction; the relative contributions of the two enzymes to de novo bile acid synthesis in vivo are not certain (Mihalik et al. 2002).
R-HSA-193767 (Reactome) 24-hydroxycholesterol is transported from the extracellular space to the endoplasmic reticulum. In humans, this event is the means by which the molecule, generated from cholesterol in the brain, is taken up by liver cells for conversion to bile acids and bile salts. While transport proteins are likely to play a role in this process, these proteins have not been identified (Lutjohann et al. 1996; Bjorkhem et al. 1998).
R-HSA-193774 (Reactome) 5beta-cholestan-3alpha,7alpha,12alpha,24(S)-tetrol is translocated from the cytosol to the mitochondrial matrix. The transporter that mediates its passage across the inner mitochondrial membrane is unknown: the StAR protein that performs this function for cholesterol at the start of steroid hormone biosynthesis is excluded as StAR is not expressed in liver. Other members of the START family of transporters are candidates, however (Russell 2003).
R-HSA-193776 (Reactome) 24-hydroxycholesterol is transported from the endoplasmic reticulum to the extracellular space. In humans, this event is the major source of 24-hydroxycholesterol in the blood and is the means by which the molecule, generated from cholesterol in the brain, is transported to the liver for conversion to bile acids and bile salts. While transport proteins are likely to play a role in this process, and the 24-hydroxycholesterol is likely to occur as part of a lipoprotein complex in the blood, the relevant proteins have not been identified (Lutjohann et al. 1996; Bjorkhem et al. 1998).
R-HSA-193780 (Reactome) 5beta-cholestan-3alpha,7alpha,12alpha,24(S),27-pentol, NADPH + H+, and O2 react to form 3alpha,7alpha,12alpha,24(S)-tetrahydroxy-5beta-cholestan-27-al, NADP+, and H2O. This oxidation reaction occurs in the mitochondrial matrix, catalyzed by CYP27A1.
R-HSA-193781 (Reactome) 5Beta-cholesten-7alpha,12alpha,24(S)-triol-3-one and NADPH + H+ form 5beta-cholestan-3alpha,7alpha,12alpha,24(S)-tetrol and NAPDP+. The reaction is catalyzed by 3alpha-hydroxysteroid dehydrogenase (AKR1C4), a cytosolic enzyme belonging to the aldo-keto reductase family (Dufort et al. 2001). Biochemical studies with rat proteins raise the possibility that other related enzymes may also carry out this reaction in vivo (Russell 2003).
R-HSA-193786 (Reactome) 3,7,24THCA (3alpha,7alpha,24(S)-trihydroxy-5beta-cholestanoate) is translocated from the mitochondrial matrix to the cytosol. The transporter that mediates its passage across the inner mitochondrial membrane has not been identified (Russell 2003). VLCS (SLC27A2), one of the enzymes that catalyzes CoA conjugation of 3,7,24THCA, may also be present in peroxisomes, and Mihalik et al. (2002) have hypothesized that 3,7,24THCA could be translocated unchanged from the mitochondrial matrix to the peroxisomal matrix and undergo conjugation there.
R-HSA-193787 (Reactome) 5beta-cholestan-3alpha,7alpha,12alpha,24(S)-tetrol, NADPH + H+, and O2 react to form 5beta-cholestan-3alpha,7alpha,12alpha,24(S),27-pentol, NADP+, and H2O. This reaction occurs in the mitochondrial matrix, catalyzed by CYP27A1.
R-HSA-193789 (Reactome) Cholest-5-ene-3beta,7alpha,24(S)-triol and NAD+ react to form 4-cholesten-7alpha,24(S)-diol-3-one and NADH + H+, catalyzed by HSD3B7 (3 beta-hydroxysteroid dehydrogenase type 7) in the endoplasmic reticulum membrane. Its function in vivo has been confirmed in studies of patients with defects in bile acid synthesis (Schwarz et al. 2000).
R-HSA-193792 (Reactome) 5beta-cholestan-3alpha,7alpha,24(S)-triol, NADPH + H+, and O2 react to form 5beta-cholestan-3alpha,7alpha,24(S),27-tetrol, NADP+, and H2O. This reaction occurs in the mitochondrial matrix, catalyzed by CYP27A1.
R-HSA-193800 (Reactome) 5Beta-cholesten-7alpha,12a,27-triol-3-one and NADPH + H+ form 5beta-cholestan-3alpha,7alpha,12a,27-tetrol and NAPDP+. The reaction is catalyzed by 3alpha-hydroxysteroid dehydrogenase (AKR1C4), a cytosolic enzyme belonging to the aldo-keto reductase family (Dufort et al. 2001). Biochemical studies with rat proteins raise the possibility that other related enzymes may also carry out this reaction in vivo (Russell 2003).
R-HSA-193801 (Reactome) 27-hydroxycholesterol is transported from the extracellular space to the endoplasmic reticulum. In humans, this event is the means by which the molecule, generated from cholesterol in the brain, is taken up by liver cells for conversion to bile acids and bile salts (Babiker et al. 1999; Bjorkhem et al. 1994). While transport proteins are likely to play a role in this process, these proteins have not been identified.
R-HSA-193808 (Reactome) 5beta-cholestan-3alpha,7alpha,27-triol is transported from the cytosol to the mitochondrial matrix. The transporter that mediates its passage across the inner mitochondrial membrane is unknown: the StAR protein that performs this function for cholesterol at the start of steroid hormone biosynthesis is excluded as StAR is not expressed in liver. Other members of the START family of transporters are candidates, however (Russell 2003).
R-HSA-193812 (Reactome) 27-hydroxycholesterol is transported from the mitochondrial matrix to the extracellular space. In humans, this event is the major source of 27-hydroxycholesterol in the blood and is the means by which the molecule, generated from cholesterol in a variety of cell types, notably macrophages, is transported to the liver for conversion to bile acids and bile salts (Babiker et al. 1999; Bjorkhem et al. 1994). While transport proteins are likely to play a role in this process, the relevant proteins have not been identified.
R-HSA-193816 (Reactome) Cholest-5-ene-3beta,7alpha,27-triol and NAD+ react to form 4-cholesten-7alpha,27-diol-3-one and NADH + H+, in a reaction catalyzed by HSD3B7 (3 beta-hydroxysteroid dehydrogenase type 7) in the endoplasmic reticulum membrane. Its function in vivo has been confirmed in studies of patients with defects in bile acid synthesis (Schwarz et al. 2000).
R-HSA-193821 (Reactome) 4-Cholesten-7alpha,12alpha,27-triol-3-one and NADPH + H+ react to form 5beta-cholesten-7alpha,12alpha,27-triol-3-one + NADP+. This reaction is catalyzed by AKR1D1 (3-oxo-5-beta-steroid 4-dehydrogenase). AKR1D1 is localized to the cytosol, and in the course of the reaction its steroid substrate moves from the endoplasmic reticulum membrane to the cytosol. It is unclear whether this translocation results simply from its increased hydrophilicity or is mediated by the enzyme or another transport protein (Russell 2003).
R-HSA-193824 (Reactome) 4-Cholesten-7alpha,27-diol-3-one, NADPH, and H+ react to form 5beta-cholestan-7alpha,27-diol-3-one and NADP+. This reaction is catalyzed by AKR1D1 (3-oxo-5-beta-steroid 4-dehydrogenase). AKR1D1 is localized to the cytosol, and in the course of the reaction its steroid substrate moves from the endoplasmic reticulum membrane to the cytosol. It is unclear whether this translocation results simply from its increased hydrophilicity or is mediated by the enzyme or another transport protein (Russell 2003).
R-HSA-193832 (Reactome) 5beta-cholestan-3alpha,7alpha,12alpha,27-tetrol is translocated from the cytosol to the mitochondrial matrix. The transporter that mediates its passage across the inner mitochondrial membrane is unknown: the StAR protein that performs this function for cholesterol at the start of steroid hormone biosynthesis is excluded as StAR is not expressed in liver. Other members of the START family of transporters are candidates, however (Russell 2003).
R-HSA-193841 (Reactome) 5Beta-cholesten-7alpha,27-diol-3-one and NADPH + H+ form 5beta-cholestan-3alpha,7alpha,27-triol and NAPDP+. The reaction is catalyzed by 3alpha-hydroxysteroid dehydrogenase (AKR1C4), a cytosolic enzyme belonging to the aldo-keto reductase family (Dufort et al. 2001). Biochemical studies with rat proteins raise the possibility that other related enzymes may also carry out this reaction in vivo (Russell 2003).
R-HSA-193845 (Reactome) Sterol 12alpha hydroxylase (CYP8B1), associated with the endoplasmic reticulum membrane, catalyses the 12-alpha-hydroxylation of 4-Cholesten-7alpha,27-diol-3-one (4CHOL7a,27DONE) to 4-Cholesten-7alpha,12alpha,27-triol-3-one. While the human gene has been cloned (Gafvels et al. 1999), its protein product has not been characterised, and the enzymatic properties of human CYP8B1 protein are inferred from those of its well-characterised rabbit homolog (Ishida et al. 1992).
R-HSA-194079 (Reactome) A molecule of extracellular glycocholate or taurocholate is transported into the cytosol, mediated by OATP-8 (SLCO1B3) in the plasma membrane. Glycocholate and taurocholate exist in the blood as complexes with serum albumin, and their uptake by OATP-8 must involve disruption of these complexes, but the molecular mechanism coupling disruption and uptake is unknown. In the body, OATP-8 is expressed on the basolateral surfaces of hepatocytes and may play a role in the uptake of glycocholate and taurocholate by the liver under physiological conditions (Kullak-Ublick et al. 2004; Trauner and Boyer 2002).
R-HSA-194083 (Reactome) A molecule of extracellular glycocholate (GCCA) or taurocholate (TCCA) is transported into the cytosol, mediated by OATP-C (SLCO1B1) in the plasma membrane. GCCA and TCCA exist in the blood as complexes with serum albumin (ALB), and its uptake by OATP-C must involve disruption of this complex, but the molecular mechanism coupling disruption and uptake is unknown. In the body, OATP-C is expressed on the basolateral surfaces of hepatocytes and may play a role in the uptake of GCCA and TCCA by the liver under physiological conditions (Kullak-Ublick et al. 2004, Trauner & Boyer 2002).
R-HSA-194121 (Reactome) A molecule of extracellular bile salt (glyco- or taurocholate, or glyco- or taurochenodeoxycholate) and two sodium ions are transported into the cytosol, mediated by NTCP (Na+ / taurocholate cotransporter) in the plasma membrane. Bile salts exist in the blood as complexes with serum albumin, and their uptake by NTCP must involve disruption of this complex, but the molecular mechanism of the coupling of the release of a bile salt from albumin to its uptake by NTCP is unknown. In the body, NTCP is expressed on the basolateral surfaces of hepatocytes, and this reaction is the major route by which bile salts reaborbed from the intestinal lumen into the portal circulation are recovered by the liver (Kullak-Ublick et al. 2004; Trauner and Boyer 2002).
R-HSA-194130 (Reactome) A molecule of extracellular bile salt (glyco- or taurocholate or taurochenodeoxycholate) or bile acid (cholate or chenodeoxycholate) is transported into the cytosol, mediated by OATP-A (SLCO1A2) in the plasma membrane. Bile salts and acids exist in the blood as complexes with serum albumin, and their uptake by OATP-A must involve disruption of this complex, but the molecular mechanism coupling release of a bile salt or acid from albumin to its uptake by OATP-A is unknown. In the body, OATP-A is expressed only at low levels on the basolateral surfaces of hepatocytes and may play only a minor role in the uptake of bile salts and acids by the liver (Kullak-Ublick et al. 2004; Trauner and Boyer 2002).
R-HSA-194153 (Reactome) A molecule of glycocholate, taurocholate, or taurochenodeoxycholate is transported from the cytosol to the extracellular space, coupled to the hydrolysis of a molecule of cytosolic ATP to ADP and orthophosphate. This reaction is mediated by ABCB3 (MRP3). In the body, this reaction mediates the release of bile salts from enterocytes into the blood (Kullak-Ublick et al. 2004; Trauner and Boyer 2002). In the cytosol, bile salts and acids are bound to a carrier protein, FABP6 (I-BABP) (Fujita et al. 1995), and in the blood these molecules are complexed with albumin. The mechanisms by which transport across the plasma membrane is coupled to release FABP6 and binding to albumin are unknown, so the entire process is annotated as a single concerted event.
R-HSA-194187 (Reactome) A molecule of extracellular bile salt or bile acid (cholate, chenodeoxycholate, or their glycine or taurine conjugates) and a sodium ion are transported into the cytosol, mediated by ASBT (apical sodium-dependent bile acid transporter; SLC10A2) in the plasma membrane. In the body, ASBT is expressed on the apical surfaces of enterocytes, and this reaction is the first step in the process by which bile salts and acids are reaborbed from the intestinal lumen and returned to the liver (Kullak-Ublick et al. 2004, Trauner & Boyer 2002). Cytosolic ileal bile acid binding protein (IBABP, FABP6) mediates the transcellular movement of bile acids to the basolateral membrane across which they exit the cells via organic solute transporters (OST) (Kurz et al. 2003).
R-HSA-5340195 (Reactome) The nuclear orphan protein bile acid receptor aka farnesoid X-activated receptor (NR1H4 aka FXR) can be activated by bile acids and their salts, its physiological ligands. Mouse Nrih4 is highly expressed in the liver, intestine, kidney and adrenal gland, and to a lesser extent in white adipose tissue and heart (Zhang et al. 2003). Bile acids tested to activate NR1H4 are chenodeoxycholic acid (CDCA), lithocholic acid (LCHA) and deoxycholic acid (DCA) (Parks et al. 1999, Makishima et al. 1999).

Once bound to its ligand, activated NR1H4 binds to retinoic acid receptor RXR-alpha (RXRA) and either nuclear receptor coactivator 1 or 2 (NCOA1 or 2) to function as a ligand-activated transcription factor. This complex repressed transcription of the CYP7A1 gene (encoding cholesterol 7alpha-hydroxylase, the rate-limiting enzyme in bile acid synthesis) (Holt et al. 2003) and activated the SLC10A2 and 6 genes (encoding Ileal sodium/bile acid cotransporters, both bile acid transporters) (Plass et al. 2002, Ananthanarayanan et al. 2001). Thus, NR1H4 is one of the most important regulators of bile acid metabolism, regulating bile acid synthesis, conjugation, secretion and uptake (Lee et al. 2006, Houten et al. 2006).
R-HSA-5340251 (Reactome) The nuclear orphan protein bile acid receptor aka farnesoid X-activated receptor (NR1H4 aka FXR) can be activated by bile acids and their salts, its physiological ligands. Bile acids tested to activate NR1H4 are chenodeoxycholic acid (CDCA), lithocholic acid (LCHA) and deoxycholic acid (DCA) (Parks et al. 1999, Makishima et al. 1999). Once bound to its ligand, activated NR1H4 binds to retinoic acid receptor RXR-alpha (RXRA) and either nuclear receptor coactivator 1 or 2 (NCOA1 or 2) to function as a ligand-activated transcription factor. This complex repressed transcription of the CYP7A1 gene (encoding cholesterol 7alpha-hydroxylase, the rate-limiting enzyme in bile acid synthesis) (Holt et al. 2003) and activated the SLC10A2 and 6 genes (encoding Ileal sodium/bile acid cotransporters; both bile acid transporters) (Plass et al. 2002, Ananthanarayanan et al. 2001). Thus, NR1H4 is one of the most important regulators of bile acid metabolism, regulating bile acid synthesis, conjugation, secretion and uptake (Lee et al. 2006, Houten et al. 2006).
R-HSA-8867667 (Reactome) Oxysterol-binding proteins (OSBPs) and OSBP-related proteins (ORPs) comprise a 12-member mammalian gene family of intracellular lipid receptors which bind oxygenated cholesterol derivatives and are thought to mediate sterol and phospholipid synthesis (Olkkonen & Li 2013, Weber-Boyvat et al. 2013). A conserved OSBP homology domain (OHD) binds sterols and lipids and a pleckstrin homology (PH) domain and two phenylalanines in an acidic tract (FFAT) motif mediate interaction with organelle membranes (Olkkonen 2015). The primary function of the protein family remains unresolved. Most (OSBPL2,3,6,7,9 and 1A), if not all of the OSBPLs are thought to bind and coordinate distribution of oxygenated cholesterol derivatives such as 25-hydroxycholesterol (25OH-CHOL). Oxysterol-binding protein 2 (OSBP2, aka ORP4) is primarily expressed in brain, and to a lesser extent in heart, skeletal muscle, spleen and kidney. It has a diffuse cytoplasmic localisation profile and is a high-affinity 25OH-CHOL binding protein (Wang et al. 2002, Suchanek et al. 2007). RNAi silencing of all OSBP2 variants in HEK293 and HeLa cells resulted in growth arrest but not cell death, suggesting OSBP2 is essential for cell proliferation and survival (Charman et al. 2014).
R-HSA-8868402 (Reactome) Oxysterol-binding protein 1 (OSBP) is involved in lipid countertransport between the Golgi and the ER membranes. It specifically exchanges sterols such as 25-hydroxycholesterol (25OH-CHOL) with phosphatidylinositol 4-phosphate (PI4P), delivering it to the Golgi in exchange for PI4P, which is degraded by the SAC1/SACM1L phosphatases in the ER. The PH-FFAT region of OSBP is necessary for membrane tethering, which then directs forward sterol and backward PI4P transport by the ORD domain of OSBP (Mesmin et al. 2013).
R-HSA-8873850 (Reactome) StAR-related lipid transfer protein 5 (STARD5) is highly expressed in at least three cell types targeted by bile acids: liver macrophage Kupffer cells, peripheral macrophages and kidney proximal tubule cells. Unlike the other members of the STARD4 subfamily of the START-containing proteins (members 4 and 6), STARD5 possesses low or no affinity for cholesterol but instead, specifically binds primary and secondary bile acids. STARD5's affinity for the secondary bile acids deoxycholic acid (DCA) and lithocholic acid (LCA), which lack the alpha-OH in C7, is greater than that of the primary bile acids cholic acid (CA) and chenodeoxycholic acid (CDCA) (Letourneau et al. 2012, Letourneau et al. 2013). The physiological roles played by STARD5 remain to be elucidated but it could act as a bile acid transporter or sensor.
RXRAR-HSA-5340251 (Reactome)
SCP2-1mim-catalysisR-HSA-192341 (Reactome)
SCP2-1mim-catalysisR-HSA-193533 (Reactome)
SLC10A1mim-catalysisR-HSA-194121 (Reactome)
SLC10A2mim-catalysisR-HSA-194187 (Reactome)
SLC27A2mim-catalysisR-HSA-193401 (Reactome)
SLC27A2mim-catalysisR-HSA-193424 (Reactome)
SLC27A2mim-catalysisR-HSA-193727 (Reactome)
SLC27A2mim-catalysisR-HSA-193743 (Reactome)
SLC27A5mim-catalysisR-HSA-159425 (Reactome)
SLC27A5mim-catalysisR-HSA-192137 (Reactome)
SLC27A5mim-catalysisR-HSA-193407 (Reactome)
SLC27A5mim-catalysisR-HSA-193711 (Reactome)
SLC27A5mim-catalysisR-HSA-193766 (Reactome)
SLCO1A2mim-catalysisR-HSA-194130 (Reactome)
SLCO1B1mim-catalysisR-HSA-194083 (Reactome)
SLCO1B3mim-catalysisR-HSA-194079 (Reactome)
STARD5:DCA,LCAArrowR-HSA-8873850 (Reactome)
STARD5R-HSA-8873850 (Reactome)
THCA-CoAArrowR-HSA-192335 (Reactome)
THCA-CoAR-HSA-192331 (Reactome)
THCAArrowR-HSA-191971 (Reactome)
THCAArrowR-HSA-192054 (Reactome)
THCAR-HSA-191971 (Reactome)
THCAR-HSA-192137 (Reactome)
THCAR-HSA-193401 (Reactome)
TetraHCAArrowR-HSA-193713 (Reactome)
TetraHCAArrowR-HSA-193722 (Reactome)
TetraHCAR-HSA-193722 (Reactome)
TetraHCAR-HSA-193727 (Reactome)
TetraHCAR-HSA-193766 (Reactome)
albumin:bile salt

and acid (OATP-A)

complex
R-HSA-194130 (Reactome)
albumin:bile salt complexR-HSA-194121 (Reactome)
bile salts and acids:FABP6ArrowR-HSA-194187 (Reactome)
bile salts and acids:FABP6R-HSA-194153 (Reactome)
bile salts and acids (OATP-A)ArrowR-HSA-194130 (Reactome)
bile salts and acids

complexed with

albumin
ArrowR-HSA-194153 (Reactome)
bile salts and acidsR-HSA-194187 (Reactome)
bile saltsArrowR-HSA-159431 (Reactome)
bile saltsArrowR-HSA-192315 (Reactome)
bile saltsArrowR-HSA-193362 (Reactome)
bile saltsArrowR-HSA-194121 (Reactome)
bile saltsR-HSA-192315 (Reactome)
bile saltsR-HSA-193362 (Reactome)
chenodeoxycholate bile saltsArrowR-HSA-193491 (Reactome)
chenodeoxycholoyl-CoAArrowR-HSA-193533 (Reactome)
chenodeoxycholoyl-CoAR-HSA-193491 (Reactome)
cholate bile saltsArrowR-HSA-192312 (Reactome)
cholate; chenodeoxycholateR-HSA-159425 (Reactome)
cholateArrowR-HSA-193385 (Reactome)
cholateR-HSA-193399 (Reactome)
choloyl-CoA; chenodeoxycholoyl-CoAArrowR-HSA-159425 (Reactome)
choloyl-CoA; chenodeoxycholoyl-CoAR-HSA-159431 (Reactome)
choloyl-CoAArrowR-HSA-192341 (Reactome)
choloyl-CoAR-HSA-192312 (Reactome)
choloyl-CoAR-HSA-193385 (Reactome)
glycine; taurineR-HSA-159431 (Reactome)
glycine; taurineR-HSA-192312 (Reactome)
glycine; taurineR-HSA-193491 (Reactome)
propionyl CoAArrowR-HSA-192341 (Reactome)
propionyl CoAArrowR-HSA-193533 (Reactome)
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