Bile acid and bile salt metabolism (Homo sapiens)

From WikiPathways

Revision as of 13:56, 8 May 2014 by Anwesha (Talk | contribs)
Jump to: navigation, search
26, 30, 31, 384612, 162421, 34, 4112, 163832351, 15272, 838383853821, 34, 416, 7, 473811, 24, 3621, 34, 4114373822, 25, 282743, 4543, 4522, 25, 2821, 34, 41321418, 20, 393834103529, 491424, 3624, 361733, 40383322, 25, 284, 42173838324, 3621, 34, 4121, 34, 4124, 36389, 27, 4421, 34, 4135143832351911, 24, 361424, 3633821, 34, 4113, 23, 371, 151422, 25, 2843, 453824, 363812, 16484, 4224, 3611, 24, 36311, 24, 3624, 36bile salts and acids endoplasmic reticulum lumencholate bile salts cytosolalbuminbile salt complex albumincholate bile salt complex CH25H bile salts and acids endoplasmic reticulum lumenendoplasmic reticulum lumenperoxisomal matrixHSD17B4 dimer mitochondrial matrixcytosolendoplasmic reticulum lumenendoplasmic reticulum lumenmitochondrial matrixACOX2FAD bile salts and acids bile salts and acids complexed with albumin bile salts endoplasmic reticulum lumenbile salts and acids complexed with FABP6 albuminbile salt and acid cytosolcytosolCYP27A1H2O5beta-cholestan-3alpha,7alpha,12alpha,245beta-cholestan-3alpha,7alpha,26-triolNADPHO2NADHH+3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-one-CoACytochrome P450 NADP+Cholest-5-ene-3beta,7alpha,24ABCC3ALB3,7,24THCA-CoACytochrome P450 NADP+NADPHH2Oglycocholate H+HSD3B73,7,24THCA-CoAO2H+AKR1D13alpha,7alpha-dihydroxy-5beta-cholest-24-one-CoAbile salts and acids24-hydroxycholesterolbile salts and acids complexed with albuminO2cholateHSD3B7H+SLCO1A2cholate NAD+NADP+H2OH+chenodeoxycholate NADP+O25beta-cholestan-3alpha,7alpha,12alpha,24ADPNAD+glycocholate bile salts and acids ALB cholate NADPHbile saltsglycocholate NADH5beta-cholestan-3alpha, 7alpha-dioltaurochenodeoxycholate Cytochrome P450 O2albumincholate bile salt complexH2Oglycine; taurine4-cholesten-7alpha, 12alpha-diol-3-oneglycochenodeoxycholate O24-cholesten-7alpha,12alpha,27-triol-3-oneATPFABP6cholate; chenodeoxycholateCYP39A1NADP+Na+H2ONADP+3alpha,7alpha,24CoA-SHH+H2OAMPNADP+PiNADPHCoA-SHSLCO1B3cholate bile saltsH2OH+5beta-cholestan-3alpha,7alpha,24ALB 25NADP+H2OH+taurocholate H2OH2OTetraHCAH2OAMPH+25H+CYP27A1NAD+SLC27A525CYP27A1albuminbile salt complexglycine; taurine27-hydroxycholesterolH+PPibile saltsAKR1D1ATPCoA-SHALB ALB 25NADP+taurocholate taurochenodeoxycholate H2ONADPHNADPH4-cholesten-7alpha,27-diol-3-oneFAD 25H+NADPH24-hydroxycholesterolSLC27A527HCHOLcholate choloyl-CoA; chenodeoxycholoyl-CoA25SLC10A1NADPH25H+Na+H+7 alpha-hydroxycholesterolDHCACoA-SHAMPNADP+4-cholesten-7alpha,12alpha,24BAATCytochrome P450 CH25H cholateH2OH+5beta-cholestan-3alpha,7alpha,12alpha,27-tetrolCholesterolNADP+CoA-SHalbuminbile salt and acid CholesterolCHOLH2OCytochrome P450 NADHFe2+ NADP+ABCB11HSD17B4NADHPibile saltsglycochenodeoxycholate NAD+NADP+NADPHCYP27A1PPiH2ONADP+ADPH+3,7,24THCANa+chenodeoxycholate H2O2CYP46A1Cytochrome P450 NADPH5beta-cholestan-3alpha,7alpha,12alpha,24H+5beta-cholestan-7alpha,24CholesterolSCP2-15beta-cholestan-7alpha,12alpha,27-triol-3-onetaurocholate 5beta-cholestan-3alpha,7alpha,24ACOT8NADPH5beta-cholestan-7alpha-ol-3-oneH2OH+O225glycochenodeoxycholate 5beta-cholestan-7alpha,27-diol-3-oneH2OH+NADP+SLC27A2NADPHH2OFABP6 5beta-cholestan-7alpha,12alpha,24H+25O2SLC27A5NADP+HSD17B4 dimerCoA-SHNADP+TetraHCA5beta-cholestan-3alpha,7alpha,26-triolDHCAcholoyl-CoAO2Aldo-keto reductase familyH2OO2SLC10A2taurochenodeoxycholate NADPHO25beta-cholestan-3alpha,7alpha,243alpha,7alpha,12alpha,24H+O2NAD+NADPHO2ACOX2 H+PPi5beta-cholestan-3alpha,7alpha-diolbile salts and acids complexed with FABP65beta-cholesten-7alpha, 12alpha-diol-3-oneCYP27A1ATPchenodeoxycholoyl-CoAO23,7,24THCANADPHCYP27A1Aldo-keto reductase family25-hydroxycholesterolNADPHO2HSD3B7H2O3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-27-alNADPHH2O27-hydroxycholesterolNADPHH+cholate bile saltsCholest-5-ene-3beta,7alpha,27-triolNADPHNADPHNADPHNADP+ACOX2FADglycocholate bile salts24-hydroxycholesterol5beta-cholestan-3alpha, 7alpha, 12alpha-triolSLCO1B1Aldo-keto reductase familyCholest-5-ene-3beta,7alpha,25-triolchenodeoxycholate bile saltsH+THCA-CoAAKR1D1NADP+H+NADP+5beta-cholestan-3alpha,7alpha,12alpha-triolNADPHtaurochenodeoxycholate 3alpha,7alpha-dihydroxy-5beta-cholestan-26-alCYP27A15beta-cholestan-3alpha,7alpha,12alpha,27-tetroltaurocholate NADP+ATPBAATATPNADP+chenodeoxycholate THCAtaurocholate CH25H THCApropionyl CoAO2CoA-SHglycocholate 4-cholesten-7alpha-ol-3-one4-cholesten-7alpha,24H+AMACRSLC27A2Na+


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). Original Pathway at Reactome: http://www.reactome.org/PathwayBrowser/#DB=gk_current&FOCUS_SPECIES_ID=48887&FOCUS_PATHWAY_ID=194068

Try the New WikiPathways

View approved pathways at the new wikipathways.org.

Quality Tags

Ontology Terms

 

Bibliography

View all...
  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

View all...
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

View all...
NameTypeDatabase referenceComment
24-hydroxycholesterolMetaboliteCHEBI:34310 (ChEBI)
25-hydroxycholesterolMetaboliteCHEBI:42977 (ChEBI)
25MetaboliteCHEBI:15494 (ChEBI)
25MetaboliteCHEBI:27393 (ChEBI)
25MetaboliteCHEBI:27458 (ChEBI)
25MetaboliteCHEBI:37642 (ChEBI)
25MetaboliteCHEBI:37643 (ChEBI)
27-hydroxycholesterolMetaboliteCHEBI:17703 (ChEBI)
27HCHOLMetaboliteCHEBI:17703 (ChEBI)
3,7,24THCA-CoAMetaboliteCHEBI:27403 (ChEBI)
3,7,24THCAMetaboliteCHEBI:27403 (ChEBI)
3alpha,7alpha,12alpha,24MetaboliteCHEBI: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,24MetaboliteCHEBI:63848 (ChEBI)
3alpha,7alpha-dihydroxy-5beta-cholest-24-one-CoAMetaboliteCHEBI:28533 (ChEBI)
3alpha,7alpha-dihydroxy-5beta-cholestan-26-alMetaboliteCHEBI:27428 (ChEBI)
4-cholesten-7alpha, 12alpha-diol-3-oneMetaboliteCHEBI:28477 (ChEBI)
4-cholesten-7alpha,12alpha,24MetaboliteCHEBI:63839 (ChEBI)
4-cholesten-7alpha,12alpha,27-triol-3-oneMetaboliteCHEBI:48333 (ChEBI)
4-cholesten-7alpha,24MetaboliteCHEBI:63838 (ChEBI)
4-cholesten-7alpha,27-diol-3-oneMetaboliteCHEBI:48825 (ChEBI)
4-cholesten-7alpha-ol-3-oneMetaboliteCHEBI:17899 (ChEBI)
5beta-cholestan-3alpha, 7alpha, 12alpha-triolMetaboliteCHEBI:16496 (ChEBI)
5beta-cholestan-3alpha, 7alpha-diolMetaboliteCHEBI:28047 (ChEBI)
5beta-cholestan-3alpha,7alpha,12alpha,24MetaboliteCHEBI:17278 (ChEBI)
5beta-cholestan-3alpha,7alpha,12alpha,24MetaboliteCHEBI:63834 (ChEBI)
5beta-cholestan-3alpha,7alpha,12alpha,24MetaboliteCHEBI:63835 (ChEBI)
5beta-cholestan-3alpha,7alpha,12alpha,27-tetrolMetaboliteCHEBI:17278 (ChEBI)
5beta-cholestan-3alpha,7alpha,12alpha-triolMetaboliteCHEBI:16496 (ChEBI)
5beta-cholestan-3alpha,7alpha,24MetaboliteCHEBI:63831 (ChEBI)
5beta-cholestan-3alpha,7alpha,24MetaboliteCHEBI:63833 (ChEBI)
5beta-cholestan-3alpha,7alpha,26-triolMetaboliteCHEBI:28540 (ChEBI)
5beta-cholestan-3alpha,7alpha-diolMetaboliteCHEBI:28047 (ChEBI)
5beta-cholestan-7alpha,12alpha,24MetaboliteCHEBI:63830 (ChEBI)
5beta-cholestan-7alpha,12alpha,27-triol-3-oneMetaboliteCHEBI:48834 (ChEBI)
5beta-cholestan-7alpha,24MetaboliteCHEBI: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 FADComplexREACT_10603 (Reactome)
ACOX2 ProteinQ99424 (Uniprot-TrEMBL)
ADPMetaboliteCHEBI:16761 (ChEBI)
AKR1D1ProteinP51857 (Uniprot-TrEMBL)
ALB ProteinP02768 (Uniprot-TrEMBL)
ALBProteinP02768 (Uniprot-TrEMBL)
AMACRProteinQ9UHK6 (Uniprot-TrEMBL)
AMPMetaboliteCHEBI:16027 (ChEBI)
ATPMetaboliteCHEBI:15422 (ChEBI)
Aldo-keto reductase familyProteinREACT_164934 (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)
CH25H ProteinO95992 (Uniprot-TrEMBL)
CH25H ComplexREACT_10164 (Reactome)
MetaboliteCHEBI:27403 (ChEBI)
MetaboliteCHEBI:52050 (ChEBI)
CHOLMetaboliteCHEBI:16113 (ChEBI)
CYP27A1ProteinQ02318 (Uniprot-TrEMBL)
CYP39A1ProteinQ9NYL5 (Uniprot-TrEMBL)
CYP46A1ProteinQ9Y6A2 (Uniprot-TrEMBL)
Cholest-5-ene-3beta,7alpha,24MetaboliteCHEBI:37640 (ChEBI)
Cholest-5-ene-3beta,7alpha,25-triolMetaboliteCHEBI:37623 (ChEBI)
Cholest-5-ene-3beta,7alpha,27-triolMetaboliteCHEBI:18431 (ChEBI)
CholesterolMetaboliteCHEBI:16113 (ChEBI)
CoA-SHMetaboliteCHEBI:15346 (ChEBI)
Cytochrome P450 ProteinREACT_160403 (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 ProteinREACT_164336 (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 ProteinREACT_165338 (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.
DHCAMetaboliteCHEBI:16577 (ChEBI)
FABP6 ProteinP51161 (Uniprot-TrEMBL)
FABP6ProteinP51161 (Uniprot-TrEMBL)
FAD MetaboliteCHEBI:16238 (ChEBI)
Fe2+ MetaboliteCHEBI:18248 (ChEBI)
H+MetaboliteCHEBI:15378 (ChEBI)
H2O2MetaboliteCHEBI:16240 (ChEBI)
H2OMetaboliteCHEBI:15377 (ChEBI)
HSD17B4 dimerComplexREACT_17840 (Reactome)
HSD17B4ProteinP51659 (Uniprot-TrEMBL)
HSD3B7ProteinQ9H2F3 (Uniprot-TrEMBL)
NAD+MetaboliteCHEBI:15846 (ChEBI)
NADHMetaboliteCHEBI:16908 (ChEBI)
NADP+MetaboliteCHEBI:18009 (ChEBI)
NADPHMetaboliteCHEBI:16474 (ChEBI)
Na+MetaboliteCHEBI:29101 (ChEBI)
O2MetaboliteCHEBI:15379 (ChEBI)
PPiMetaboliteCHEBI:29888 (ChEBI)
PiMetaboliteCHEBI:18367 (ChEBI)
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)
THCA-CoAMetaboliteCHEBI:27505 (ChEBI)
THCAMetaboliteCHEBI:18402 (ChEBI)
TetraHCAMetaboliteCHEBI:63824 (ChEBI)
albumin bile salt and acid ComplexREACT_10829 (Reactome)
albumin bile salt complexComplexREACT_10145 (Reactome)
albumin cholate bile salt complexComplexREACT_10265 (Reactome)
bile salts and acids MetaboliteREACT_10444 (Reactome)
bile salts and acids complexed with FABP6ComplexREACT_10401 (Reactome)
bile salts and acids complexed with albuminComplexREACT_10309 (Reactome)
bile salts and acidsMetaboliteREACT_9533 (Reactome)
bile saltsMetaboliteREACT_10276 (Reactome)
bile saltsMetaboliteREACT_10834 (Reactome)
bile saltsMetaboliteREACT_11011 (Reactome)
chenodeoxycholate MetaboliteCHEBI:16755 (ChEBI)
chenodeoxycholate bile saltsMetaboliteREACT_10485 (Reactome)
chenodeoxycholoyl-CoAMetaboliteCHEBI:28701 (ChEBI)
cholate MetaboliteCHEBI:16359 (ChEBI)
cholate bile saltsMetaboliteREACT_10246 (Reactome)
cholate bile saltsMetaboliteREACT_10914 (Reactome)
cholate; chenodeoxycholateMetaboliteREACT_10869 (Reactome)
cholateMetaboliteCHEBI:16359 (ChEBI)
choloyl-CoA; chenodeoxycholoyl-CoAMetaboliteREACT_10852 (Reactome)
choloyl-CoAMetaboliteCHEBI:15519 (ChEBI)
glycine; taurineMetaboliteREACT_10219 (Reactome)
glycine; taurineMetaboliteREACT_10925 (Reactome)
glycochenodeoxycholate MetaboliteCHEBI:36274 (ChEBI)
glycocholate MetaboliteCHEBI:17687 (ChEBI)
propionyl CoAMetaboliteCHEBI:15539 (ChEBI)
taurochenodeoxycholate MetaboliteCHEBI:16525 (ChEBI)
taurochenodeoxycholate MetaboliteCHEBI:9407 (ChEBI)
taurocholate MetaboliteCHEBI:28865 (ChEBI)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
24-hydroxycholesterolArrowREACT_10129 (Reactome)
24-hydroxycholesterolREACT_10066 (Reactome)
25-hydroxycholesterolArrowREACT_10030 (Reactome)
25-hydroxycholesterolREACT_9950 (Reactome)
25ArrowREACT_10000 (Reactome)
25ArrowREACT_10003 (Reactome)
25ArrowREACT_10020 (Reactome)
25ArrowREACT_10049 (Reactome)
25ArrowREACT_10064 (Reactome)
25ArrowREACT_10106 (Reactome)
25ArrowREACT_10119 (Reactome)
25REACT_10003 (Reactome)
25REACT_10074 (Reactome)
25REACT_9952 (Reactome)
27-hydroxycholesterolArrowREACT_9953 (Reactome)
27HCHOLREACT_9994 (Reactome)
3,7,24THCA-CoAArrowREACT_10087 (Reactome)
3,7,24THCA-CoAArrowREACT_9970 (Reactome)
3,7,24THCAArrowREACT_9988 (Reactome)
3,7,24THCAREACT_10087 (Reactome)
3,7,24THCAREACT_9970 (Reactome)
3alpha,7alpha,12alpha,24ArrowREACT_10042 (Reactome)
3alpha,7alpha,12alpha,24REACT_10100 (Reactome)
3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-one-CoAArrowREACT_10065 (Reactome)
3alpha,7alpha,12alpha-trihydroxy-5beta-cholest-24-one-CoAREACT_10113 (Reactome)
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-27-alArrowREACT_10025 (Reactome)
3alpha,7alpha,12alpha-trihydroxy-5beta-cholestan-27-alREACT_10001 (Reactome)
3alpha,7alpha,24ArrowREACT_9976 (Reactome)
3alpha,7alpha,24REACT_9988 (Reactome)
3alpha,7alpha-dihydroxy-5beta-cholest-24-one-CoAArrowREACT_9967 (Reactome)
3alpha,7alpha-dihydroxy-5beta-cholest-24-one-CoAREACT_10103 (Reactome)
3alpha,7alpha-dihydroxy-5beta-cholestan-26-alArrowREACT_9960 (Reactome)
3alpha,7alpha-dihydroxy-5beta-cholestan-26-alREACT_10005 (Reactome)
4-cholesten-7alpha, 12alpha-diol-3-oneArrowREACT_10071 (Reactome)
4-cholesten-7alpha, 12alpha-diol-3-oneREACT_10048 (Reactome)
4-cholesten-7alpha,12alpha,24ArrowREACT_10016 (Reactome)
4-cholesten-7alpha,12alpha,24REACT_10131 (Reactome)
4-cholesten-7alpha,12alpha,27-triol-3-oneArrowREACT_10028 (Reactome)
4-cholesten-7alpha,12alpha,27-triol-3-oneREACT_10018 (Reactome)
4-cholesten-7alpha,24ArrowREACT_10090 (Reactome)
4-cholesten-7alpha,24REACT_10016 (Reactome)
4-cholesten-7alpha,24REACT_10086 (Reactome)
4-cholesten-7alpha,27-diol-3-oneArrowREACT_10115 (Reactome)
4-cholesten-7alpha,27-diol-3-oneREACT_10028 (Reactome)
4-cholesten-7alpha,27-diol-3-oneREACT_10102 (Reactome)
4-cholesten-7alpha-ol-3-oneArrowREACT_10067 (Reactome)
4-cholesten-7alpha-ol-3-oneREACT_10071 (Reactome)
4-cholesten-7alpha-ol-3-oneREACT_9972 (Reactome)
5beta-cholestan-3alpha, 7alpha, 12alpha-triolREACT_10009 (Reactome)
5beta-cholestan-3alpha, 7alpha-diolREACT_10075 (Reactome)
5beta-cholestan-3alpha,7alpha,12alpha,24ArrowREACT_10044 (Reactome)
5beta-cholestan-3alpha,7alpha,12alpha,24ArrowREACT_10104 (Reactome)
5beta-cholestan-3alpha,7alpha,12alpha,24REACT_10042 (Reactome)
5beta-cholestan-3alpha,7alpha,12alpha,24REACT_10104 (Reactome)
5beta-cholestan-3alpha,7alpha,12alpha,27-tetrolArrowREACT_10009 (Reactome)
5beta-cholestan-3alpha,7alpha,12alpha,27-tetrolArrowREACT_10038 (Reactome)
5beta-cholestan-3alpha,7alpha,12alpha,27-tetrolREACT_10025 (Reactome)
5beta-cholestan-3alpha,7alpha,12alpha-triolArrowREACT_10120 (Reactome)
5beta-cholestan-3alpha,7alpha,24ArrowREACT_10054 (Reactome)
5beta-cholestan-3alpha,7alpha,24ArrowREACT_10096 (Reactome)
5beta-cholestan-3alpha,7alpha,24REACT_10096 (Reactome)
5beta-cholestan-3alpha,7alpha,24REACT_9976 (Reactome)
5beta-cholestan-3alpha,7alpha,26-triolArrowREACT_10008 (Reactome)
5beta-cholestan-3alpha,7alpha,26-triolArrowREACT_10075 (Reactome)
5beta-cholestan-3alpha,7alpha,26-triolREACT_9960 (Reactome)
5beta-cholestan-3alpha,7alpha-diolArrowREACT_10068 (Reactome)
5beta-cholestan-7alpha,12alpha,24ArrowREACT_10131 (Reactome)
5beta-cholestan-7alpha,12alpha,24REACT_10044 (Reactome)
5beta-cholestan-7alpha,12alpha,27-triol-3-oneArrowREACT_10018 (Reactome)
5beta-cholestan-7alpha,12alpha,27-triol-3-oneREACT_10038 (Reactome)
5beta-cholestan-7alpha,24ArrowREACT_10086 (Reactome)
5beta-cholestan-7alpha,24REACT_10054 (Reactome)
5beta-cholestan-7alpha,27-diol-3-oneArrowREACT_10102 (Reactome)
5beta-cholestan-7alpha,27-diol-3-oneREACT_10008 (Reactome)
5beta-cholestan-7alpha-ol-3-oneArrowREACT_9972 (Reactome)
5beta-cholestan-7alpha-ol-3-oneREACT_10068 (Reactome)
5beta-cholesten-7alpha, 12alpha-diol-3-oneArrowREACT_10048 (Reactome)
5beta-cholesten-7alpha, 12alpha-diol-3-oneREACT_10120 (Reactome)
7 alpha-hydroxycholesterolArrowREACT_10052 (Reactome)
7 alpha-hydroxycholesterolREACT_10067 (Reactome)
ABCB11mim-catalysisREACT_10101 (Reactome)
ABCC3mim-catalysisREACT_10078 (Reactome)
ACOT8mim-catalysisREACT_10061 (Reactome)
ACOX2 FADmim-catalysisREACT_10003 (Reactome)
ACOX2 FADmim-catalysisREACT_10074 (Reactome)
ADPArrowREACT_10078 (Reactome)
ADPArrowREACT_10101 (Reactome)
AKR1D1mim-catalysisREACT_10018 (Reactome)
AKR1D1mim-catalysisREACT_10048 (Reactome)
AKR1D1mim-catalysisREACT_10086 (Reactome)
AKR1D1mim-catalysisREACT_10102 (Reactome)
AKR1D1mim-catalysisREACT_10131 (Reactome)
AKR1D1mim-catalysisREACT_9972 (Reactome)
ALBArrowREACT_10072 (Reactome)
ALBArrowREACT_10091 (Reactome)
ALBArrowREACT_10124 (Reactome)
ALBArrowREACT_9958 (Reactome)
ALBREACT_10078 (Reactome)
AMACRmim-catalysisREACT_10047 (Reactome)
AMACRmim-catalysisREACT_10132 (Reactome)
AMACRmim-catalysisREACT_9964 (Reactome)
AMACRmim-catalysisREACT_9998 (Reactome)
AMPArrowREACT_10000 (Reactome)
AMPArrowREACT_10020 (Reactome)
AMPArrowREACT_10034 (Reactome)
AMPArrowREACT_10049 (Reactome)
AMPArrowREACT_10064 (Reactome)
AMPArrowREACT_10087 (Reactome)
AMPArrowREACT_10106 (Reactome)
AMPArrowREACT_10119 (Reactome)
AMPArrowREACT_9970 (Reactome)
ATPREACT_10000 (Reactome)
ATPREACT_10020 (Reactome)
ATPREACT_10034 (Reactome)
ATPREACT_10049 (Reactome)
ATPREACT_10064 (Reactome)
ATPREACT_10078 (Reactome)
ATPREACT_10087 (Reactome)
ATPREACT_10101 (Reactome)
ATPREACT_10106 (Reactome)
ATPREACT_10119 (Reactome)
ATPREACT_9970 (Reactome)
Aldo-keto reductase familymim-catalysisREACT_10008 (Reactome)
Aldo-keto reductase familymim-catalysisREACT_10038 (Reactome)
Aldo-keto reductase familymim-catalysisREACT_10044 (Reactome)
Aldo-keto reductase familymim-catalysisREACT_10054 (Reactome)
Aldo-keto reductase familymim-catalysisREACT_10068 (Reactome)
Aldo-keto reductase familymim-catalysisREACT_10120 (Reactome)
BAATmim-catalysisREACT_9968 (Reactome)
BAATmim-catalysisREACT_9974 (Reactome)
BAATmim-catalysisREACT_9991 (Reactome)
CH25H mim-catalysisREACT_10030 (Reactome)
CHOLREACT_10030 (Reactome)
CYP27A1mim-catalysisREACT_10001 (Reactome)
CYP27A1mim-catalysisREACT_10005 (Reactome)
CYP27A1mim-catalysisREACT_10009 (Reactome)
CYP27A1mim-catalysisREACT_10025 (Reactome)
CYP27A1mim-catalysisREACT_10042 (Reactome)
CYP27A1mim-catalysisREACT_10075 (Reactome)
CYP27A1mim-catalysisREACT_10096 (Reactome)
CYP27A1mim-catalysisREACT_10100 (Reactome)
CYP27A1mim-catalysisREACT_10104 (Reactome)
CYP27A1mim-catalysisREACT_9953 (Reactome)
CYP27A1mim-catalysisREACT_9960 (Reactome)
CYP27A1mim-catalysisREACT_9976 (Reactome)
CYP27A1mim-catalysisREACT_9988 (Reactome)
CYP39A1mim-catalysisREACT_10066 (Reactome)
CYP46A1mim-catalysisREACT_10129 (Reactome)
Cholest-5-ene-3beta,7alpha,24ArrowREACT_10066 (Reactome)
Cholest-5-ene-3beta,7alpha,24REACT_10090 (Reactome)
Cholest-5-ene-3beta,7alpha,25-triolArrowREACT_9950 (Reactome)
Cholest-5-ene-3beta,7alpha,27-triolArrowREACT_9994 (Reactome)
Cholest-5-ene-3beta,7alpha,27-triolREACT_10115 (Reactome)
CholesterolREACT_10052 (Reactome)
CholesterolREACT_10129 (Reactome)
CholesterolREACT_9953 (Reactome)
CoA-SHArrowREACT_10061 (Reactome)
CoA-SHArrowREACT_9968 (Reactome)
CoA-SHArrowREACT_9974 (Reactome)
CoA-SHArrowREACT_9991 (Reactome)
CoA-SHREACT_10000 (Reactome)
CoA-SHREACT_10020 (Reactome)
CoA-SHREACT_10034 (Reactome)
CoA-SHREACT_10049 (Reactome)
CoA-SHREACT_10064 (Reactome)
CoA-SHREACT_10087 (Reactome)
CoA-SHREACT_10103 (Reactome)
CoA-SHREACT_10106 (Reactome)
CoA-SHREACT_10113 (Reactome)
CoA-SHREACT_10119 (Reactome)
CoA-SHREACT_9970 (Reactome)
Cytochrome P450 mim-catalysisREACT_10016 (Reactome)
Cytochrome P450 mim-catalysisREACT_10028 (Reactome)
Cytochrome P450 mim-catalysisREACT_10052 (Reactome)
Cytochrome P450 mim-catalysisREACT_10071 (Reactome)
Cytochrome P450 mim-catalysisREACT_9950 (Reactome)
Cytochrome P450 mim-catalysisREACT_9994 (Reactome)
DHCAArrowREACT_10005 (Reactome)
DHCAREACT_10064 (Reactome)
DHCAREACT_10119 (Reactome)
FABP6ArrowREACT_10078 (Reactome)
FABP6REACT_10050 (Reactome)
H+ArrowREACT_10025 (Reactome)
H+ArrowREACT_10065 (Reactome)
H+ArrowREACT_10067 (Reactome)
H+ArrowREACT_10090 (Reactome)
H+ArrowREACT_10115 (Reactome)
H+ArrowREACT_9960 (Reactome)
H+ArrowREACT_9967 (Reactome)
H+REACT_10001 (Reactome)
H+REACT_10005 (Reactome)
H+REACT_10008 (Reactome)
H+REACT_10009 (Reactome)
H+REACT_10016 (Reactome)
H+REACT_10018 (Reactome)
H+REACT_10028 (Reactome)
H+REACT_10030 (Reactome)
H+REACT_10038 (Reactome)
H+REACT_10042 (Reactome)
H+REACT_10044 (Reactome)
H+REACT_10048 (Reactome)
H+REACT_10052 (Reactome)
H+REACT_10054 (Reactome)
H+REACT_10066 (Reactome)
H+REACT_10068 (Reactome)
H+REACT_10071 (Reactome)
H+REACT_10075 (Reactome)
H+REACT_10086 (Reactome)
H+REACT_10096 (Reactome)
H+REACT_10100 (Reactome)
H+REACT_10102 (Reactome)
H+REACT_10104 (Reactome)
H+REACT_10120 (Reactome)
H+REACT_10129 (Reactome)
H+REACT_10131 (Reactome)
H+REACT_9950 (Reactome)
H+REACT_9953 (Reactome)
H+REACT_9972 (Reactome)
H+REACT_9976 (Reactome)
H+REACT_9988 (Reactome)
H+REACT_9994 (Reactome)
H2O2ArrowREACT_10003 (Reactome)
H2O2ArrowREACT_10074 (Reactome)
H2OArrowREACT_10000 (Reactome)
H2OArrowREACT_10001 (Reactome)
H2OArrowREACT_10005 (Reactome)
H2OArrowREACT_10009 (Reactome)
H2OArrowREACT_10016 (Reactome)
H2OArrowREACT_10028 (Reactome)
H2OArrowREACT_10030 (Reactome)
H2OArrowREACT_10034 (Reactome)
H2OArrowREACT_10042 (Reactome)
H2OArrowREACT_10052 (Reactome)
H2OArrowREACT_10066 (Reactome)
H2OArrowREACT_10071 (Reactome)
H2OArrowREACT_10075 (Reactome)
H2OArrowREACT_10087 (Reactome)
H2OArrowREACT_10096 (Reactome)
H2OArrowREACT_10100 (Reactome)
H2OArrowREACT_10104 (Reactome)
H2OArrowREACT_10106 (Reactome)
H2OArrowREACT_10129 (Reactome)
H2OArrowREACT_9950 (Reactome)
H2OArrowREACT_9953 (Reactome)
H2OArrowREACT_9970 (Reactome)
H2OArrowREACT_9976 (Reactome)
H2OArrowREACT_9988 (Reactome)
H2OArrowREACT_9994 (Reactome)
H2OREACT_10019 (Reactome)
H2OREACT_10061 (Reactome)
H2OREACT_10101 (Reactome)
H2OREACT_9952 (Reactome)
HSD17B4 dimermim-catalysisREACT_10019 (Reactome)
HSD17B4 dimermim-catalysisREACT_10065 (Reactome)
HSD17B4 dimermim-catalysisREACT_9952 (Reactome)
HSD17B4 dimermim-catalysisREACT_9967 (Reactome)
HSD3B7mim-catalysisREACT_10067 (Reactome)
HSD3B7mim-catalysisREACT_10090 (Reactome)
HSD3B7mim-catalysisREACT_10115 (Reactome)
NAD+REACT_10065 (Reactome)
NAD+REACT_10067 (Reactome)
NAD+REACT_10090 (Reactome)
NAD+REACT_10115 (Reactome)
NAD+REACT_9967 (Reactome)
NADHArrowREACT_10065 (Reactome)
NADHArrowREACT_10067 (Reactome)
NADHArrowREACT_10090 (Reactome)
NADHArrowREACT_10115 (Reactome)
NADHArrowREACT_9967 (Reactome)
NADP+ArrowREACT_10001 (Reactome)
NADP+ArrowREACT_10005 (Reactome)
NADP+ArrowREACT_10008 (Reactome)
NADP+ArrowREACT_10009 (Reactome)
NADP+ArrowREACT_10016 (Reactome)
NADP+ArrowREACT_10018 (Reactome)
NADP+ArrowREACT_10028 (Reactome)
NADP+ArrowREACT_10030 (Reactome)
NADP+ArrowREACT_10038 (Reactome)
NADP+ArrowREACT_10042 (Reactome)
NADP+ArrowREACT_10044 (Reactome)
NADP+ArrowREACT_10048 (Reactome)
NADP+ArrowREACT_10052 (Reactome)
NADP+ArrowREACT_10054 (Reactome)
NADP+ArrowREACT_10066 (Reactome)
NADP+ArrowREACT_10068 (Reactome)
NADP+ArrowREACT_10071 (Reactome)
NADP+ArrowREACT_10075 (Reactome)
NADP+ArrowREACT_10086 (Reactome)
NADP+ArrowREACT_10096 (Reactome)
NADP+ArrowREACT_10100 (Reactome)
NADP+ArrowREACT_10102 (Reactome)
NADP+ArrowREACT_10104 (Reactome)
NADP+ArrowREACT_10120 (Reactome)
NADP+ArrowREACT_10129 (Reactome)
NADP+ArrowREACT_10131 (Reactome)
NADP+ArrowREACT_9950 (Reactome)
NADP+ArrowREACT_9953 (Reactome)
NADP+ArrowREACT_9972 (Reactome)
NADP+ArrowREACT_9976 (Reactome)
NADP+ArrowREACT_9988 (Reactome)
NADP+ArrowREACT_9994 (Reactome)
NADP+REACT_10025 (Reactome)
NADP+REACT_9960 (Reactome)
NADPHArrowREACT_10025 (Reactome)
NADPHArrowREACT_9960 (Reactome)
NADPHREACT_10001 (Reactome)
NADPHREACT_10005 (Reactome)
NADPHREACT_10008 (Reactome)
NADPHREACT_10009 (Reactome)
NADPHREACT_10016 (Reactome)
NADPHREACT_10018 (Reactome)
NADPHREACT_10028 (Reactome)
NADPHREACT_10030 (Reactome)
NADPHREACT_10038 (Reactome)
NADPHREACT_10042 (Reactome)
NADPHREACT_10044 (Reactome)
NADPHREACT_10048 (Reactome)
NADPHREACT_10052 (Reactome)
NADPHREACT_10054 (Reactome)
NADPHREACT_10066 (Reactome)
NADPHREACT_10068 (Reactome)
NADPHREACT_10071 (Reactome)
NADPHREACT_10075 (Reactome)
NADPHREACT_10086 (Reactome)
NADPHREACT_10096 (Reactome)
NADPHREACT_10100 (Reactome)
NADPHREACT_10102 (Reactome)
NADPHREACT_10104 (Reactome)
NADPHREACT_10120 (Reactome)
NADPHREACT_10129 (Reactome)
NADPHREACT_10131 (Reactome)
NADPHREACT_9950 (Reactome)
NADPHREACT_9953 (Reactome)
NADPHREACT_9972 (Reactome)
NADPHREACT_9976 (Reactome)
NADPHREACT_9988 (Reactome)
NADPHREACT_9994 (Reactome)
Na+ArrowREACT_10050 (Reactome)
Na+ArrowREACT_9958 (Reactome)
Na+REACT_10050 (Reactome)
Na+REACT_9958 (Reactome)
O2REACT_10001 (Reactome)
O2REACT_10003 (Reactome)
O2REACT_10005 (Reactome)
O2REACT_10009 (Reactome)
O2REACT_10016 (Reactome)
O2REACT_10028 (Reactome)
O2REACT_10030 (Reactome)
O2REACT_10042 (Reactome)
O2REACT_10052 (Reactome)
O2REACT_10066 (Reactome)
O2REACT_10071 (Reactome)
O2REACT_10074 (Reactome)
O2REACT_10075 (Reactome)
O2REACT_10096 (Reactome)
O2REACT_10100 (Reactome)
O2REACT_10104 (Reactome)
O2REACT_10129 (Reactome)
O2REACT_9950 (Reactome)
O2REACT_9953 (Reactome)
O2REACT_9976 (Reactome)
O2REACT_9988 (Reactome)
O2REACT_9994 (Reactome)
PPiArrowREACT_10000 (Reactome)
PPiArrowREACT_10020 (Reactome)
PPiArrowREACT_10034 (Reactome)
PPiArrowREACT_10049 (Reactome)
PPiArrowREACT_10064 (Reactome)
PPiArrowREACT_10087 (Reactome)
PPiArrowREACT_10106 (Reactome)
PPiArrowREACT_10119 (Reactome)
PPiArrowREACT_9970 (Reactome)
PiArrowREACT_10078 (Reactome)
PiArrowREACT_10101 (Reactome)
REACT_10000 (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).
REACT_10001 (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.
REACT_10003 (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.
REACT_10005 (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.
REACT_10008 (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).
REACT_10009 (Reactome) 5beta-cholestan-3alpha, 7alpha, 12alpha-triol, NADPH + H+, and O2 react to form 5beta-cholestan-3alpha, 7alpha, 12alpha, 27-tetrol + NADP+ + H2O. This reaction occurs in the mitochondrial matrix, catalyzed by CYP27A1.
REACT_10012 (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.
REACT_10015 (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).
REACT_10016 (Reactome) 4-Cholesten-7alpha,24(S)-diol-3-one, NADPH + H+, and O2 form 4-cholesten-7-alpha,12-alpha,24(S)-triol-3-one + NADP+ + H2O. This reaction is catalyzed by sterol 12alpha hydroxylase (CYP8B1), an enzyme associated with the endoplasmic reticulum membrane. While the human gene has been cloned (Gafvels et al. 1999), its protein product has not been characterized, and the enzymatic properties of human CYP8B1 protein are inferred from those of its well-characterized rabbit homolog (Ishida et al. 1992).
REACT_10018 (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).
REACT_10019 (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.
REACT_10020 (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).
REACT_10025 (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.
REACT_10028 (Reactome) 4-Cholesten-7alpha,27-diol-3-one, NADPH + H+, and O2 form 4-Cholesten-7alpha,12alpha,27-triol-3-one + NADP+ + H2O. This reaction is catalyzed by sterol 12alpha hydroxylase (CYP8B1), an enzyme associated with the endoplasmic reticulum membrane. While the human gene has been cloned (Gafvels et al. 1999), its protein product has not been characterized, and the enzymatic properties of human CYP8B1 protein are inferred from those of its well-characterized rabbit homolog (Ishida et al. 1992).
REACT_10030 (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.
REACT_10034 (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).
REACT_10038 (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).
REACT_10042 (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.
REACT_10044 (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).
REACT_10047 (Reactome) The isomerization of 25(R) DHCA-CoA to 25(S) DHCA-CoA, catalyzed by 2-methylacyl-CoA racemase, occurs in the peroxisomal matrix.
REACT_10048 (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).
REACT_10049 (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).
REACT_10050 (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. Within the cytosol, bile salts and acids are bound to a carrier protein, FABP6 (I-BABP) (Fujita et al. 1995). Studies in a rabbit model system suggest that translocation and FABP6 binding occur as a single concerted event (Kramer et al. 1995). 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 and Boyer 2002).
REACT_10052 (Reactome) Cholesterol, NADPH + H+, and O2 form 7alpha-cholesterol (5-cholesten-3beta, 7alpha-diol), NADP+,and H2O, in a reaction catalyzed 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 (Russell 2003; Pullinger et al. 2002).
REACT_10054 (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).
REACT_10057 (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.
REACT_10061 (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).
REACT_10064 (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).
REACT_10065 (Reactome)
REACT_10066 (Reactome) 24-hydroxycholesterol, NADPH + H+, and O2 react to form cholest-5-ene-3beta,7alpha,24-triol, NADP+, and H2O. This hydroxylation reaction is catalyzed by CYP39A1 in the membrane of the endoplasmic reticulum. In the body, expression of CYP39A1 is restricted to the liver.
REACT_10067 (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).
REACT_10068 (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).
REACT_10071 (Reactome) 7-Alpha-hydroxycholest-4-en-3-one, NADPH + H+, and O2 form 7-alpha,12-alpha-dihydroxycholest-4-en-3-one + NADP+ + H2O. This reaction is catalyzed by sterol 12alpha hydroxylase (CYP8B1), an enzyme associated with the endoplasmic reticulum membrane. While the human gene has been cloned (Gafvels et al. 1999), its protein product has not been characterized, and the enzymatic properties of human CYP8B1 protein are inferred from those of its well-characterized rabbit homolog (Ishida et al. 1992).
REACT_10072 (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).
REACT_10073 (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.
REACT_10074 (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.
REACT_10075 (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.
REACT_10078 (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.
REACT_10080 (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).
REACT_10085 (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).
REACT_10086 (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).
REACT_10087 (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).
REACT_10089 (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.
REACT_10090 (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).
REACT_10091 (Reactome) A molecule of extracellular glycocholate or taurocholate is transported into the cytosol, mediated by OATP-C (SLCO1B1) in the plasma membrane. Glyco- and taurocholate exist in the blood as complexes with serum albumin, 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 glyco- and taurocholate by the liver under physiological conditions (Kullak-Ublick et al. 2004; Trauner and Boyer 2002).
REACT_10096 (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.
REACT_10097 (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).
REACT_10099 (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).
REACT_10100 (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.
REACT_10101 (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).
REACT_10102 (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).
REACT_10103 (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).
REACT_10104 (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.
REACT_10105 (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.
REACT_10106 (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).
REACT_10107 (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.
REACT_10112 (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).
REACT_10113 (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).
REACT_10115 (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).
REACT_10118 (Reactome) 3,7,24THCA-CoA is transported from the cytosol into the peroxisome.
REACT_10119 (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).
REACT_10120 (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).
REACT_10121 (Reactome) 25(R) TetraHCA-CoA is transported from the cytosol into the peroxisome.
REACT_10124 (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).
REACT_10129 (Reactome) Cholesterol, NADPH + H+, and O2 react to form 24-hydroxycholesterol , NADP+, and H2O. This reaction is catalyzed by CYP46A1 in the endoplasmic reticulum membrane. In the body, this enzyme is expressed predominantly in the brain and is thought to play a major role in cholesterol turnover there (Javitt 2002).
REACT_10130 (Reactome) Cholate is translocated from the peroxisomal matrix to the cytosol. The transporter that mediates this event is unknown.
REACT_10131 (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).
REACT_10132 (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.
REACT_9950 (Reactome) 25-hydroxycholesterol is 7alpha-hydroxylated to cholest-5-ene-3beta,7alpha,25-triol by CYP7B1.
REACT_9952 (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.
REACT_9953 (Reactome) Cholesterol, NADPH + H+, and O2 react to form 27-hydroxycholesterol, H2O, and NADP+, in the mitochondrial matrix, catalyzed by CYP27A1. 27-Hydroxycholesterol is the most abundant oxysterol in the plasma in humans; its formation is thought to play a central role in the mobilization of cholesterol from non-hepatic tissues.
REACT_9958 (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).
REACT_9960 (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.
REACT_9964 (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.
REACT_9965 (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).
REACT_9967 (Reactome)
REACT_9968 (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).
REACT_9970 (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).
REACT_9972 (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).
REACT_9974 (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).
REACT_9976 (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.
REACT_9979 (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).
REACT_9984 (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.
REACT_9985 (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).
REACT_9988 (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.
REACT_9991 (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).
REACT_9992 (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.
REACT_9994 (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).
REACT_9998 (Reactome) The isomerization of 25(R) THCA-CoA to 25(S) THCA-CoA, catalyzed by 2-methylacyl-CoA racemase, occurs in the peroxisomal matrix.
SCP2-1mim-catalysisREACT_10103 (Reactome)
SCP2-1mim-catalysisREACT_10113 (Reactome)
SLC10A1mim-catalysisREACT_9958 (Reactome)
SLC10A2mim-catalysisREACT_10050 (Reactome)
SLC27A2mim-catalysisREACT_10049 (Reactome)
SLC27A2mim-catalysisREACT_10106 (Reactome)
SLC27A2mim-catalysisREACT_10119 (Reactome)
SLC27A2mim-catalysisREACT_9970 (Reactome)
SLC27A5mim-catalysisREACT_10000 (Reactome)
SLC27A5mim-catalysisREACT_10020 (Reactome)
SLC27A5mim-catalysisREACT_10034 (Reactome)
SLC27A5mim-catalysisREACT_10064 (Reactome)
SLC27A5mim-catalysisREACT_10087 (Reactome)
SLCO1A2mim-catalysisREACT_10072 (Reactome)
SLCO1B1mim-catalysisREACT_10091 (Reactome)
SLCO1B3mim-catalysisREACT_10124 (Reactome)
THCA-CoAArrowREACT_10074 (Reactome)
THCA-CoAREACT_10019 (Reactome)
THCAArrowREACT_10001 (Reactome)
THCAREACT_10020 (Reactome)
THCAREACT_10049 (Reactome)
TetraHCAArrowREACT_10100 (Reactome)
TetraHCAREACT_10000 (Reactome)
TetraHCAREACT_10106 (Reactome)
albumin bile salt complexREACT_9958 (Reactome)
bile salts and acids ArrowREACT_10072 (Reactome)
bile salts and acids complexed with FABP6ArrowREACT_10050 (Reactome)
bile salts and acids complexed with FABP6REACT_10078 (Reactome)
bile salts and acids complexed with albuminArrowREACT_10078 (Reactome)
bile salts and acidsREACT_10050 (Reactome)
bile saltsArrowREACT_10101 (Reactome)
bile saltsArrowREACT_9958 (Reactome)
bile saltsArrowREACT_9991 (Reactome)
bile saltsREACT_10101 (Reactome)
chenodeoxycholate bile saltsArrowREACT_9968 (Reactome)
chenodeoxycholoyl-CoAArrowREACT_10103 (Reactome)
chenodeoxycholoyl-CoAREACT_9968 (Reactome)
cholate bile saltsArrowREACT_10091 (Reactome)
cholate bile saltsArrowREACT_10124 (Reactome)
cholate bile saltsArrowREACT_9974 (Reactome)
cholate; chenodeoxycholateREACT_10034 (Reactome)
cholateArrowREACT_10061 (Reactome)
choloyl-CoA; chenodeoxycholoyl-CoAArrowREACT_10034 (Reactome)
choloyl-CoA; chenodeoxycholoyl-CoAREACT_9991 (Reactome)
choloyl-CoAArrowREACT_10113 (Reactome)
choloyl-CoAREACT_10061 (Reactome)
choloyl-CoAREACT_9974 (Reactome)
glycine; taurineREACT_9968 (Reactome)
glycine; taurineREACT_9974 (Reactome)
glycine; taurineREACT_9991 (Reactome)
propionyl CoAArrowREACT_10103 (Reactome)
propionyl CoAArrowREACT_10113 (Reactome)
Retrieved from "https://classic.wikipathways.org/index.php/Pathway:WP1788"
Personal tools