Nicotinate metabolism (Homo sapiens)

From WikiPathways

Revision as of 11:15, 1 November 2018 by ReactomeTeam (Talk | contribs)
Jump to: navigation, search
224220, 488, 36, 40, 4612, 37, 38, 436, 30, 32, 4716, 399, 1711, 18, 21, 23, 2910, 5314, 31, 342, 6, 3021, 23, 294911, 21, 23, 29, 516, 30, 32, 473, 5, 3341410, 24, 35, 5218, 21, 23, 291, 6, 15, 3014, 31, 344926, 4113, 27, 284475025cytosolperoxisomal matrixnucleoplasmendoplasmic reticulum lumenmitochondrial matrixGolgi lumenH+AMPQUINPYR NAD+NADHSLC5A81,6-dh-beta-NAD PTGS2 NRNAMH2OCYP8B1 (ADP-D-ribosyl)(n)-acceptorNa+NUDT12APOA1BP dimerMg2+ PYR NT5E:Zn2+ dimerPTGIS LACT NARPPiNMNPPiATPH2OMg2+ NMRK1NCA ADPNADP+e-NADK2 Zn2+ NADP+L-Glnheme b Zn2+ H+PPi(3-)H+ATP(4-)Na+NMNAT1 CARKDH2OH2ONAADPTGS2 dimerPPi(3-)PiBUT NAADATP(4-)PARP16 PARP14 ADP(3-)PTGIS,CYP8B1adenosine5'-monophosphateNAMPTNMRK26xNMNAT1:6xZn2+(ADP-D-ribosyl)(n+1)-acceptorNAMNH2ONAMNNADSYN1 hexamerPGG2NADPHO2PPiH+ATP(4-)NCA NMNAT2 RNLS L-GluBST1 PARP10 ATP(4-)NADK:Zn2+ tetramerPGI2CH3COO- ATPNAMNMRK2FAD EtCOO- or C2H5COO- PPi(3-)monocarboxylatestransported bySLC5A8NAADADP(3-)ADP-riboseACSQPRTH2O2NNMTPRPPdh-beta-NADS-NADPHXEtCOO- or C2H5COO- PiATPPRPPAdoMetBUT RNLS:FADNCAH+PARP9 Zn2+ NRCO2H+4xNMNAT3:4xMg2+NCASLC22A13PPiNAMNT5E PiNAMNPARP4 NADSYN1 PARP8 NAD+PPi(3-)NMNAT2:Mg2+PRPPBST1 dimerNMNHPGH2NMNAT3 NAPRT1 dimerCD38PARPsAPOA1BP H+H+1,2-dh-beta-NAD H+NADK2 dimerR-NADPHXLACT CH3COO- NAD+PARP6 ATPADPNMNMg2+H2OATP(4-)NAPRT1 Histidine, lysine,phenylalanine,tyrosine, prolineand tryptophancatabolismMNANADK AdoHcyH2Omonocarboxylatestransported bySLC5A821192521212131, 45621


Description

Nicotinate (niacin) and nicotinamide are precursors of the coenzymes nicotinamide-adenine dinucleotide (NAD+) and nicotinamide-adenine dinucleotide phosphate (NADP+). When NAD+ and NADP+ are interchanged in a reaction with their reduced forms, NADH and NADPH respectively, they are important cofactors in several hundred redox reactions. Nicotinate is synthesized from 2-amino-3-carboxymuconate semialdehyde, an intermediate in the catabolism of the essential amino acid tryptophan (Magni et al. 2004). View original pathway at:Reactome.

Comments

Reactome-Converter 
Pathway is converted from Reactome ID: 196807
Reactome-version 
Reactome version: 66
Reactome Author 
Reactome Author: Jassal, Bijay

Try the New WikiPathways

View approved pathways at the new wikipathways.org.

Quality Tags

Ontology Terms

 

Bibliography

View all...
  1. Yamamoto-Katayama S, Ariyoshi M, Ishihara K, Hirano T, Jingami H, Morikawa K.; ''Crystallographic studies on human BST-1/CD157 with ADP-ribosyl cyclase and NAD glycohydrolase activities.''; PubMed Europe PMC Scholia
  2. Ohashi K, Kawai S, Murata K.; ''Identification and characterization of a human mitochondrial NAD kinase.''; PubMed Europe PMC Scholia
  3. Zhang X, Kurnasov OV, Karthikeyan S, Grishin NV, Osterman AL, Zhang H.; ''Structural characterization of a human cytosolic NMN/NaMN adenylyltransferase and implication in human NAD biosynthesis.''; PubMed Europe PMC Scholia
  4. Hamberg M, Samuelsson B.; ''Detection and isolation of an endoperoxide intermediate in prostaglandin biosynthesis.''; PubMed Europe PMC Scholia
  5. Stockbridge RB, Wolfenden R.; ''The intrinsic reactivity of ATP and the catalytic proficiencies of kinases acting on glucose, N-acetylgalactosamine, and homoserine: a thermodynamic analysis.''; PubMed Europe PMC Scholia
  6. Wada M, Yokoyama C, Hatae T, Shimonishi M, Nakamura M, Imai Y, Ullrich V, Tanabe T.; ''Purification and characterization of recombinant human prostacyclin synthase.''; PubMed Europe PMC Scholia
  7. Bahn A, Hagos Y, Reuter S, Balen D, Brzica H, Krick W, Burckhardt BC, Sabolic I, Burckhardt G.; ''Identification of a new urate and high affinity nicotinate transporter, hOAT10 (SLC22A13).''; PubMed Europe PMC Scholia
  8. Houten SM, Denis S, Te Brinke H, Jongejan A, van Kampen AH, Bradley EJ, Baas F, Hennekam RC, Millington DS, Young SP, Frazier DM, Gucsavas-Calikoglu M, Wanders RJ.; ''Mitochondrial NADP(H) deficiency due to a mutation in NADK2 causes dienoyl-CoA reductase deficiency with hyperlysinemia.''; PubMed Europe PMC Scholia
  9. Lee HC, Graeff R, Walseth TF.; ''Cyclic ADP-ribose and its metabolic enzymes.''; PubMed Europe PMC Scholia
  10. Misumi Y, Ogata S, Ohkubo K, Hirose S, Ikehara Y.; ''Primary structure of human placental 5'-nucleotidase and identification of the glycolipid anchor in the mature form.''; PubMed Europe PMC Scholia
  11. Ritter M, Buechler C, Boettcher A, Barlage S, Schmitz-Madry A, Orsó E, Bared SM, Schmiedeknecht G, Baehr CH, Fricker G, Schmitz G.; ''Cloning and characterization of a novel apolipoprotein A-I binding protein, AI-BP, secreted by cells of the kidney proximal tubules in response to HDL or ApoA-I.''; PubMed Europe PMC Scholia
  12. Sorci L, Cimadamore F, Scotti S, Petrelli R, Cappellacci L, Franchetti P, Orsomando G, Magni G.; ''Initial-rate kinetics of human NMN-adenylyltransferases: substrate and metal ion specificity, inhibition by products and multisubstrate analogues, and isozyme contributions to NAD+ biosynthesis.''; PubMed Europe PMC Scholia
  13. Magni G, Amici A, Emanuelli M, Orsomando G, Raffaelli N, Ruggieri S.; ''Enzymology of NAD+ homeostasis in man.''; PubMed Europe PMC Scholia
  14. Tempel W, Rabeh WM, Bogan KL, Belenky P, Wojcik M, Seidle HF, Nedyalkova L, Yang T, Sauve AA, Park HW, Brenner C.; ''Nicotinamide riboside kinase structures reveal new pathways to NAD+.''; PubMed Europe PMC Scholia
  15. Di Paola S, Micaroni M, Di Tullio G, Buccione R, Di Girolamo M.; ''PARP16/ARTD15 is a novel endoplasmic-reticulum-associated mono-ADP-ribosyltransferase that interacts with, and modifies karyopherin-ß1.''; PubMed Europe PMC Scholia
  16. Yan Q, Xu R, Zhu L, Cheng X, Wang Z, Manis J, Shipp MA.; ''BAL1 and its partner E3 ligase, BBAP, link Poly(ADP-ribose) activation, ubiquitylation, and double-strand DNA repair independent of ATM, MDC1, and RNF8.''; PubMed Europe PMC Scholia
  17. Beaupre BA, Hoag MR, Roman J, Försterling FH, Moran GR.; ''Metabolic function for human renalase: oxidation of isomeric forms of β-NAD(P)H that are inhibitory to primary metabolism.''; PubMed Europe PMC Scholia
  18. Berger F, Lau C, Dahlmann M, Ziegler M.; ''Subcellular compartmentation and differential catalytic properties of the three human nicotinamide mononucleotide adenylyltransferase isoforms.''; PubMed Europe PMC Scholia
  19. Yu M, Schreek S, Cerni C, Schamberger C, Lesniewicz K, Poreba E, Vervoorts J, Walsemann G, Grötzinger J, Kremmer E, Mehraein Y, Mertsching J, Kraft R, Austen M, Lüscher-Firzlaff J, Lüscher B.; ''PARP-10, a novel Myc-interacting protein with poly(ADP-ribose) polymerase activity, inhibits transformation.''; PubMed Europe PMC Scholia
  20. Yalowitz JA, Xiao S, Biju MP, Antony AC, Cummings OW, Deeg MA, Jayaram HN.; ''Characterization of human brain nicotinamide 5'-mononucleotide adenylyltransferase-2 and expression in human pancreas.''; PubMed Europe PMC Scholia
  21. Thompson LF, Ruedi JM, Low MG.; ''Purification of 5'-nucleotidase from human placenta after release from plasma membranes by phosphatidylinositol-specific phospholipase C.''; PubMed Europe PMC Scholia
  22. Kraus D, Yang Q, Kong D, Banks AS, Zhang L, Rodgers JT, Pirinen E, Pulinilkunnil TC, Gong F, Wang YC, Cen Y, Sauve AA, Asara JM, Peroni OD, Monia BP, Bhanot S, Alhonen L, Puigserver P, Kahn BB.; ''Nicotinamide N-methyltransferase knockdown protects against diet-induced obesity.''; PubMed Europe PMC Scholia
  23. Lee HC.; ''Cyclic ADP-ribose and nicotinic acid adenine dinucleotide phosphate (NAADP) as messengers for calcium mobilization.''; PubMed Europe PMC Scholia
  24. Moreschi I, Bruzzone S, Melone L, De Flora A, Zocchi E.; ''NAADP+ synthesis from cADPRP and nicotinic acid by ADP-ribosyl cyclases.''; PubMed Europe PMC Scholia
  25. Li J, Mayne R, Wu C.; ''A novel muscle-specific beta 1 integrin binding protein (MIBP) that modulates myogenic differentiation.''; PubMed Europe PMC Scholia
  26. Aksoy S, Brandriff BF, Ward A, Little PF, Weinshilboum RM.; ''Human nicotinamide N-methyltransferase gene: molecular cloning, structural characterization and chromosomal localization.''; PubMed Europe PMC Scholia
  27. Barnett J, Chow J, Ives D, Chiou M, Mackenzie R, Osen E, Nguyen B, Tsing S, Bach C, Freire J.; ''Purification, characterization and selective inhibition of human prostaglandin G/H synthase 1 and 2 expressed in the baculovirus system.''; PubMed Europe PMC Scholia
  28. Milani M, Ciriello F, Baroni S, Pandini V, Canevari G, Bolognesi M, Aliverti A.; ''FAD-binding site and NADP reactivity in human renalase: a new enzyme involved in blood pressure regulation.''; PubMed Europe PMC Scholia
  29. Miyauchi S, Gopal E, Fei YJ, Ganapathy V.; ''Functional identification of SLC5A8, a tumor suppressor down-regulated in colon cancer, as a Na(+)-coupled transporter for short-chain fatty acids.''; PubMed Europe PMC Scholia
  30. Bieganowski P, Brenner C.; ''Discoveries of nicotinamide riboside as a nutrient and conserved NRK genes establish a Preiss-Handler independent route to NAD+ in fungi and humans.''; PubMed Europe PMC Scholia
  31. Lee HC, Munshi C, Graeff R.; ''Structures and activities of cyclic ADP-ribose, NAADP and their metabolic enzymes.''; PubMed Europe PMC Scholia
  32. Dong L, Vecchio AJ, Sharma NP, Jurban BJ, Malkowski MG, Smith WL.; ''Human cyclooxygenase-2 is a sequence homodimer that functions as a conformational heterodimer.''; PubMed Europe PMC Scholia
  33. Swinney DC, Mak AY, Barnett J, Ramesha CS.; ''Differential allosteric regulation of prostaglandin H synthase 1 and 2 by arachidonic acid.''; PubMed Europe PMC Scholia
  34. Zhou T, Kurnasov O, Tomchick DR, Binns DD, Grishin NV, Marquez VE, Osterman AL, Zhang H.; ''Structure of human nicotinamide/nicotinic acid mononucleotide adenylyltransferase. Basis for the dual substrate specificity and activation of the oncolytic agent tiazofurin.''; PubMed Europe PMC Scholia
  35. Peters JC.; ''Tryptophan nutrition and metabolism: an overview.''; PubMed Europe PMC Scholia
  36. Hara N, Yamada K, Terashima M, Osago H, Shimoyama M, Tsuchiya M.; ''Molecular identification of human glutamine- and ammonia-dependent NAD synthetases. Carbon-nitrogen hydrolase domain confers glutamine dependency.''; PubMed Europe PMC Scholia
  37. Hara N, Yamada K, Shibata T, Osago H, Hashimoto T, Tsuchiya M.; ''Elevation of cellular NAD levels by nicotinic acid and involvement of nicotinic acid phosphoribosyltransferase in human cells.''; PubMed Europe PMC Scholia
  38. Marbaix AY, Noël G, Detroux AM, Vertommen D, Van Schaftingen E, Linster CL.; ''Extremely conserved ATP- or ADP-dependent enzymatic system for nicotinamide nucleotide repair.''; PubMed Europe PMC Scholia
  39. PREISS J, HANDLER P.; ''Biosynthesis of diphosphopyridine nucleotide. II. Enzymatic aspects.''; PubMed Europe PMC Scholia
  40. Sasiak K, Saunders PP.; ''Purification and properties of a human nicotinamide ribonucleoside kinase.''; PubMed Europe PMC Scholia
  41. Coady MJ, Chang MH, Charron FM, Plata C, Wallendorff B, Sah JF, Markowitz SD, Romero MF, Lapointe JY.; ''The human tumour suppressor gene SLC5A8 expresses a Na+-monocarboxylate cotransporter.''; PubMed Europe PMC Scholia
  42. Fukuoka SI, Nyaruhucha CM, Shibata K.; ''Characterization and functional expression of the cDNA encoding human brain quinolinate phosphoribosyltransferase.''; PubMed Europe PMC Scholia
  43. Hla T, Neilson K.; ''Human cyclooxygenase-2 cDNA.''; PubMed Europe PMC Scholia
  44. Nikiforov A, Dölle C, Niere M, Ziegler M.; ''Pathways and subcellular compartmentation of NAD biosynthesis in human cells: from entry of extracellular precursors to mitochondrial NAD generation.''; PubMed Europe PMC Scholia
  45. Raffaelli N, Sorci L, Amici A, Emanuelli M, Mazzola F, Magni G.; ''Identification of a novel human nicotinamide mononucleotide adenylyltransferase.''; PubMed Europe PMC Scholia
  46. Aksoy S, Szumlanski CL, Weinshilboum RM.; ''Human liver nicotinamide N-methyltransferase. cDNA cloning, expression, and biochemical characterization.''; PubMed Europe PMC Scholia
  47. Zimmermann H.; ''5'-Nucleotidase: molecular structure and functional aspects.''; PubMed Europe PMC Scholia
  48. Lerner F, Niere M, Ludwig A, Ziegler M.; ''Structural and functional characterization of human NAD kinase.''; PubMed Europe PMC Scholia
  49. Samal B, Sun Y, Stearns G, Xie C, Suggs S, McNiece I.; ''Cloning and characterization of the cDNA encoding a novel human pre-B-cell colony-enhancing factor.''; PubMed Europe PMC Scholia
  50. Schweiger M, Hennig K, Lerner F, Niere M, Hirsch-Kauffmann M, Specht T, Weise C, Oei SL, Ziegler M.; ''Characterization of recombinant human nicotinamide mononucleotide adenylyl transferase (NMNAT), a nuclear enzyme essential for NAD synthesis.''; PubMed Europe PMC Scholia
  51. Niedel J, Dietrich LS.; ''Nicotinate phosphoribosyltransferase of human erythrocytes. Purification and properties.''; PubMed Europe PMC Scholia
  52. Chlopicki S, Swies J, Mogielnicki A, Buczko W, Bartus M, Lomnicka M, Adamus J, Gebicki J.; ''1-Methylnicotinamide (MNA), a primary metabolite of nicotinamide, exerts anti-thrombotic activity mediated by a cyclooxygenase-2/prostacyclin pathway.''; PubMed Europe PMC Scholia
  53. Abdelraheim SR, Spiller DG, McLennan AG.; ''Mammalian NADH diphosphatases of the Nudix family: cloning and characterization of the human peroxisomal NUDT12 protein.''; PubMed Europe PMC Scholia
  54. Garavaglia S, Bruzzone S, Cassani C, Canella L, Allegrone G, Sturla L, Mannino E, Millo E, De Flora A, Rizzi M.; ''The high-resolution crystal structure of periplasmic Haemophilus influenzae NAD nucleotidase reveals a novel enzymatic function of human CD73 related to NAD metabolism.''; PubMed Europe PMC Scholia

History

View all...
CompareRevisionActionTimeUserComment
114689view16:16, 25 January 2021ReactomeTeamReactome version 75
113135view11:20, 2 November 2020ReactomeTeamReactome version 74
112366view15:29, 9 October 2020ReactomeTeamReactome version 73
101268view11:15, 1 November 2018ReactomeTeamreactome version 66
100806view20:44, 31 October 2018ReactomeTeamreactome version 65
100348view19:21, 31 October 2018ReactomeTeamreactome version 64
99893view16:04, 31 October 2018ReactomeTeamreactome version 63
99450view14:37, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
93524view11:26, 9 August 2017ReactomeTeamNew pathway

External references

DataNodes

View all...
NameTypeDatabase referenceComment
(ADP-D-ribosyl)(n)-acceptorMetaboliteCHEBI:133202 (ChEBI)
(ADP-D-ribosyl)(n+1)-acceptorMetaboliteCHEBI:133203 (ChEBI)
1,2-dh-beta-NAD MetaboliteCHEBI:90171 (ChEBI)
1,6-dh-beta-NAD MetaboliteCHEBI:90174 (ChEBI)
4xNMNAT3:4xMg2+ComplexR-HSA-200487 (Reactome)
6xNMNAT1:6xZn2+ComplexR-HSA-200489 (Reactome)
ACSMetaboliteCHEBI:29044 (ChEBI)
ADP(3-)MetaboliteCHEBI:456216 (ChEBI)
ADP-riboseMetaboliteCHEBI:57967 (ChEBI)
ADPMetaboliteCHEBI:16761 (ChEBI)
AMPMetaboliteCHEBI:16027 (ChEBI)
APOA1BP ProteinQ8NCW5 (Uniprot-TrEMBL)
APOA1BP dimerComplexR-HSA-6807487 (Reactome)
ATP(4-)MetaboliteCHEBI:30616 (ChEBI) ATP(4-) is the major ionization state of ATP at pH 7.2 (Stockbridge & Wolfenden 2009).
ATPMetaboliteCHEBI:15422 (ChEBI)
AdoHcyMetaboliteCHEBI:16680 (ChEBI)
AdoMetMetaboliteCHEBI:15414 (ChEBI)
BST1 ProteinQ10588 (Uniprot-TrEMBL)
BST1 dimerComplexR-HSA-8870344 (Reactome)
BUT MetaboliteCHEBI:30772 (ChEBI)
CARKDProteinQ8IW45 (Uniprot-TrEMBL)
CD38ProteinP28907 (Uniprot-TrEMBL)
CH3COO- MetaboliteCHEBI:15366 (ChEBI)
CO2MetaboliteCHEBI:16526 (ChEBI)
CYP8B1 ProteinQ9UNU6 (Uniprot-TrEMBL)
EtCOO- or C2H5COO- MetaboliteCHEBI:30768 (ChEBI)
FAD MetaboliteCHEBI:16238 (ChEBI)
H+MetaboliteCHEBI:15378 (ChEBI)
H2O2MetaboliteCHEBI:16240 (ChEBI)
H2OMetaboliteCHEBI:15377 (ChEBI)
Histidine, lysine,

phenylalanine, tyrosine, proline and tryptophan

catabolism
PathwayR-HSA-6788656 (Reactome) The catabolic pathways of histidine, lysine, phenylalanine, tyrosine, proline and tryptophan are described in this section (Berg et al. 2002).
L-GlnMetaboliteCHEBI:58359 (ChEBI)
L-GluMetaboliteCHEBI:29985 (ChEBI)
LACT MetaboliteCHEBI:422 (ChEBI)
MNAMetaboliteCHEBI:16797 (ChEBI)
Mg2+ MetaboliteCHEBI:18420 (ChEBI)
Mg2+MetaboliteCHEBI:18420 (ChEBI)
NAADMetaboliteCHEBI:18304 (ChEBI)
NAD+MetaboliteCHEBI:15846 (ChEBI)
NADHMetaboliteCHEBI:16908 (ChEBI)
NADK ProteinO95544 (Uniprot-TrEMBL)
NADK2 ProteinQ4G0N4 (Uniprot-TrEMBL)
NADK2 dimerComplexR-HSA-8955031 (Reactome)
NADK:Zn2+ tetramerComplexR-HSA-197222 (Reactome)
NADP+MetaboliteCHEBI:18009 (ChEBI)
NADPHMetaboliteCHEBI:16474 (ChEBI)
NADSYN1 ProteinQ6IA69 (Uniprot-TrEMBL)
NADSYN1 hexamerComplexR-HSA-197192 (Reactome)
NAMMetaboliteCHEBI:17154 (ChEBI)
NAMNMetaboliteCHEBI:15763 (ChEBI)
NAMPTProteinP43490 (Uniprot-TrEMBL)
NAPRT1 ProteinQ6XQN6 (Uniprot-TrEMBL)
NAPRT1 dimerComplexR-HSA-389377 (Reactome)
NARMetaboliteCHEBI:58527 (ChEBI)
NCA MetaboliteCHEBI:15940 (ChEBI)
NCA MetaboliteCHEBI:32544 (ChEBI)
NCAMetaboliteCHEBI:15940 (ChEBI)
NCAMetaboliteCHEBI:32544 (ChEBI)
NMNAT1 ProteinQ9HAN9 (Uniprot-TrEMBL)
NMNAT2 ProteinQ9BZQ4 (Uniprot-TrEMBL)
NMNAT2:Mg2+ComplexR-HSA-197266 (Reactome)
NMNAT3 ProteinQ96T66 (Uniprot-TrEMBL)
NMNMetaboliteCHEBI:14649 (ChEBI)
NMNHMetaboliteCHEBI:74452 (ChEBI)
NMRK1ProteinQ9NWW6 (Uniprot-TrEMBL)
NMRK2ProteinQ9NPI5 (Uniprot-TrEMBL)
NNMTProteinP40261 (Uniprot-TrEMBL)
NRMetaboliteCHEBI:15927 (ChEBI)
NRNAMMetaboliteCHEBI:15927 (ChEBI)
NT5E ProteinP21589 (Uniprot-TrEMBL)
NT5E:Zn2+ dimerComplexR-HSA-109266 (Reactome)
NUDT12ProteinQ9BQG2 (Uniprot-TrEMBL)
Na+MetaboliteCHEBI:29101 (ChEBI)
O2MetaboliteCHEBI:15379 (ChEBI)
PARP10 ProteinQ53GL7 (Uniprot-TrEMBL)
PARP14 ProteinQ460N5 (Uniprot-TrEMBL)
PARP16 ProteinQ8N5Y8 (Uniprot-TrEMBL)
PARP4 ProteinQ9UKK3 (Uniprot-TrEMBL)
PARP6 ProteinQ2NL67 (Uniprot-TrEMBL)
PARP8 ProteinQ8N3A8 (Uniprot-TrEMBL)
PARP9 ProteinQ8IXQ6 (Uniprot-TrEMBL)
PARPsComplexR-HSA-8938273 (Reactome)
PGG2MetaboliteCHEBI:27647 (ChEBI)
PGH2MetaboliteCHEBI:15554 (ChEBI)
PGI2MetaboliteCHEBI:15552 (ChEBI)
PPi(3-)MetaboliteCHEBI:33019 (ChEBI)
PPiMetaboliteCHEBI:29888 (ChEBI)
PRPPMetaboliteCHEBI:17111 (ChEBI)
PTGIS ProteinQ16647 (Uniprot-TrEMBL)
PTGIS,CYP8B1ComplexR-HSA-3222410 (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.
PTGS2 ProteinP35354 (Uniprot-TrEMBL)
PTGS2 dimerComplexR-HSA-140491 (Reactome)
PYR MetaboliteCHEBI:32816 (ChEBI)
PiMetaboliteCHEBI:18367 (ChEBI)
QPRTProteinQ15274 (Uniprot-TrEMBL)
QUINMetaboliteCHEBI:46828 (ChEBI)
R-NADPHXMetaboliteCHEBI:64085 (ChEBI)
RNLS ProteinQ5VYX0 (Uniprot-TrEMBL)
RNLS:FADComplexR-HSA-8956472 (Reactome)
S-NADPHXMetaboliteCHEBI:64084 (ChEBI)
SLC22A13ProteinQ9Y226 (Uniprot-TrEMBL)
SLC5A8ProteinQ8N695 (Uniprot-TrEMBL)
Zn2+ MetaboliteCHEBI:29105 (ChEBI)
adenosine 5'-monophosphateMetaboliteCHEBI:16027 (ChEBI)
dh-beta-NADComplexR-ALL-8956473 (Reactome)
e-MetaboliteCHEBI:10545 (ChEBI)
heme b MetaboliteCHEBI:26355 (ChEBI)
monocarboxylates

transported by

SLC5A8
ComplexR-ALL-429739 (Reactome)
monocarboxylates

transported by

SLC5A8
ComplexR-ALL-429748 (Reactome)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
(ADP-D-ribosyl)(n)-acceptorR-HSA-8938073 (Reactome)
(ADP-D-ribosyl)(n+1)-acceptorArrowR-HSA-8938073 (Reactome)
4xNMNAT3:4xMg2+mim-catalysisR-HSA-200474 (Reactome)
6xNMNAT1:6xZn2+mim-catalysisR-HSA-200512 (Reactome)
ACSR-HSA-197187 (Reactome)
ADP(3-)ArrowR-HSA-8869606 (Reactome)
ADP(3-)ArrowR-HSA-8869607 (Reactome)
ADP(3-)ArrowR-HSA-8869627 (Reactome)
ADP(3-)ArrowR-HSA-8869633 (Reactome)
ADP-riboseArrowR-HSA-8870346 (Reactome)
ADP-riboseArrowR-HSA-8938076 (Reactome)
ADPArrowR-HSA-197198 (Reactome)
ADPArrowR-HSA-6806967 (Reactome)
ADPArrowR-HSA-8955030 (Reactome)
AMPArrowR-HSA-197271 (Reactome)
APOA1BP dimermim-catalysisR-HSA-6806966 (Reactome)
ATP(4-)R-HSA-197235 (Reactome)
ATP(4-)R-HSA-200474 (Reactome)
ATP(4-)R-HSA-200512 (Reactome)
ATP(4-)R-HSA-8869606 (Reactome)
ATP(4-)R-HSA-8869607 (Reactome)
ATP(4-)R-HSA-8869627 (Reactome)
ATP(4-)R-HSA-8869633 (Reactome)
ATP(4-)R-HSA-8939959 (Reactome)
ATPR-HSA-197198 (Reactome)
ATPR-HSA-197271 (Reactome)
ATPR-HSA-6806967 (Reactome)
ATPR-HSA-8955030 (Reactome)
AdoHcyArrowR-HSA-5359451 (Reactome)
AdoMetR-HSA-5359451 (Reactome)
BST1 dimermim-catalysisR-HSA-8870346 (Reactome)
CARKDmim-catalysisR-HSA-6806967 (Reactome)
CD38mim-catalysisR-HSA-8938076 (Reactome)
CO2ArrowR-HSA-197268 (Reactome)
H+ArrowR-HSA-6806967 (Reactome)
H+ArrowR-HSA-6809287 (Reactome)
H+ArrowR-HSA-8869606 (Reactome)
H+ArrowR-HSA-8869607 (Reactome)
H+ArrowR-HSA-8869627 (Reactome)
H+ArrowR-HSA-8869633 (Reactome)
H+ArrowR-HSA-8870346 (Reactome)
H+ArrowR-HSA-8938076 (Reactome)
H+ArrowR-HSA-8955030 (Reactome)
H+R-HSA-197186 (Reactome)
H+R-HSA-197268 (Reactome)
H+R-HSA-2309773 (Reactome)
H+R-HSA-8956458 (Reactome)
H2O2ArrowR-HSA-8956458 (Reactome)
H2OArrowR-HSA-197187 (Reactome)
H2OArrowR-HSA-2309773 (Reactome)
H2OR-HSA-197271 (Reactome)
H2OR-HSA-6809287 (Reactome)
H2OR-HSA-8870346 (Reactome)
H2OR-HSA-8938076 (Reactome)
H2OR-HSA-8940070 (Reactome)
H2OR-HSA-8940074 (Reactome)
L-GlnR-HSA-197271 (Reactome)
L-GluArrowR-HSA-197271 (Reactome)
MNAArrowR-HSA-2309773 (Reactome)
MNAArrowR-HSA-5359451 (Reactome)
Mg2+ArrowR-HSA-197186 (Reactome)
NAADArrowR-HSA-197235 (Reactome)
NAADArrowR-HSA-200474 (Reactome)
NAADArrowR-HSA-200512 (Reactome)
NAADR-HSA-197271 (Reactome)
NAD+ArrowR-HSA-197271 (Reactome)
NAD+ArrowR-HSA-8939959 (Reactome)
NAD+ArrowR-HSA-8956458 (Reactome)
NAD+R-HSA-197198 (Reactome)
NAD+R-HSA-8870346 (Reactome)
NAD+R-HSA-8938073 (Reactome)
NAD+R-HSA-8938076 (Reactome)
NAD+R-HSA-8940070 (Reactome)
NAD+R-HSA-8955030 (Reactome)
NADHR-HSA-6809287 (Reactome)
NADK2 dimermim-catalysisR-HSA-8955030 (Reactome)
NADK:Zn2+ tetramermim-catalysisR-HSA-197198 (Reactome)
NADP+ArrowR-HSA-197198 (Reactome)
NADP+ArrowR-HSA-8955030 (Reactome)
NADPHArrowR-HSA-6806967 (Reactome)
NADSYN1 hexamermim-catalysisR-HSA-197271 (Reactome)
NAMArrowR-HSA-8870346 (Reactome)
NAMArrowR-HSA-8938073 (Reactome)
NAMArrowR-HSA-8938076 (Reactome)
NAMNArrowR-HSA-197186 (Reactome)
NAMNArrowR-HSA-197250 (Reactome)
NAMNArrowR-HSA-197268 (Reactome)
NAMNArrowR-HSA-8869606 (Reactome)
NAMNArrowR-HSA-8869607 (Reactome)
NAMNR-HSA-197235 (Reactome)
NAMNR-HSA-200474 (Reactome)
NAMNR-HSA-200512 (Reactome)
NAMPTmim-catalysisR-HSA-197250 (Reactome)
NAMR-HSA-197250 (Reactome)
NAMR-HSA-5359451 (Reactome)
NAPRT1 dimermim-catalysisR-HSA-197186 (Reactome)
NARR-HSA-8869606 (Reactome)
NARR-HSA-8869607 (Reactome)
NCAArrowR-HSA-8869603 (Reactome)
NCAR-HSA-197186 (Reactome)
NCAR-HSA-8869603 (Reactome)
NMNAT2:Mg2+mim-catalysisR-HSA-197235 (Reactome)
NMNAT2:Mg2+mim-catalysisR-HSA-8939959 (Reactome)
NMNArrowR-HSA-8869627 (Reactome)
NMNArrowR-HSA-8869633 (Reactome)
NMNArrowR-HSA-8940070 (Reactome)
NMNHArrowR-HSA-6809287 (Reactome)
NMNR-HSA-8939959 (Reactome)
NMNR-HSA-8940074 (Reactome)
NMRK1mim-catalysisR-HSA-8869606 (Reactome)
NMRK1mim-catalysisR-HSA-8869633 (Reactome)
NMRK2mim-catalysisR-HSA-8869607 (Reactome)
NMRK2mim-catalysisR-HSA-8869627 (Reactome)
NNMTmim-catalysisR-HSA-5359451 (Reactome)
NRNAMArrowR-HSA-8940074 (Reactome)
NRR-HSA-8869627 (Reactome)
NRR-HSA-8869633 (Reactome)
NT5E:Zn2+ dimermim-catalysisR-HSA-8940070 (Reactome)
NT5E:Zn2+ dimermim-catalysisR-HSA-8940074 (Reactome)
NUDT12mim-catalysisR-HSA-6809287 (Reactome)
Na+ArrowR-HSA-429749 (Reactome)
Na+R-HSA-429749 (Reactome)
O2R-HSA-8956458 (Reactome)
PARPsmim-catalysisR-HSA-8938073 (Reactome)
PGG2R-HSA-2309773 (Reactome)
PGH2ArrowR-HSA-2309773 (Reactome)
PGH2R-HSA-76496 (Reactome)
PGI2ArrowR-HSA-76496 (Reactome)
PPi(3-)ArrowR-HSA-197235 (Reactome)
PPi(3-)ArrowR-HSA-200474 (Reactome)
PPi(3-)ArrowR-HSA-200512 (Reactome)
PPi(3-)ArrowR-HSA-8939959 (Reactome)
PPiArrowR-HSA-197186 (Reactome)
PPiArrowR-HSA-197250 (Reactome)
PPiArrowR-HSA-197268 (Reactome)
PPiArrowR-HSA-197271 (Reactome)
PRPPR-HSA-197186 (Reactome)
PRPPR-HSA-197250 (Reactome)
PRPPR-HSA-197268 (Reactome)
PTGIS,CYP8B1mim-catalysisR-HSA-76496 (Reactome)
PTGS2 dimermim-catalysisR-HSA-2309773 (Reactome)
PiArrowR-HSA-6806967 (Reactome)
PiArrowR-HSA-8940070 (Reactome)
PiArrowR-HSA-8940074 (Reactome)
QPRTmim-catalysisR-HSA-197268 (Reactome)
QUINArrowR-HSA-197187 (Reactome)
QUINR-HSA-197268 (Reactome)
R-HSA-197186 (Reactome) Cytosolic nicotinate phosphoribosyltransferase (NaPRT) catalyzes the Mg++-dependent reaction of nicotinate and phosphoribosyl pyrophosphate to form nicotinate mononucleotide (NaMN, nicotinate D-ribonucleotide) and pyrophosphate. The active form of the enzyme is a homodimer (Preiss and Handler 1958; Niedel and Dietrich 1973; Hara et al. 2007).
R-HSA-197187 (Reactome) Cytosolic 2-amino 3-carboxymuconate semialdehyde reacts non-enzymatically to form quinolinate and water (Fukuoka et al. 1998).
R-HSA-197198 (Reactome) Cytosolic NAD+ kinase (NADK) catalyses the transfer of a phosphate group from ATP to NAD+, forming NADP+. This is the only way to generate NADP+ in all living organisms. NADK is tetrameric and requires one divalent metal such as Zn2+ per subunit to function correctly (Lerner et al. 2004).
R-HSA-197235 (Reactome) NMNAT2 catalyzes the reaction of nicotinate D-ribonucleotide and ATP to form deamino-NAD+ (nicotinate adenine dinucleotide) and pyrophosphate (Sorci et al. 2007). The active form of the enzyme is a monomer in vitro; Mg2+ is required for activity (Raffaelli et al. 2002; Sorci et al. 2007). Although the predicted amino acid sequence of the enzyme lacks an obvious signal sequence or transmembrane domain (Yalowitz et al. 2004), recombinant FLAG-tagged protein expressed in HeLa cells localizes predominantly to the Golgi apparatus (Berger et al. 2005). Its localization within the Golgi apparatus is unknown and the annotation here is based on the plausible but speculative assumption that the enzyme is associated with the Gogi membrane and accessible from the cytosol. Immunostaining studies indicate that the protein is abundant in Islets of Langerhans and in several regions of the brain (Yalowitz et al. 2004).
R-HSA-197250 (Reactome) Nicotinamide phosphoribosyltransferase (NamPRT) catalyzes the condensation of nicotinamide with 5- phosphoribosyl-1-pyrophosphate to yield nicotinamide D-ribonucleotide (NMN), an intermediate in the biosynthesis of NAD. It is the rate limiting component in the mammalian NAD biosynthesis pathway.
R-HSA-197268 (Reactome) The enzyme, nicotinate nucleotide pyrophosphorylase, is specific for quinolinate. Its activity is strictly dependent on Mg2+ ions being present. A phosphoribosyl group is transferred to quinolinate to form nicotinate D-ribonucleotide. This reaction represents another rate-limiting step of the pathway from tryptophan to NAD+.
R-HSA-197271 (Reactome) NAD synthases 1 and 2 (NADSYN1 and NADSYN2) catalyse the final step in the biosynthesis of NAD+, both in de novo synthesis and in the salvage pathway. The enzymes makes use of an amide donor in the reaction. NADSYNs exist as a homohexamers in the cytosol. The major difference between the two forms is that NADSYN1 appears to be glutamine-dependent whereas NADSYN2 is strictly ammonia-dependent (Hara et al. 2003).
R-HSA-200474 (Reactome) NMNAT3 catalyzes the reaction of nicotinate D-ribonucleotide and ATP to form deamino-NAD+ (nicotinate adenine dinucleotide) and pyrophosphate (Sorci et al. 2007). The active form of the enzyme is a tetramer in vitro (Zhang et al. 2003). Recombinant FLAG-tagged protein expressed in HeLa cells localizes both to the cytosol and to mitochondria (Berger et al. 2005). The cytosolic protein is annotated here.
R-HSA-200512 (Reactome) NMNAT1 catalyzes the reaction of nicotinate D-ribonucleotide and ATP to form deamino-NAD+ (nicotinate adenine dinucleotide) and pyrophosphate (Schweiger et al. 2001). The active form of the enzyme in vitro is a hexamer (Zhou et al. 2002), and its activity is substantially greater in the presence of Zn++ than of Mg++ (Sorci et al. 2007). The predicted amino acid sequence of the enzyme contains a nuclear localization domain and the protein is observed to localize to the nucleus (Schweiger et al. 2001; Berger et al. 2005).
R-HSA-2309773 (Reactome) Prostaglandin G/H synthase 2 (PTGS2) exhibits a dual catalytic activity, a cyclooxygenase and a peroxidase. The peroxidase function converts prostaglandin G2 (PGG2) to prostaglandin H2 (PGH2) via a two-electron reduction (Hamberg et al. 1973, Hla & Neilson 1992, Swinney et al. 1997, Barnett et al. 1994).
R-HSA-429749 (Reactome) The human tumour suppressor gene SLC5A8 encodes sodium-coupled monocarboxylate transporter 1, SMCT1 (also called AIT) and is abundantly expressed in the colon (Coady et al. 2004, Myauchi et al. 2004). When the human protein is expressed in Xenopus oocytes, it was found to transport small monocarboxylates and carboxylate drugs, co-transporting Na+ ions electrogenically (3 Na+ ions co-transported with 1 carboxylate).
R-HSA-5359451 (Reactome) Nicotinamide N-methyltransferase (NNMT) is a cytosolic protein which catalyses the N-methylation of nicotinamide (NAM aka vitamin B3) and other pyridines (Aksoy et al. 1994, 1995). It is mainly expressed in the liver and to a lesser extent in the kidney, lung, skeletal muscle, placenta and heart. NAM is a precursor for NAD+, an important cofactor in cellular redox states and energy metabolism. NNMT methylates NAM using S-adenosylmethionine (SAM) as the methyl donor to form 1-methylnicotinamide (MNA). Kraus et al. found Nnmt expression is increased in white adipose tissue and liver of obese and diabetic mice. An Nnmt knockdown stategy could protect against diet-induced obesity by increasing cellular energy expenditure thus could be a target for treating obesity and type 2 diabetes (Kraus et al. 2014). Experiments on rats with thrombolytic models suggest endogenous MNA could be a stimulator of the COX2/PGI2 pathway and thus regulate an anti-thrombotic effect (Chlopicki et al. 2007).
R-HSA-6806966 (Reactome) NAD(P)H-hydrate epimerase (APOA1BP) is a homodimeric protein located in the mitochondrion (Ritter et al. 2002). Mammalian APOA1BP is able to mediate the epimerisation of the R-form of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration (Marbaix et al. 2011). This is a prerequisite for the S-specific NAD(P)H-hydrate dehydratase to allow the repair of both epimers of NAD(P)HX.
R-HSA-6806967 (Reactome) Human ATP-dependent (S)-NAD(P)H-hydrate dehydratase (CARKD) is thought to catalyze the dehydration, and thus repair, of the S-form of NAD(P)HX, a damaged form of NAD(P)H that is a result of enzymatic or heat-dependent hydration. The human event is deduced on the basis of evidence from mouse experiments (Marbaix et al. 2011).
R-HSA-6809287 (Reactome) The human nudix hydrolase peroxisomal NADH pyrophosphatase (NUDT12) shows in vitro hydrolase activity towards NAD(P)H, NAD(P)+, ADP-ribose and diadenosine triphosphate. Like other NADH diphosphatases of the Nudix family, NUDT12 has a marked substrate preference for reduced nicotinamide nucleotides. It can hydrolyse NAD(H) to the nicotinamide mononucleotide NMN(H) and may act to regulate the concentration of peroxisomal nicotinamide nucleotide cofactors required for oxidative metabolism here (Abdelraheim et al. 2003).
R-HSA-76496 (Reactome) Prostacyclin synthase (PTGIS) aka CYP8A1 mediates the isomerisation of prostaglandin H2 (PGH2) to prostaglandin I2 (PGI2) aka prostacyclin (Wada et al. 2004). This reaction is not coupled with any P450 reductase proteins nor consumes NADPH. Experiments on rats with thrombolytic models suggest endogenous MNA could be a stimulator of the COX2/PGI2 pathway and thus regulate an anti-thrombotic effect (Chlopicki et al. 2007).
R-HSA-8869603 (Reactome) Plasma membrane-associated SLC22A13 (solute carrier family 22 member 13, also known as OCTL3 - organic cation transporter-like 3) mediates the uptake of extracellular nicotinate (NCA). The protein is especially abundant in the kidney but is widely expressed in tissues of the body (Bahn et al. 2008).
R-HSA-8869606 (Reactome) NMRK1 (nicotinamide riboside kinase 1) catalyzes the reaction of NAR (N-ribosylnicotinate) and ATP to yield NAMN (beta-nicotinate D-ribonucleotide), ADP, and H+ (Tempel et al. 2007). The reaction is annotated with ATP(4-), the major ionized form of ATP at pH 7.2 (Stockbridge & Wolfenden 2009), as the phosphate donor. NMRK1 is a cytosolic enzyme (Nikiforov et al. 2011).
R-HSA-8869607 (Reactome) NMRK2 (nicotinamide riboside kinase 2) catalyzes the reaction of NAR (N-ribosylnicotinate) and ATP to yield NAMN (beta-nicotinate D-ribonucleotide), ADP, and H+ (Tempel et al. 2007). The reaction is annotated with ATP(4-), the major ionized form of ATP at pH 7.2 (Stockbridge & Wolfenden 2009), as the phosphate donor. NMRK2 is a cytosolic enzyme (Nikiforov et al. 2011), localized predominantly in myocytes (Li et al. 1999).
R-HSA-8869627 (Reactome) NMRK2 (nicotinamide riboside kinase 2) catalyzes the reaction of NR (N-ribosylnicotinamide) and ATP to yield NMN (beta-nicotinamide D-ribonucleotide), ADP, and H+ (Bieganowsky & Brenner 2004; Tempel et al. 2007). The reaction is annotated with ATP(4-), the major ionized form of ATP at pH 7.2 (Stockbridge & Wolfenden 2009), as the phosphate donor. NMRK2 is a cytosolic enzyme (Nikiforov et al. 2011), localized predominantly in myocytes (Li et al. 1999).
R-HSA-8869633 (Reactome) NMRK1 (nicotinamide riboside kinase 1) catalyzes the reaction of NR (N-ribosylnicotinamide) and ATP to yield NMN (beta-nicotinamide D-ribonucleotide), ADP, and H+. The enzyme is also active with GTP as a phosphate donor (not annotated here) (Bieganowsky & Brenner 2004; Sasiak & Saunders 1996; Tempel et al. 2007). The reaction is annotated with ATP(4-), the major ionized form of ATP at pH 7.2 (Stockbridge & Wolfenden 2009), as the phosphate donor. NMRK1 is a cytosolic enzyme (Nikiforov et al. 2011).
R-HSA-8870346 (Reactome) BST1 dimer associated with the plasma membrane catalyzes the hydrolysis of extracellular NAD+ to yield NAM and ADP-ribose (Yamamoto-Katayama et al. 2002).
R-HSA-8938073 (Reactome) Poly (ADP-ribose) polymerases (PARPs) catalyse the poly(ADP-ribosyl)ation posttranslational modification of proteins. At least 18 human members share homology with the catalytic domain of the founding member, PARP1. PARPs cleave the glycosidic bond of NAD+ between nicotinamide (NAM) and ribose followed by the covalent modification of mainly glutamate residues on acceptor proteins with an ADP-ribosyl unit, with subsequent ADP-ribosyl unit additions linked by glycosidic ribose-ribose bonds. NAM can be utilised in the NAD+ regeneration process. Poly(ADP-ribosyl)ation is important in many biological processess including DNA repair, regulation of chromosome structure, transcriptional regulation, mitosis and apoptosis. PARPs can localise to either the cytosol or the nucleus. The cytosolic PARPs described here are PARP9, PARP10 and PARP16 (Yan et al. 2013, Yu et al. 2005, Di Paolo et al. 2012). PARP4, PARP6, PARP8 and PARP14 may also be located in the cytosol with the same functionality.
R-HSA-8938076 (Reactome) ADP-ribosyl cyclase/cyclic ADP-ribose hydrolase 1 (CD38) is a multifunctional enzyme that can catalyse the hydrolysis of NAD+ to form linear ADP-ribose (ADP-D-ribose) and/or cyclization of NAD+ forming cyclic ADP-ribose (cADPR) via a two-step enzymatic reaction. The first common step involves the cleavage of the nicotinamide group of NAD+. The reaction intermediate can either be hydrolysed to form ADP-D-ribose or cyclized to form cADPR (Lee et al. 1995, Moreschi et al. 2006). CD38 can also produce nicotinic acid adenine dinucleotide phosphate (NAADP) (Lee et al. 1999). Both cADPR and NAADP are established second messengers for mobilising intracellular Ca2+ stores (Lee 2012). The reaction annotated here describes the hydrolysis of NAD+ to form ADP-D-ribose.
R-HSA-8939959 (Reactome) NMNAT2 catalyzes the reaction of nicotinate D-ribonucleotide and ATP to form deamino-NAD+ (nicotinate adenine dinucleotide) and pyrophosphate (Sorci et al. 2007). The active form of the enzyme is a monomer in vitro; Mg2+ is required for activity (Raffaelli et al. 2002; Sorci et al. 2007). Although the predicted amino acid sequence of the enzyme lacks an obvious signal sequence or transmembrane domain (Yalowitz et al. 2004), recombinant FLAG-tagged protein expressed in HeLa cells localizes predominantly to the Golgi apparatus (Berger et al. 2005). Its localization within the Golgi apparatus is unknown and the annotation here is based on the plausible but speculative assumption that the enzyme is associated with the Gogi membrane and accessible from the cytosol. Immunostaining studies indicate that the protein is abundant in Islets of Langerhans and in several regions of the brain (Yalowitz et al. 2004).
R-HSA-8940070 (Reactome) 5'-nucleotidase (NT5E, CD73) is able to hydrolyse extracellular nucleotides into membrane permeable nucleosides. It displays a broad specificity, acting on mono- or di-nucleotide nicotinamides and different adenosine phosphates, with maximal activity on 5'-adenosine monophosphate. Human NT5E can hydrolyse both NAD+ and NMN, suggesting a role in NAD metabolism (Garavaglia et al. 2012). NT5E is a glycolipid-anchored plasma membrane enzyme (Misumi et al. 1990) that is active in dimeric form and requires one zinc ion per subunit (Zimmermann 1992).
R-HSA-8940074 (Reactome) 5'-nucleotidase (NT5E, CD73) is able to hydrolyse extracellular nucleotides into membrane permeable nucleosides. It displays a broad specificity, acting on mono- or di-nucleotide nicotinamides and different adenosine phosphates, with maximal activity on 5'-adenosine monophosphate. Human NT5E can hydrolyse both NAD+ and NMN, suggesting a role in NAD metabolism (Garavaglia et al. 2012). NT5E is a glycolipid-anchored plasma membrane enzyme (Misumi et al. 1990) that is active in dimeric form and requires one zinc ion per subunit (Zimmermann 1992).
R-HSA-8955030 (Reactome) NAD kinase is the sole NADP(+) biosynthetic enzyme. A cytosolic form of NAD kinase is already characterised but recently, a mitochondrial form has been found to exist. Mitochondrial NAD kinase 2 (NADK2 aka C5orf33, MNADK, NADKD1) uses ATP to phosphorylate NAD+ to NADP+ (Ohashi et al. 2012). NADK2 is ubiquitously expressed and is more abundant than its cytosolic counterpart. Defects in NADK2 can cause 2,4-dienoyl-CoA reductase deficiency (DECRD), a rare, autosomal recessive, inborn error of polyunsaturated fatty acids and lysine metabolism, resulting in mitochondrial dysfunction (Houten et al. 2014).
R-HSA-8956458 (Reactome) Renalase (RNLS) is a flavoprotein that is secreted by the kidney and circulates in blood from where it can regulate blood pressure, regulate sodium and phosphate excretion and display cardioprotectivity through a mechanism which is not understood to date. RNLS, using FAD as cofactor, can oxidise isomeric forms of beta-NAD(P)H that can arise either by nonspecific reduction of beta-NAD(P)+ or by tautomerisation of beta-NAD(P)H (Milani et al. 2011, Beaupre et al. 2015). These forms are 1,2- and 1,6-dihydroNAD(P) (dh-beta-NAD(P)) and are potent inhibitors of primary metabolism dehydrogenases. RNLS may thus play a role in eliminating these isomeric forms which threaten normal respiratory activity.
R-NADPHXR-HSA-6806966 (Reactome)
RNLS:FADmim-catalysisR-HSA-8956458 (Reactome)
S-NADPHXArrowR-HSA-6806966 (Reactome)
S-NADPHXR-HSA-6806967 (Reactome)
SLC22A13mim-catalysisR-HSA-8869603 (Reactome)
SLC5A8mim-catalysisR-HSA-429749 (Reactome)
adenosine 5'-monophosphateR-HSA-6809287 (Reactome)
dh-beta-NADR-HSA-8956458 (Reactome)
e-R-HSA-2309773 (Reactome)
monocarboxylates

transported by

SLC5A8
ArrowR-HSA-429749 (Reactome)
monocarboxylates

transported by

SLC5A8
R-HSA-429749 (Reactome)
Personal tools