Nucleotide salvage (Homo sapiens)

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543313, 28, 32, 5026, 34, 4922, 46, 471430, 35, 4816, 238, 11, 22, 24, 27...3, 19, 3721, 31, 5625, 532, 5, 17, 20, 38...10, 129417, 10, 121, 17, 20, 5210, 12, 15, 43184, 39, 404, 39, 40mitochondrial matrixdI DCK dU PURIDADAGMPR tetramersDCK dimerdAMP NH4+Cyt-Rib, Ura-RibAMPADPCMP ADAL:Zn(d)CMPUCK2 tetramerUra Ade-Rib Gua(d)UraMg2+ GMPR HGPRT tetramerPPidG Gua, HypH2OAPRT dimerdU5MP dU R1P, dRibPAPRT TYMP dimer(d)AMPDGUOK dimerPRPPAMP Ura-Rib Ura-Rib ADPdGMP dC R1P, dRibPADAL DCK PURIDPThy dG CDA TK2PiThy-dRibPNP dAMP, dGMPThy-dRib CDA tetramerGua-Rib dU TYMP AMPD1 Ino Ura-Rib ADKDCK dimerADPGMPdCMP dCMP, TMP, dUMPIno Mg2+ dGMP AMPD tetramersdIMP CMP, UMPThy-Rib, dUAdeTK1 tetramerUCK 2 Zn2+ NADPHUPP1, UPP2R1P ADPADPMg2+ ATPNH4+dA, dG, dIAde-Rib, dAdG UCK1 tetramerNADP+NH4+ADK dRibPPiUCKL1PidAMP, dGMP, dIMPTMPUPP1 Mg2+ HDHD1:Mg2+Thy, UraZn2+ (d)UraIMPAMPD3 HPRT1 dC TK1 NP trimerATPADPCMP ATPdA, dGHDHD1 ADPdC, Thy-dRib, dUNH4+UPP2 dRibP H2OIMPATPdA N6-methyl-AMPHypdU UraGMP Cyt-Rib Hyp GMP, IMPG, dGdA H2OR1P dA dAMP AMPD2 dAMP UCK1 GMPR2 dRibP Cyt-Rib dCMP Mg2+ ATPDGUOK ATPTMP UMP ATPIno, dIGua Thy-dRib IMP H2OH+methylaminedI dI Ino, dICyt-Rib, dC325530, 482474711, 22, 4642336, 361526, 454, 391611, 22, 46


Nucleosides and free bases generated by RNA and DNA breakdown are converted back to nucleotide monophosphates, allowing them to re-enter the pathways of nucleotide biosynthesis and interconversion. Under normal conditions, DNA turnover is limited and deoxyribonucleotide salvage operates at a correspondingly low level (Watts 1974). View original pathway at:Reactome.


Pathway is converted from Reactome ID: 8956321
Reactome version: 61
Reactome Author 
Reactome Author: Jassal, Bijay

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  1. Deng Y, Wang Z, Ying K, Gu S, Ji C, Huang Y, Gu X, Wang Y, Xu Y, Li Y, Xie Y, Mao Y.; ''NADPH-dependent GMP reductase isoenzyme of human (GMPR2). Expression, purification, and kinetic properties.''; PubMed Europe PMC
  2. Shewach DS, Reynolds KK, Hertel L.; ''Nucleotide specificity of human deoxycytidine kinase.''; PubMed Europe PMC
  3. Laliberté J, Momparler RL.; ''Human cytidine deaminase: purification of enzyme, cloning, and expression of its complementary DNA.''; PubMed Europe PMC
  4. Usova EV, Eriksson S.; ''Identification of residues involved in the substrate specificity of human and murine dCK.''; PubMed Europe PMC
  5. Chung SJ, Fromme JC, Verdine GL.; ''Structure of human cytidine deaminase bound to a potent inhibitor.''; PubMed Europe PMC
  6. Wang L, Hellman U, Eriksson S.; ''Cloning and expression of human mitochondrial deoxyguanosine kinase cDNA.''; PubMed Europe PMC
  7. Datta NS, Shewach DS, Hurley MC, Mitchell BS, Fox IH.; ''Human T-lymphoblast deoxycytidine kinase: purification and properties.''; PubMed Europe PMC
  8. Hurley MC, Lin B, Fox IH.; ''Regulation of deoxyadenosine and nucleoside analog phosphorylation by human placental adenosine kinase.''; PubMed Europe PMC
  9. Van Rompay AR, Johansson M, Karlsson A.; ''Substrate specificity and phosphorylation of antiviral and anticancer nucleoside analogues by human deoxyribonucleoside kinases and ribonucleoside kinases.''; PubMed Europe PMC
  10. Mathews II, Erion MD, Ealick SE.; ''Structure of human adenosine kinase at 1.5 A resolution.''; PubMed Europe PMC
  11. Wiginton DA, Coleman MS, Hutton JJ.; ''Characterization of purine nucleoside phosphorylase from human granulocytes and its metabolism of deoxyribonucleosides.''; PubMed Europe PMC
  12. Roosild TP, Castronovo S, Fabbiani M, Pizzorno G.; ''Implications of the structure of human uridine phosphorylase 1 on the development of novel inhibitors for improving the therapeutic window of fluoropyrimidine chemotherapy.''; PubMed Europe PMC
  13. Hershfield MS, Fetter JE, Small WC, Bagnara AS, Williams SR, Ullman B, Martin DW, Wasson DB, Carson DA.; ''Effects of mutational loss of adenosine kinase and deoxycytidine kinase on deoxyATP accumulation and deoxyadenosine toxicity in cultured CEM human T-lymphoblastoid cells.''; PubMed Europe PMC
  14. Greenberg N, Schumm DE, Webb TE.; ''Uridine kinase activities and pyrimidine nucleoside phosphorylation in fluoropyrimidine-sensitive and -resistant cell lines of the Novikoff hepatoma.''; PubMed Europe PMC
  15. Bausch-Jurken MT, Mahnke-Zizelman DK, Morisaki T, Sabina RL.; ''Molecular cloning of AMP deaminase isoform L. Sequence and bacterial expression of human AMPD2 cDNA.''; PubMed Europe PMC
  16. Jolly DJ, Okayama H, Berg P, Esty AC, Filpula D, Bohlen P, Johnson GG, Shively JE, Hunkapillar T, Friedmann T.; ''Isolation and characterization of a full-length expressible cDNA for human hypoxanthine phosphoribosyl transferase.''; PubMed Europe PMC
  17. Ashby B, Frieden C.; ''Adenylate deaminase. Kinetic and binding studies on the rabbit muscle enzyme.''; PubMed Europe PMC
  18. Norman RA, Barry ST, Bate M, Breed J, Colls JG, Ernill RJ, Luke RW, Minshull CA, McAlister MS, McCall EJ, McMiken HH, Paterson DS, Timms D, Tucker JA, Pauptit RA.; ''Crystal structure of human thymidine phosphorylase in complex with a small molecule inhibitor.''; PubMed Europe PMC
  19. Akeson AL, Wiginton DA, Dusing MR, States JC, Hutton JJ.; ''Mutant human adenosine deaminase alleles and their expression by transfection into fibroblasts.''; PubMed Europe PMC
  20. Usuki K, Saras J, Waltenberger J, Miyazono K, Pierce G, Thomason A, Heldin CH.; ''Platelet-derived endothelial cell growth factor has thymidine phosphorylase activity.''; PubMed Europe PMC
  21. Preumont A, Rzem R, Vertommen D, Van Schaftingen E.; ''HDHD1, which is often deleted in X-linked ichthyosis, encodes a pseudouridine-5'-phosphatase.''; PubMed Europe PMC
  22. Mahnke-Zizelman DK, Tullson PC, Sabina RL.; ''Novel aspects of tetramer assembly and N-terminal domain structure and function are revealed by recombinant expression of human AMP deaminase isoforms.''; PubMed Europe PMC
  23. Johansson M.; ''Identification of a novel human uridine phosphorylase.''; PubMed Europe PMC
  24. Munch-Petersen B, Tyrsted G, Cloos L.; ''Reversible ATP-dependent transition between two forms of human cytosolic thymidine kinase with different enzymatic properties.''; PubMed Europe PMC
  25. Kashuba E, Kashuba V, Sandalova T, Klein G, Szekely L.; ''Epstein-Barr virus encoded nuclear protein EBNA-3 binds a novel human uridine kinase/uracil phosphoribosyltransferase.''; PubMed Europe PMC
  26. Sarup JC, Johnson MA, Verhoef V, Fridland A.; ''Regulation of purine deoxynucleoside phosphorylation by deoxycytidine kinase from human leukemic blast cells.''; PubMed Europe PMC
  27. Watts RW.; ''Molecular variation in relation to purine metabolism.''; PubMed Europe PMC
  28. Desgranges C, Razaka G, Rabaud M, Bricaud H.; ''Catabolism of thymidine in human blood platelets: purification and properties of thymidine phosphorylase.''; PubMed Europe PMC
  29. Sherley JL, Kelly TJ.; ''Human cytosolic thymidine kinase. Purification and physical characterization of the enzyme from HeLa cells.''; PubMed Europe PMC
  30. Wang L, Munch-Petersen B, Herrström Sjöberg A, Hellman U, Bergman T, Jörnvall H, Eriksson S.; ''Human thymidine kinase 2: molecular cloning and characterisation of the enzyme activity with antiviral and cytostatic nucleoside substrates.''; PubMed Europe PMC
  31. Suzuki NN, Koizumi K, Fukushima M, Matsuda A, Inagaki F.; ''Structural basis for the specificity, catalysis, and regulation of human uridine-cytidine kinase.''; PubMed Europe PMC
  32. Van Rompay AR, Norda A, Lindén K, Johansson M, Karlsson A.; ''Phosphorylation of uridine and cytidine nucleoside analogs by two human uridine-cytidine kinases.''; PubMed Europe PMC
  33. Jansson O, Bohman C, Munch-Petersen B, Eriksson S.; ''Mammalian thymidine kinase 2. Direct photoaffinity labeling with [32P]dTTP of the enzyme from spleen, liver, heart and brain.''; PubMed Europe PMC
  34. Hatzis P, Al-Madhoon AS, Jüllig M, Petrakis TG, Eriksson S, Talianidis I.; ''The intracellular localization of deoxycytidine kinase.''; PubMed Europe PMC
  35. Williams SR, Gekeler V, McIvor RS, Martin DW.; ''A human purine nucleoside phosphorylase deficiency caused by a single base change.''; PubMed Europe PMC
  36. Chottiner EG, Shewach DS, Datta NS, Ashcraft E, Gribbin D, Ginsburg D, Fox IH, Mitchell BS.; ''Cloning and expression of human deoxycytidine kinase cDNA.''; PubMed Europe PMC
  37. Sabini E, Ort S, Monnerjahn C, Konrad M, Lavie A.; ''Structure of human dCK suggests strategies to improve anticancer and antiviral therapy.''; PubMed Europe PMC
  38. Birringer MS, Claus MT, Folkers G, Kloer DP, Schulz GE, Scapozza L.; ''Structure of a type II thymidine kinase with bound dTTP.''; PubMed Europe PMC
  39. Spector T, Jones TE, Miller RL.; ''Reaction mechanism and specificity of human GMP reductase. Substrates, inhibitors, activators, and inactivators.''; PubMed Europe PMC
  40. Yun S, Suelter CH.; ''Human erythrocyte 5'-AMP aminohydrolase. Purification and characterization.''; PubMed Europe PMC
  41. Datta NS, Shewach DS, Mitchell BS, Fox IH.; ''Kinetic properties and inhibition of human T lymphoblast deoxycytidine kinase.''; PubMed Europe PMC
  42. LEE YP.; ''5'-Adenylic acid deaminase. III. Properties and kinetic studies.''; PubMed Europe PMC
  43. Johansson M, Karlsson A.; ''Cloning and expression of human deoxyguanosine kinase cDNA.''; PubMed Europe PMC
  44. Lee LS, Cheng YC.; ''Human deoxythymidine kinase. I. Purification and general properties of the cytoplasmic and mitochondrial isozymes derived from blast cells of acute myelocytic leukemia.''; PubMed Europe PMC
  45. Sherley JL, Kelly TJ.; ''Regulation of human thymidine kinase during the cell cycle.''; PubMed Europe PMC
  46. Ealick SE, Rule SA, Carter DC, Greenhough TJ, Babu YS, Cook WJ, Habash J, Helliwell JR, Stoeckler JD, Parks RE.; ''Three-dimensional structure of human erythrocytic purine nucleoside phosphorylase at 3.2 A resolution.''; PubMed Europe PMC
  47. Park I, Ives DH.; ''Properties of a highly purified mitochondrial deoxyguanosine kinase.''; PubMed Europe PMC
  48. Ashby B, Holmsen H.; ''Platelet AMP deaminase. Purification and kinetic studies.''; PubMed Europe PMC
  49. Andres CM, Fox IH.; ''Purification and properties of human placental adenosine kinase.''; PubMed Europe PMC
  50. Li J, Wei Z, Zheng M, Gu X, Deng Y, Qiu R, Chen F, Ji C, Gong W, Xie Y, Mao Y.; ''Crystal structure of human guanosine monophosphate reductase 2 (GMPR2) in complex with GMP.''; PubMed Europe PMC
  51. Johansson K, Ramaswamy S, Ljungcrantz C, Knecht W, Piskur J, Munch-Petersen B, Eriksson S, Eklund H.; ''Structural basis for substrate specificities of cellular deoxyribonucleoside kinases.''; PubMed Europe PMC
  52. Bohman C, Eriksson S.; ''Deoxycytidine kinase from human leukemic spleen: preparation and characteristics of homogeneous enzyme.''; PubMed Europe PMC
  53. Holden JA, Meredith GS, Kelley WN.; ''Human adenine phosphoribosyltransferase. Affinity purification, subunit structure, amino acid composition, and peptide mapping.''; PubMed Europe PMC
  54. Murakami E, Bao H, Mosley RT, Du J, Sofia MJ, Furman PA.; ''Adenosine deaminase-like protein 1 (ADAL1): characterization and substrate specificity in the hydrolysis of N(6)- or O(6)-substituted purine or 2-aminopurine nucleoside monophosphates.''; PubMed Europe PMC
  55. Watanabe S, Uchida T.; ''Cloning and expression of human uridine phosphorylase.''; PubMed Europe PMC
  56. Munch-Petersen B, Cloos L, Tyrsted G, Eriksson S.; ''Diverging substrate specificity of pure human thymidine kinases 1 and 2 against antiviral dideoxynucleosides.''; PubMed Europe PMC


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101624view11:49, 1 November 2018ReactomeTeamreactome version 66
101160view21:35, 31 October 2018ReactomeTeamreactome version 65
100686view20:08, 31 October 2018ReactomeTeamreactome version 64
100236view16:53, 31 October 2018ReactomeTeamreactome version 63
99788view15:18, 31 October 2018ReactomeTeamreactome version 62 (2nd attempt)
99339view12:47, 31 October 2018ReactomeTeamreactome version 62
97319view14:41, 9 May 2018Lorasimonsconnect lines
97318view14:32, 9 May 2018Lorasimonsconnect lines
93456view11:24, 9 August 2017ReactomeTeamNew pathway

External references


View all...
NameTypeDatabase referenceComment
(d)AMPComplexR-ALL-500088 (Reactome)
(d)CMPComplexR-ALL-500828 (Reactome)
(d)UraComplexR-ALL-500430 (Reactome)
ADAL ProteinQ6DHV7 (Uniprot-TrEMBL)
ADAL:ZnComplexR-HSA-2161178 (Reactome)
ADAProteinP00813 (Uniprot-TrEMBL)
ADK ProteinP55263 (Uniprot-TrEMBL)
ADKComplexR-HSA-76542 (Reactome)
ADPMetaboliteCHEBI:16761 (ChEBI)
AMP MetaboliteCHEBI:16027 (ChEBI)
AMPMetaboliteCHEBI:16027 (ChEBI)
AMPD tetramersComplexR-HSA-500235 (Reactome)
AMPD1 ProteinP23109 (Uniprot-TrEMBL)
AMPD2 ProteinQ01433 (Uniprot-TrEMBL)
AMPD3 ProteinQ01432 (Uniprot-TrEMBL)
APRT ProteinP07741 (Uniprot-TrEMBL)
APRT dimerComplexR-HSA-74211 (Reactome)
ATPMetaboliteCHEBI:15422 (ChEBI)
Ade-Rib MetaboliteCHEBI:16335 (ChEBI)
Ade-Rib, dAComplexR-ALL-500173 (Reactome)
AdeMetaboliteCHEBI:16708 (ChEBI)
CDA ProteinP32320 (Uniprot-TrEMBL)
CDA tetramerComplexR-HSA-73462 (Reactome)
CMP MetaboliteCHEBI:17361 (ChEBI)
CMP, UMPComplexR-ALL-500761 (Reactome)
Cyt-Rib MetaboliteCHEBI:17562 (ChEBI)
Cyt-Rib, Ura-RibComplexR-ALL-500759 (Reactome)
Cyt-Rib, dCComplexR-ALL-500829 (Reactome)
DCK ProteinP27707 (Uniprot-TrEMBL)
DCK dimerComplexR-HSA-73516 (Reactome)
DGUOK ProteinQ16854 (Uniprot-TrEMBL)
DGUOK dimerComplexR-HSA-74205 (Reactome)
G, dGComplexR-ALL-500245 (Reactome)
GMP MetaboliteCHEBI:17345 (ChEBI)
GMP, IMPComplexR-ALL-500260 (Reactome)
GMPMetaboliteCHEBI:17345 (ChEBI)
GMPR ProteinP36959 (Uniprot-TrEMBL)
GMPR tetramersComplexR-HSA-514620 (Reactome)
GMPR2 ProteinQ9P2T1 (Uniprot-TrEMBL)
Gua MetaboliteCHEBI:16235 (ChEBI)
Gua, HypComplexR-ALL-500259 (Reactome)
Gua-Rib MetaboliteCHEBI:16750 (ChEBI)
GuaMetaboliteCHEBI:16235 (ChEBI)
H+MetaboliteCHEBI:15378 (ChEBI)
H2OMetaboliteCHEBI:15377 (ChEBI)
HDHD1 ProteinQ08623 (Uniprot-TrEMBL)
HDHD1:Mg2+ComplexR-HSA-6788292 (Reactome)
HGPRT tetramerComplexR-HSA-74208 (Reactome)
HPRT1 ProteinP00492 (Uniprot-TrEMBL)
Hyp MetaboliteCHEBI:17368 (ChEBI)
HypMetaboliteCHEBI:17368 (ChEBI)
IMP MetaboliteCHEBI:17202 (ChEBI)
IMPMetaboliteCHEBI:17202 (ChEBI)
Ino MetaboliteCHEBI:17596 (ChEBI)
Ino, dIComplexR-ALL-500172 (Reactome)
Mg2+ MetaboliteCHEBI:18420 (ChEBI)
N6-methyl-AMPMetaboliteCHEBI:40196 (ChEBI)
NADP+MetaboliteCHEBI:18009 (ChEBI)
NADPHMetaboliteCHEBI:16474 (ChEBI)
NH4+MetaboliteCHEBI:28938 (ChEBI)
NP trimerComplexR-HSA-74237 (Reactome)
PNP ProteinP00491 (Uniprot-TrEMBL)
PPiMetaboliteCHEBI:29888 (ChEBI)
PRPPMetaboliteCHEBI:17111 (ChEBI)
PURIDMetaboliteCHEBI:17802 (ChEBI)
PURIDPMetaboliteCHEBI:18116 (ChEBI)
PiMetaboliteCHEBI:18367 (ChEBI)
R1P MetaboliteCHEBI:35425 (ChEBI)
R1P, dRibPComplexR-ALL-500244 (Reactome)
TK1 ProteinP04183 (Uniprot-TrEMBL)
TK1 tetramerComplexR-HSA-73501 (Reactome)
TK2ProteinO00142 (Uniprot-TrEMBL)
TMP MetaboliteCHEBI:17013 (ChEBI)
TMPMetaboliteCHEBI:17013 (ChEBI)
TYMP ProteinP19971 (Uniprot-TrEMBL)
TYMP dimerComplexR-HSA-74363 (Reactome)
Thy MetaboliteCHEBI:17821 (ChEBI)
Thy, UraComplexR-ALL-500438 (Reactome)
Thy-Rib, dUComplexR-ALL-500444 (Reactome)
Thy-dRib MetaboliteCHEBI:17748 (ChEBI)
Thy-dRibMetaboliteCHEBI:17748 (ChEBI)
UCK 2 ProteinQ9BZX2 (Uniprot-TrEMBL)
UCK1 ProteinQ9HA47 (Uniprot-TrEMBL)
UCK1 tetramerComplexR-HSA-73504 (Reactome)
UCK2 tetramerComplexR-HSA-500801 (Reactome)
UCKL1ProteinQ9NWZ5 (Uniprot-TrEMBL)
UMP MetaboliteCHEBI:16695 (ChEBI)
UPP1 ProteinQ16831 (Uniprot-TrEMBL)
UPP1, UPP2ComplexR-HSA-977408 (Reactome)
UPP2 ProteinO95045 (Uniprot-TrEMBL)
Ura MetaboliteCHEBI:17568 (ChEBI)
Ura-Rib MetaboliteCHEBI:16704 (ChEBI)
UraMetaboliteCHEBI:17568 (ChEBI)
Zn2+ MetaboliteCHEBI:29105 (ChEBI)
dA MetaboliteCHEBI:17256 (ChEBI)
dA, dG, dIComplexR-ALL-500224 (Reactome)
dA, dGComplexR-ALL-500201 (Reactome)
dAMP MetaboliteCHEBI:17713 (ChEBI)
dAMP, dGMP, dIMPComplexR-ALL-500222 (Reactome)
dAMP, dGMPComplexR-ALL-500199 (Reactome)
dC MetaboliteCHEBI:15698 (ChEBI)
dC, Thy-dRib, dUComplexR-ALL-500822 (Reactome)
dCMP MetaboliteCHEBI:15918 (ChEBI)
dCMP, TMP, dUMPComplexR-ALL-500823 (Reactome)
dG MetaboliteCHEBI:17172 (ChEBI)
dGMP MetaboliteCHEBI:16192 (ChEBI)
dI MetaboliteCHEBI:28997 (ChEBI)
dIMP MetaboliteCHEBI:28806 (ChEBI)
dRibP MetaboliteCHEBI:28542 (ChEBI)
dRibPMetaboliteCHEBI:28542 (ChEBI)
dU MetaboliteCHEBI:16450 (ChEBI)
dU5MP MetaboliteCHEBI:17622 (ChEBI)
methylamineMetaboliteCHEBI:16830 (ChEBI)

Annotated Interactions

View all...
SourceTargetTypeDatabase referenceComment
(d)AMPArrowR-HSA-109624 (Reactome)
(d)CMPArrowR-HSA-73598 (Reactome)
(d)UraArrowR-HSA-73608 (Reactome)
(d)UraArrowR-HSA-74372 (Reactome)
ADAL:Znmim-catalysisR-HSA-2161187 (Reactome)
ADAmim-catalysisR-HSA-74241 (Reactome)
ADKmim-catalysisR-HSA-109624 (Reactome)
ADPArrowR-HSA-109624 (Reactome)
ADPArrowR-HSA-109671 (Reactome)
ADPArrowR-HSA-109759 (Reactome)
ADPArrowR-HSA-109903 (Reactome)
ADPArrowR-HSA-73598 (Reactome)
ADPArrowR-HSA-73599 (Reactome)
ADPArrowR-HSA-73632 (Reactome)
ADPArrowR-HSA-74207 (Reactome)
ADPArrowR-HSA-8954327 (Reactome)
AMPD tetramersmim-catalysisR-HSA-76590 (Reactome)
AMPR-HSA-76590 (Reactome)
APRT dimermim-catalysisR-HSA-74213 (Reactome)
ATPR-HSA-109624 (Reactome)
ATPR-HSA-109759 (Reactome)
ATPR-HSA-109903 (Reactome)
ATPR-HSA-73598 (Reactome)
ATPR-HSA-73599 (Reactome)
ATPR-HSA-73632 (Reactome)
ATPR-HSA-74207 (Reactome)
ATPR-HSA-8954327 (Reactome)
Ade-Rib, dAR-HSA-109624 (Reactome)
Ade-Rib, dAR-HSA-74241 (Reactome)
AdeAMPArrowR-HSA-74213 (Reactome) Cytosolic APRT dimer catalyzes the reaction of adenine and 5-phospho-alpha-D-ribose 1-diphosphate to form AMP and pyrophosphate (Holden et al. 1979).
CDA tetramermim-catalysisR-HSA-73608 (Reactome)
CMP, UMPArrowR-HSA-109903 (Reactome)
CMP, UMPArrowR-HSA-73599 (Reactome)
CMP, UMPArrowR-HSA-8954327 (Reactome)
Cyt-Rib, Ura-RibR-HSA-109903 (Reactome)
Cyt-Rib, Ura-RibR-HSA-73599 (Reactome)
Cyt-Rib, Ura-RibR-HSA-8954327 (Reactome)
Cyt-Rib, dCR-HSA-73598 (Reactome)
Cyt-Rib, dCR-HSA-73608 (Reactome)
DCK dimermim-catalysisR-HSA-109671 (Reactome)
DCK dimermim-catalysisR-HSA-73598 (Reactome)
DGUOK dimermim-catalysisR-HSA-74207 (Reactome)
G, dGArrowR-HSA-112034 (Reactome)
GMPR tetramersmim-catalysisR-HSA-514604 (Reactome)
GMPR-HSA-514604 (Reactome)
Gua, HypGMP, IMPArrowR-HSA-74215 (Reactome) Cytosolic hypoxanthine-guanine phosphoribosyltransferase (HPRT1) tetramer catalyzes the reactions of guanine or hypoxanthine with PRPP to form GMP ir IMP and pyrophosphate (Holden and Kelley 1978; Jolly et al. 1983).
GuaR-HSA-112034 (Reactome)
H+R-HSA-514604 (Reactome)
H2OR-HSA-2161187 (Reactome)
H2OR-HSA-6788295 (Reactome)
H2OR-HSA-73608 (Reactome)
H2OR-HSA-74241 (Reactome)
H2OR-HSA-76590 (Reactome)
HDHD1:Mg2+mim-catalysisR-HSA-6788295 (Reactome)
HGPRT tetramermim-catalysisR-HSA-74215 (Reactome)
HypR-HSA-112033 (Reactome)
IMPArrowR-HSA-2161187 (Reactome)
IMPArrowR-HSA-514604 (Reactome)
IMPArrowR-HSA-76590 (Reactome)
Ino, dIArrowR-HSA-112033 (Reactome)
Ino, dIArrowR-HSA-74241 (Reactome)
N6-methyl-AMPR-HSA-2161187 (Reactome)
NADP+ArrowR-HSA-514604 (Reactome)
NADPHR-HSA-514604 (Reactome)
NH4+ArrowR-HSA-514604 (Reactome)
NH4+ArrowR-HSA-73608 (Reactome)
NH4+ArrowR-HSA-74241 (Reactome)
NH4+ArrowR-HSA-76590 (Reactome)
NP trimermim-catalysisR-HSA-112033 (Reactome)
NP trimermim-catalysisR-HSA-112034 (Reactome)
PPiArrowR-HSA-74213 (Reactome)
PPiArrowR-HSA-74215 (Reactome)
PURIDArrowR-HSA-6788295 (Reactome)
PURIDPR-HSA-6788295 (Reactome)
PiArrowR-HSA-112033 (Reactome)
PiArrowR-HSA-112034 (Reactome)
PiArrowR-HSA-112266 (Reactome)
PiArrowR-HSA-6788295 (Reactome)
PiArrowR-HSA-74372 (Reactome)
R-HSA-109624 (Reactome) Cytosolic adenosine linase (ADK) catalyzes the reactions of adenosine and deoxyadenosine with ATP to yield the corresponding nucleotide monophosphates and ADP (Andres and Fox 1979). The enzyme is substantially more active on adenosine than deoxyadenosine in vitro (Hurley at al. 1985) though studies of cultured cells suggest that both reactions may be physiologically relevant (Hershfield et al. 1982). The enzyme is a monomer complexed with magnesium (Mathews et al. 1998).
R-HSA-109759 (Reactome) Mitochondrial thymidine kinase 2 (TK2) catalyzes the reactions of deoxycytidine, thymidine, and deoxyuridine with ATP to form the corresponding deoxynucleotide monophosphates and ADP. The enzyme has been purified from human spleen and is active as a monomer (Munch-Petersen et al. 1991). The enzyme requires divalent cations for activity (Mg++ is preferred) but the nature of the association between the metal ion and the enzyme polypeptide is unclear (Lee and Cheng 1976). The mitochondrial localization of the enzyme has been established experimentally for rats and cattle (Jansson et al. 1992); its mitochondrial localization in humans is inferred from these results and the presence of a mitochondrial localization motif at the amino terminus of the open reading frame of a cloned human cDNA that is missing from the mature catalytically active protein (Wang et al. 1999).
R-HSA-109903 (Reactome) Cytosolic uridine-cytidine kinase 2 (UCK2) catalyzes the reactions of cytidine or uridine with ATP to form CMP or UMP and ADP (Greenberg et al. 1977; Van Rompay et al. 2001). Crystallographic data show the enzyme to be a tetramer (Suzuki et al. 2004). When it is expressed as a fusion construct with green fluorescent protein, the protein localizes primarily to the cytosol of transfected CHO cells (Van Rompay et al. 2003).
R-HSA-112033 (Reactome) Cytosolic nucleoside phosphorylase (NP) trimer catalyzes the reversible reaction of hypoxanthine with ribose 1-phosphate or deoxyribose 1-phosphate to form inosine or deoxyinosine and orthophosphate (Ealick et al. 1990; Wiginton et al. 1980). While NP is active with either ribose 1-phosphate or deoxyribose 1-phosphate in vitro, levels of deoxyribose 1-phosphate are normally low in vivo, limiting the extent of this reaction. NP deficiency in vivo is associated with defects in purine nucleotide salvage and leads to immunodeficiency (Williams et al. 1987).
R-HSA-112034 (Reactome) Cytosolic nucleoside phosphorylase (NP) trimer catalyzes the reversible reaction of guanine with ribose 1-phosphate or deoxyribose 1-phosphate to form guanosine or deoxyguanosine and orthophosphate (Ealick et al. 1990; Wiginton et al. 1980). While NP is active with either ribose 1-phosphate or deoxyribose 1-phosphate in vitro, levels of deoxyribose 1-phosphate are normally low in vivo, limiting the extent of this reaction. NP deficiency in vivo is associated with defects in purine nucleotide salvage and leads to immunodeficiency (Williams et al. 1987).
R-HSA-112266 (Reactome) Cytosolic thymidine phosphorylase (TYMP) catalyzes the reversible reactions of thymine or uracil with 2-deoxy-D-ribose 1-phosphate to form thymidine or deoxyuridine and orthiophosphate. The active form of the enzyme is a homodimer (Desgranges et al. 1981; Norman et al. 2004; Usuki et al. 1992).
R-HSA-2161187 (Reactome) Cytosolic ADAL (Adenosine DeAminase-Like) catalyzes the reaction of N6-methyl-AMP and water to form IMP and methylamine. The active form of the enzyme is a protein monomer complexed with a zinc ion (Murakami et al. 2011).
R-HSA-514604 (Reactome) Cytosolic GMP reductase (GMPR) catalyzes the reaction of GMP and NADPH + H+ to yield IMP and NADP+ + NH4+ (Spector et al. 1979; Deng et al. 2002). Two GMPR proteins have been identified, GMPR and GMPR2. Both proteins form homotetramers (GMPR - unpublished crstallographic data PDB 2BLE; GMPR2 - Li et al. 2006).
R-HSA-6788295 (Reactome) Pseudouridine 5'-phosphate (PURIDP) is a potential intermediate in RNA degradation. Pseudouridine 5'-phosphatase (HDHD1) is a Mg2+-dependent enzyme present in erythrocytes that can dephosphorylate PURIDP to pseudouridine (PURID), the fifth-most abundant nucleoside in RNA. PURID is not metabolised in mammals but excreted intact in urine (Preumont et al. 2010).
R-HSA-73598 (Reactome) Cytosolic deoxycytidine kinase (DCK) catalyzes the reactions of cytidine or deoxycytidine with ATP to form CMP or dCMP and ADP. The enzyme is a homodimer (Sabini et al. 2003). Although a chimeric deoxycytidine kinase - green fluorescent protein expressed at high levels in cultured cells localized to nuclei, endogenous protein is primarily cytosolic (Hatzis et al. 1998). Despite its name, the enzyme has a broad substrate specificity, acting on cytidine, deoxycytidine, deoxyguanosine, and deoxyadenosine (Bohman and Eriksson 1988; Datta et al. 1989a, b; Sarup et al. 1989; Usova and Eriksson 2002). While ATP functions efficiently as a phosphate donor, other nucleoside triphosphates, notably UTP, function efficiently as phosphate donors in vitro and may function in this way in vivo as well (Shewach et al. 1992).
R-HSA-73599 (Reactome) Cytosolic uridine-cytidine kinase 1 (UCK1) catalyzes the reactions of cytidine or uridine with ATP to form CMP or UMP and ADP (Greenberg et al. 1977; Van Rompay et al. 2001). Unpublished crystallographic data show the enzyme to be a tetramer (PDB - 2JEO).
R-HSA-73608 (Reactome) Cytosolic cytidine deaminase catalyzes the hydrolysis of cytidine or dexoycytidine to form uridine or deoxyuridine and ammonia (Laliberte and Momparler 1994). The active form of the enzyme is a tetramer (Chung et al. 2005).
R-HSA-73632 (Reactome) Cytosolic thymidine kinase 1 (TK1) catalyzes the reaction of thymidine and ATP to form TMP (thymidine 5'-monophosphate) and ADP. TK1 has been purified from human spleen and from cultured cells. The enzyme is active as a homotetramer, and phosphorylates thymidine and deoxyuridine using ATP as a phosphate donor in vitro (Sherley and Kelly 1988a; Munch-Petersen et al. 1991; Birringer et al. 2005). Divalent cations are required for enzyme activity (Mg++ is preferred) (Lee and Cheng 1986), and ATP stabilizes the tetrameric form of the enzyme (Munch-Petersen et al. 1993). In cells, enzyme activity is high during S phase of the cell cycle and low otherwise, correlated with intracellular levels of thymidine kinase 1 protein (Sherley and Kelly 1988b), and consistent with a requirement for TMP synthesis in normal cells only as part of DNA replication.
R-HSA-74207 (Reactome) Mitochondrial deoxyguanosine kinase (DGUOK) catalyzes the reactions of deoxyadenosine, deoxyguanosine, and deoxyinosine with ATP to form the corresponding nucleotide monophosphates and ADP (Park and Ives 1988; Johansson and Karlson 1996). Crystallographic studies of the human enzyme have confirmed its dimeric structure and allowed identification of key amino acid residues responsible for its substrate specificity (Johansson et al. 2001).
R-HSA-74241 (Reactome) Cytosolic adenosine deaminase (ADA) catalyzes the hydrolysis of 2'deoxyadenosine and adenosine to yield deoxyinosine and inosine, respectively, plus ammonia (Akeson et al. 1988). Unpublished crystallographic data (PDB 3IAR) indicate that the human enzyme is a monomer.
R-HSA-74372 (Reactome) Cytosolic uridine phosphorylase (isoforms UPP1 and UPP2) catalyzes the reversible reactions of uracil with ribose 1-phosphate or deoxyribose 1-phosphate to yield uridine or deoxyuridine and orthophosphate (Watanabe and Uchida 1995; Johansson, 2003). The active form of UPP1 is a dimer (Rooslid et al. 2009).
R-HSA-76590 (Reactome) Cytosolic AMP deaminase (AMPD) catalyzes the hydrolysis of AMP to yield IMP and ammonia. Three isoforms of AMPD, E, L, and M, have been identified that differ in their expression patterns in the body. All occur as tetramers and all have qualitatively the same catalytic activity, however (Bausch-Jurken et al. 1992; Mahnke-Zizelman et al. 1998).
R-HSA-8954327 (Reactome) Based on sequence similarity, cytosolic uridine-cytidine kinase-like 1 (UCKL1 aka F538) is thought to function as a novel human uridine kinase/uracil phosphoribosyltransferase (Kashuba et al. 2002). The two human uridine kinases 1 and 2 (UCK1 and UCK2) characterised to date phosphorylate uridine/cytidine to uridine monophosphate (UMP)/cytidine monophosphate (CMP) using ATP as a phosphate donor (Greenberg et al. 1977, Van Rompay et al. 2001).
R1P, dRibPR-HSA-112033 (Reactome)
R1P, dRibPR-HSA-112034 (Reactome)
R1P, dRibPR-HSA-74372 (Reactome)
TK1 tetramermim-catalysisR-HSA-73632 (Reactome)
TK2mim-catalysisR-HSA-109759 (Reactome)
TMPArrowR-HSA-73632 (Reactome)
TYMP dimermim-catalysisR-HSA-112266 (Reactome)
Thy, UraR-HSA-112266 (Reactome)
Thy-Rib, dUArrowR-HSA-112266 (Reactome)
Thy-dRibR-HSA-73632 (Reactome)
UCK1 tetramermim-catalysisR-HSA-73599 (Reactome)
UCK2 tetramermim-catalysisR-HSA-109903 (Reactome)
UCKL1mim-catalysisR-HSA-8954327 (Reactome)
UPP1, UPP2mim-catalysisR-HSA-74372 (Reactome)
UraR-HSA-74372 (Reactome)
dA, dG, dIR-HSA-74207 (Reactome)
dA, dGdAMP, dGMPArrowR-HSA-109671 (Reactome) Cytosolic deoxycytidine kinase (DCK) catalyzes the reactions of deoxyadenosine and deoxyguanosine with ATP to form the corresponding nucleotide monophosphates and AMP, The enzyme is a dimer (Bohman and Eriksson 1988; Datta et al. 1989). While the enzyme can be found in nuclei of cultured cells expressing high levels of a tagged recombinant protein, its normal location appears to be cytosolic (Hatzis et al. 1998).
dAMP, dGMP, dIMPArrowR-HSA-74207 (Reactome)
dC, Thy-dRib, dUR-HSA-109759 (Reactome)
dCMP, TMP, dUMPArrowR-HSA-109759 (Reactome)
dRibPR-HSA-112266 (Reactome)
methylamineArrowR-HSA-2161187 (Reactome)
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