Nucleotide salvage (Homo sapiens)

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2715, 2243, 47, 511911, 35, 4630, 33, 44, 56542, 4, 7, 26, 34...3, 51, 39, 5011, 35, 4612, 23, 559, 14, 31, 3214, 3216537, 34, 5218, 20, 28218, 10, 13, 4914, 25, 3224, 29, 38, 44, 45, 56cytosolmitochondrial matrixR1P HDHD1:Mg2+Mg2+ Gua ATPIMPHGPRT tetramerdC, Thy-dRib, dUguanosine5'-monophosphateUCKL1Ura NH4+Mg2+ TK1 H2OdA, dGADP(d)AMPdA ADPThy-Rib, dUdU dI Ino, dIDGUOK Thy dRibPAde-Rib, dAGua-Rib DCK dimerADPPiMg2+ AMPD tetramersPPiUra-Rib ADPdC HypH+UCK1 tetramerAMPD2 DCK dRibP R1P, dRibP2'-deoxyadenosine 5'-monophosphate Gua, HypUra-Rib ADK UPP2 Thy-dRib Cyt-Rib 2'-deoxyadenosine 5'-monophosphate GMP, IMPPRPPdC HDHD1 ADPPURIDguanosine 5'-monophosphate dU H2ONH4+UCK1 R1P, dRibP(d)CMPADPdIMP cytidine 5'-monophosphate 2'-deoxycytosine 5'-monophosphate uridine 5'-monophosphate NH4+ATPIno ATPdAMP, dGMP, dIMPDGUOK dimerThy, UraR1P H2OdAMP, dGMPdI AMPD3 PNP CDA 2'-deoxyguanosine 5'-monophosphate 2'-deoxycytosine 5'-monophosphate Thy-dRibTMP PiCMP, UMPIno dG methylamineUra-Rib ATPATPCyt-Rib ADAL ADPAde-Rib GMPR (d)UraAPRT dRibP APRT dimerAMP GMPR tetramersZn2+ G, dGAdeIMPADAL:ZnHyp dG DCK dimercytidine 5'-monophosphate ADAAMPdCMP, TMP, dUMPPiGMPR2 2'-deoxyguanosine 5'-monophosphate (d)UraUPP1 Thy-dRib HPRT1 2'-deoxyadenosine 5'-monophosphate UCK2 tetramerTK1 tetramerCDA tetramerTK2TYMP dimerMg2+ UPP1, UPP2dA, dG, dIATPIno, dIdA Cyt-Rib, Ura-RibNADP+UraIMP TMPN6-methyl-AMPNH4+Cyt-Rib, dCZn2+ NP trimerdU5MP GuaATPAMPD1 dG TYMP dU NADPHdA ADKDCK PURIDPMg2+ dU UCK 2 dI H2O7, 37, 52387, 37, 52103411, 4617, 425440485346, 473118, 28


Description

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.

Comments

Reactome-Converter 
Pathway is converted from Reactome ID: 8956321
Reactome-version 
Reactome version: 66
Reactome Author 
Reactome Author: Jassal, Bijay

Quality Tags

Ontology Terms

 

Bibliography

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  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
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  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
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  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
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  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

History

View all...
CompareRevisionActionTimeUserComment
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

DataNodes

View all...
NameTypeDatabase referenceComment
(d)AMPComplexR-ALL-500088 (Reactome)
(d)CMPComplexR-ALL-500828 (Reactome)
(d)UraComplexR-ALL-500430 (Reactome)
2'-deoxyadenosine 5'-monophosphate MetaboliteCHEBI:17713 (ChEBI)
2'-deoxycytosine 5'-monophosphate MetaboliteCHEBI:15918 (ChEBI)
2'-deoxyguanosine 5'-monophosphate MetaboliteCHEBI:16192 (ChEBI)
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, 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, IMPComplexR-ALL-500260 (Reactome)
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)
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)
cytidine 5'-monophosphate MetaboliteCHEBI:17361 (ChEBI)
dA MetaboliteCHEBI:17256 (ChEBI)
dA, dG, dIComplexR-ALL-500224 (Reactome)
dA, dGComplexR-ALL-500201 (Reactome)
dAMP, dGMP, dIMPComplexR-ALL-500222 (Reactome)
dAMP, dGMPComplexR-ALL-500199 (Reactome)
dC MetaboliteCHEBI:15698 (ChEBI)
dC, Thy-dRib, dUComplexR-ALL-500822 (Reactome)
dCMP, TMP, dUMPComplexR-ALL-500823 (Reactome)
dG MetaboliteCHEBI:17172 (ChEBI)
dI MetaboliteCHEBI:28997 (ChEBI)
dIMP MetaboliteCHEBI:28806 (ChEBI)
dRibP MetaboliteCHEBI:28542 (ChEBI)
dRibPMetaboliteCHEBI:28542 (ChEBI)
dU MetaboliteCHEBI:16450 (ChEBI)
dU5MP MetaboliteCHEBI:17622 (ChEBI)
guanosine 5'-monophosphateMetaboliteCHEBI:17345 (ChEBI)
guanosine 5'-monophosphate MetaboliteCHEBI:17345 (ChEBI)
methylamineMetaboliteCHEBI:16830 (ChEBI)
uridine 5'-monophosphate MetaboliteCHEBI:16695 (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)
AMPArrowR-HSA-74213 (Reactome)
AMPD tetramersmim-catalysisR-HSA-76590 (Reactome)
AMPR-HSA-76590 (Reactome)
APRT dimermim-catalysisR-HSA-74213 (Reactome)
ATPR-HSA-109624 (Reactome)
ATPR-HSA-109671 (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)
AdeR-HSA-74213 (Reactome)
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)
GMP, IMPArrowR-HSA-74215 (Reactome)
GMPR tetramersmim-catalysisR-HSA-514604 (Reactome)
Gua, HypR-HSA-74215 (Reactome)
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)
PRPPR-HSA-74213 (Reactome)
PRPPR-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-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).
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-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).
R-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).
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, dGR-HSA-109671 (Reactome)
dAMP, dGMP, dIMPArrowR-HSA-74207 (Reactome)
dAMP, dGMPArrowR-HSA-109671 (Reactome)
dC, Thy-dRib, dUR-HSA-109759 (Reactome)
dCMP, TMP, dUMPArrowR-HSA-109759 (Reactome)
dRibPR-HSA-112266 (Reactome)
guanosine 5'-monophosphateR-HSA-514604 (Reactome)
methylamineArrowR-HSA-2161187 (Reactome)
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