Enzyme

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     2. Transferases
        2.7 Transferring phosphorus-containing groups
            2.7.1 Phosphotransferases with an alcohol group as acceptor
ID:2.7.1.74
Description:Deoxycytidine kinase.
Cath: 3.40.50.300;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.1.74
BRENDA Enzyme Link: BRENDA 2.7.1.74
KEGG Enzyme Link: KEGG2.7.1.74
BioCyc Enzyme Link: BioCyc 2.7.1.74
ExPASy Enzyme Link: ExPASy2.7.1.74
EC2PDB Enzyme Link: EC2PDB 2.7.1.74
ExplorEnz Enzyme Link: ExplorEnz 2.7.1.74
PRIAM enzyme-specific profiles Link: PRIAM 2.7.1.74
IntEnz Enzyme Link: IntEnz 2.7.1.74
MEDLINE Enzyme Link: MEDLINE 2.7.1.74
MSA:

2.7.1.74;

Phylogenetic Tree:

2.7.1.74;

Uniprot:
M-CSA:
RHEA:46040 2'-deoxycytidine + ATP = ADP + dCMP + H(+)
RULE(radius=1) [*:1]-[OH;+0:2].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:7]-[*:8]>>[*:8]-[OH;+0:7].[*:3]=[P;H0;+0:4](-[*:5])(-[*:6])-[O;H0;+0:2]-[*:1]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Structural and kinetic characterization of human deoxycytidine kinase variants able to phosphorylate 5-substituted deoxycytidine and thymidine analogues .Hazra S, Ort S, Konrad M, Lavie A2010 Aug 1020614893
Extending thymidine kinase activity to the catalytic repertoire of human deoxycytidine kinase.Hazra S, Sabini E, Ort S, Konrad M, Lavie A2009 Feb 1719159229
Structural basis for substrate promiscuity of dCK.Sabini E, Hazra S, Ort S, Konrad M, Lavie A2008 May 218377927
Structural basis for the preference of UTP over ATP in human deoxycytidine kinase: illuminating the role of main-chain reorganization.Godsey MH, Ort S, Sabini E, Konrad M, Lavie A2006 Jan 1716401075

RHEA:46036 2'-deoxycytidine + UTP = dCMP + H(+) + UDP
RULE(radius=1) [*:1]-[O;H0;+0:2]-[P;H0;+0:3](=[*:4])(-[*:5])-[*:6].[*:7]-[OH;+0:8]>>[*:1]-[OH;+0:2].[*:4]=[P;H0;+0:3](-[*:5])(-[*:6])-[O;H0;+0:8]-[*:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Structural and kinetic characterization of human deoxycytidine kinase variants able to phosphorylate 5-substituted deoxycytidine and thymidine analogues .Hazra S, Ort S, Konrad M, Lavie A2010 Aug 1020614893
Extending thymidine kinase activity to the catalytic repertoire of human deoxycytidine kinase.Hazra S, Sabini E, Ort S, Konrad M, Lavie A2009 Feb 1719159229
Structural basis for substrate promiscuity of dCK.Sabini E, Hazra S, Ort S, Konrad M, Lavie A2008 May 218377927
Structural basis for the preference of UTP over ATP in human deoxycytidine kinase: illuminating the role of main-chain reorganization.Godsey MH, Ort S, Sabini E, Konrad M, Lavie A2006 Jan 1716401075

RHEA:20061 2'-deoxycytidine + a ribonucleoside 5'-triphosphate = a ribonucleoside 5'-diphosphate + dCMP + H(+)
RULE(radius=1) [*:1]-[O;H0;+0:2]-[P;H0;+0:3](=[*:4])(-[*:5])-[*:6].[*:7]-[OH;+0:8]>>[*:1]-[OH;+0:2].[*:4]=[P;H0;+0:3](-[*:5])(-[*:6])-[O;H0;+0:8]-[*:7]
Reaction
Core-to-Core No scaffolds atoms were exchanged as a result of the reaction

References

TitleAuthorsDatePubMed ID
Structural and kinetic characterization of human deoxycytidine kinase variants able to phosphorylate 5-substituted deoxycytidine and thymidine analogues .Hazra S, Ort S, Konrad M, Lavie A2010 Aug 1020614893
Extending thymidine kinase activity to the catalytic repertoire of human deoxycytidine kinase.Hazra S, Sabini E, Ort S, Konrad M, Lavie A2009 Feb 1719159229
Structural basis for substrate promiscuity of dCK.Sabini E, Hazra S, Ort S, Konrad M, Lavie A2008 May 218377927
Structure of human dCK suggests strategies to improve anticancer and antiviral therapy.Sabini E, Ort S, Monnerjahn C, Konrad M, Lavie A2003 Jul12808445