Enzyme

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EC Tree
     2. Transferases
        2.7 Transferring phosphorus-containing groups
            2.7.4 Phosphotransferases with a phosphate group as acceptor
ID:2.7.4.13
Description:(Deoxy)nucleoside-phosphate kinase.
Cath: 1.10.238.70; 3.40.50.300;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.4.13
BRENDA Enzyme Link: BRENDA 2.7.4.13
KEGG Enzyme Link: KEGG2.7.4.13
BioCyc Enzyme Link: BioCyc 2.7.4.13
ExPASy Enzyme Link: ExPASy2.7.4.13
EC2PDB Enzyme Link: EC2PDB 2.7.4.13
ExplorEnz Enzyme Link: ExplorEnz 2.7.4.13
PRIAM enzyme-specific profiles Link: PRIAM 2.7.4.13
IntEnz Enzyme Link: IntEnz 2.7.4.13
MEDLINE Enzyme Link: MEDLINE 2.7.4.13
MSA:

2.7.4.13;

Phylogenetic Tree:

2.7.4.13;

Uniprot:
M-CSA:
RHEA:11216 a 2'-deoxyribonucleoside 5'-phosphate + ATP = a 2'-deoxyribonucleoside 5'-diphosphate + ADP
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
Crystal structure of bacteriophage T4 deoxynucleotide kinase with its substrates dGMP and ATP.Teplyakov A, Sebastiao P, Obmolova G, Perrakis A, Brush GS, Bessman MJ, Wilson KS1996 Jul 158670851
The enzymology of virus-infected bacteria. X. A biochemical-genetic study of the deoxynucleotide kinase induced by wild type and amber mutants of phage T4.Duckworth DH, Bessman MJ1967 Jun 255338507
Identification, cloning, and expression of bacteriophage T5 dnk gene encoding a broad specificity deoxyribonucleoside monophosphate kinase (EC 2.7.4.13).Mikoulinskaia GV, Zimin AA, Feofanov SA, Miroshnikov AI2004 Feb14711503
THE ENZYMOLOGY OF VIRUS-INFECTED BACTERIA. VI. PURIFICATION AND PROPERTIES OF THE DEOXYNUCLEOTIDE KINASE INDUCED BY BACTERIOPHAGE T5.BESSMAN MJ, HERRIOTT ST, ORR MJ1965 Jan14253449