EC number:2.7.1.145

Enzyme

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     2. Transferases
        2.7 Transferring phosphorus-containing groups
            2.7.1 Phosphotransferases with an alcohol group as acceptor
ID:2.7.1.145
Description:Deoxynucleoside kinase.
Alternative Name: Multisubstrate deoxyribonucleoside kinase.
Multispecific deoxynucleoside kinase.
Multifunctional deoxynucleoside kinase.
Ms-dNK.
Cath: 3.40.50.300;

3D structure

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PDB

References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.1.145
BRENDA Enzyme Link: BRENDA 2.7.1.145
KEGG Enzyme Link: KEGG2.7.1.145
BioCyc Enzyme Link: BioCyc 2.7.1.145
ExPASy Enzyme Link: ExPASy2.7.1.145
EC2PDB Enzyme Link: EC2PDB 2.7.1.145
ExplorEnz Enzyme Link: ExplorEnz 2.7.1.145
PRIAM enzyme-specific profiles Link: PRIAM 2.7.1.145
IntEnz Enzyme Link: IntEnz 2.7.1.145
MEDLINE Enzyme Link: MEDLINE 2.7.1.145

EC number:2.7.1.145

MSA:

2.7.1.145;
Phylogenetic Tree:

2.7.1.145;
Uniprot:
M-CSA:
RHEA:12140 a 2'-deoxyribonucleoside + ATP = a 2'-deoxyribonucleoside 5'-phosphate + ADP + 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
Four deoxynucleoside kinase activities from Drosophila melanogaster are contained within a single monomeric enzyme, a new multifunctional deoxynucleoside kinase.Munch-Petersen B, Piskur J, Sondergaard L1998 Feb 139461577
Structural basis for the changed substrate specificity of Drosophila melanogaster deoxyribonucleoside kinase mutant N64D.Welin M, Skovgaard T, Knecht W, Zhu C, Berenstein D, Munch-Petersen B, Piskur J, Eklund H2005 Jul16008571
Functional expression of a multisubstrate deoxyribonucleoside kinase from Drosophila melanogaster and its C-terminal deletion mutants.Munch-Petersen B, Knecht W, Lenz C, Søndergaard L, Piskur J2000 Mar 310692477
Cloning and characterization of the multisubstrate deoxyribonucleoside kinase of Drosophila melanogaster.Johansson M, van Rompay AR, Degrève B, Balzarini J, Karlsson A1999 Aug 2010446143
RHEA:19129 ATP + thymidine = ADP + dTMP + 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
Purification and properties of thymidine kinase from regenerating rat liver.Kizer DE, Holman L1974 May 204407348
Thymidine kinase 1 regulatory fine-tuning through tetramer formation.Mutahir Z, Clausen AR, Andersson KM, Wisen SM, Munch-Petersen B, Piškur J2013 Mar23351158
Two thymidine kinases and one multisubstrate deoxyribonucleoside kinase salvage DNA precursors in Arabidopsis thaliana.Clausen AR, Girandon L, Ali A, Knecht W, Rozpedowska E, Sandrini MP, Andreasson E, Munch-Petersen B, Piškur J2012 Oct22897443
Dictyostelium discoideum salvages purine deoxyribonucleosides by highly specific bacterial-like deoxyribonucleoside kinases.Sandrini MP, Söderbom F, Mikkelsen NE, Piskur J2007 Jun 817448496
Structure of vaccinia virus thymidine kinase in complex with dTTP: insights for drug design.El Omari K, Solaroli N, Karlsson A, Balzarini J, Stammers DK2006 Oct 2417062140
Structure of the substrate complex of thymidine kinase from Ureaplasma urealyticum and investigations of possible drug targets for the enzyme.Kosinska U, Carnrot C, Eriksson S, Wang L, Eklund H2005 Dec16336273
Structural basis for the dual thymidine and thymidylate kinase activity of herpes thymidine kinases.Gardberg A, Shuvalova L, Monnerjahn C, Konrad M, Lavie A2003 Oct14527394
DEOXYTHYMIDINE KINASE OF ESCHERICHIA COLI. I. PURIFICATION AND SOME PROPERTIES OF THE ENZYME.OKAZAKI R, KORNBERG A1964 Jan14114853
Nucleoside binding site of herpes simplex type 1 thymidine kinase analyzed by X-ray crystallography.Vogt J, Perozzo R, Pautsch A, Prota A, Schelling P, Pilger B, Folkers G, Scapozza L, Schulz GE2000 Dec 111056041
Four deoxynucleoside kinase activities from Drosophila melanogaster are contained within a single monomeric enzyme, a new multifunctional deoxynucleoside kinase.Munch-Petersen B, Piskur J, Sondergaard L1998 Feb 139461577
Adenosine diphosphate: thymidine 5'-phosphotransferase, a new enzyme activity, associated with the Herpes simplex virus-induced deoxypyrimidine kinase.Falke D, Labenz J, Brauer D, Müller WE1982 Oct 206293576
Functional expression of a multisubstrate deoxyribonucleoside kinase from Drosophila melanogaster and its C-terminal deletion mutants.Munch-Petersen B, Knecht W, Lenz C, Søndergaard L, Piskur J2000 Mar 310692477
RHEA:19201 2'-deoxyguanosine + ATP = ADP + dGMP + 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
Cloning and expression of human mitochondrial deoxyguanosine kinase cDNA.Wang L, Hellman U, Eriksson S1996 Jul 158706825
Dictyostelium discoideum salvages purine deoxyribonucleosides by highly specific bacterial-like deoxyribonucleoside kinases.Sandrini MP, Söderbom F, Mikkelsen NE, Piskur J2007 Jun 817448496
Deoxynucleoside kinases encoded by the yaaG and yaaF genes of Bacillus subtilis. Substrate specificity and kinetic analysis of deoxyguanosine kinase with UTP as the preferred phosphate donor.Andersen RB, Neuhard J2001 Feb 2311078735
RHEA:23452 2'-deoxyadenosine + ATP = ADP + dAMP + 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
Dictyostelium discoideum salvages purine deoxyribonucleosides by highly specific bacterial-like deoxyribonucleoside kinases.Sandrini MP, Söderbom F, Mikkelsen NE, Piskur J2007 Jun 817448496
Four deoxynucleoside kinase activities from Drosophila melanogaster are contained within a single monomeric enzyme, a new multifunctional deoxynucleoside kinase.Munch-Petersen B, Piskur J, Sondergaard L1998 Feb 139461577
Functional expression of a multisubstrate deoxyribonucleoside kinase from Drosophila melanogaster and its C-terminal deletion mutants.Munch-Petersen B, Knecht W, Lenz C, Søndergaard L, Piskur J2000 Mar 310692477
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