Enzyme

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     2. Transferases
        2.7 Transferring phosphorus-containing groups
            2.7.1 Phosphotransferases with an alcohol group as acceptor
ID:2.7.1.21
Description:Thymidine kinase.
Prosite: PDOC00524;
PDB:
PDBScop
2JA1 8089751; 8089752; 8089753;
2J87 8089745; 8089746; 8089747; 8089745; 8089746; 8089747; 8089745; 8089746; 8089747; 8089745; 8089746; 8089747;
2QQE 8089742; 8089743; 8089744; 8089742; 8089743; 8089744;
2QQ0 8089742; 8089743; 8089744; 8089742; 8089743; 8089744;
2ORW 8089742; 8089743; 8089744; 8089742; 8089743; 8089744;
 » show all

Cath: 3.30.60.20; 3.40.50.300;

3D structure

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References

External Links

UniProtKB Enzyme Link: UniProtKB 2.7.1.21
BRENDA Enzyme Link: BRENDA 2.7.1.21
KEGG Enzyme Link: KEGG2.7.1.21
BioCyc Enzyme Link: BioCyc 2.7.1.21
ExPASy Enzyme Link: ExPASy2.7.1.21
EC2PDB Enzyme Link: EC2PDB 2.7.1.21
ExplorEnz Enzyme Link: ExplorEnz 2.7.1.21
PRIAM enzyme-specific profiles Link: PRIAM 2.7.1.21
IntEnz Enzyme Link: IntEnz 2.7.1.21
MEDLINE Enzyme Link: MEDLINE 2.7.1.21
MSA:

2.7.1.21;

Phylogenetic Tree:

2.7.1.21;

Uniprot:
M-CSA:
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