dTMP kinase
thymidylate kinase | |||||||||
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Identifiers | |||||||||
EC no. | 2.7.4.9 | ||||||||
CAS no. | 9014-43-1 | ||||||||
Databases | |||||||||
IntEnz | IntEnz view | ||||||||
BRENDA | BRENDA entry | ||||||||
ExPASy | NiceZyme view | ||||||||
KEGG | KEGG entry | ||||||||
MetaCyc | metabolic pathway | ||||||||
PRIAM | profile | ||||||||
PDB structures | RCSB PDB PDBe PDBsum | ||||||||
Gene Ontology | AmiGO / QuickGO | ||||||||
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In enzymology, a dTMP kinase (EC 2.7.4.9) is an enzyme that catalyzes the chemical reaction
- ATP + dTMP ADP + dTDP
Thus, the two substrates of this enzyme are ATP and dTMP, whereas its two products are ADP and dTDP.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with a phosphate group as acceptor. The systematic name of this enzyme class is ATP:dTMP phosphotransferase. Other names in common use include thymidine monophosphate kinase, thymidylate kinase, thymidylate monophosphate kinase, thymidylic acid kinase, thymidylic kinase, deoxythymidine 5'-monophosphate kinase, TMPK, and thymidine 5'-monophosphate kinase. This enzyme participates in pyrimidine metabolism.
Structural studies
As of late 2007, 40 structures have been solved for this class of enzymes, with PDB accession codes 1E2D, 1E2E, 1E2F, 1E2G, 1E2Q, 1E98, 1E99, 1E9A, 1E9B, 1E9C, 1E9D, 1E9E, 1E9F, 1G3U, 1GSI, 1GTV, 1MRN, 1MRS, 1N5I, 1N5J, 1N5K, 1N5L, 1NMX, 1NMY, 1NMZ, 1NN0, 1NN1, 1NN3, 1NN5, 1TMK, 1W2G, 1W2H, 2CCG, 2CCJ, 2CCK, 2PBR, 2TMK, 3TMK, 4TMK, and 5TMP.
References
- Hurwitz J (1959). "The enzymatic incorporation of ribonucleotides into polydeoxynucleotide material". J. Biol. Chem. 234: 2351–2358.
- Kielley RK (1970). "Purification and properties of thymidine monophosphate kinase from mouse hepatoma". J. Biol. Chem. 245 (16): 4204–12. PMID 4323166.
- Nelson DJ, Carter CE (1969). "Purification and characterization of Thymidine 5-monophosphate kinase from Escherichia coli B". J. Biol. Chem. 244 (19): 5254–62. PMID 4899016.