Thymidylate kinase

Thymidylate kinase (EC 2.7.4.9; dTMP kinase) catalyzes the phosphorylation of thymidine 5'-monophosphate (dTMP) to form thymidine 5'-diphosphate (dTDP) in the presence of ATP and magnesium:

ATP + thymidine 5'-phosphate ${\displaystyle \rightleftharpoons }$ ADP + thymidine 5'-diphosphate

thymidylate kinase
Thymidylate kinase dimer, Human
Identifiers
EC no.	2.7.4.9
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
Search PMC articles PubMed articles NCBI proteins

Thymidylate kinase
Identifiers
Symbol	Thymidylate_kin
Pfam	PF02223
InterPro	IPR000062
PROSITE	PDOC01034
Available protein structures: Pfam   structures / ECOD   PDB RCSB PDB; PDBe; PDBj PDBsum structure summary PDB PDB: 1e2d​ PDB: 1e2e​ PDB: 1e2f​ PDB: 1e2g​ PDB: 1e2q​ PDB: 1e98​ PDB: 1e99​ PDB: 1e9a​ PDB: 1e9b​ PDB: 1e9c​

Thymidylate kinase is a ubiquitous enzyme of about 25 Kd and is important in the dTTP synthesis pathway for DNA synthesis. The function of dTMP kinase in eukaryotes comes from the study of a cell cycle mutant, cdc8, in Saccharomyces cerevisiae. Structural and functional analyses suggest that the cDNA codes for authentic human dTMP kinase. The mRNA levels and enzyme activities corresponded to cell cycle progression and cell growth stages.^[1]

Thymidylate kinase's subfamily is predicted thymidylate kinase, TKRP1. InterPro: IPR014505

Human protein DTYMK contains this domain.

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.

See also

• Thymidine kinase
• Thymidylate synthase
• Thymidine kinase in clinical chemistry