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 ADP + thymidine 5'-diphosphate
thymidylate kinase
Thymidylate kinase dimer, Human
Identifiers
EC no.2.7.4.9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
Thymidylate kinase
Identifiers
SymbolThymidylate_kin
PfamPF02223
InterProIPR000062
PROSITEPDOC01034
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
PDBPDB: 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

References

  1. Li C, Huang SH, Tang A, Drisco B, Zhang SQ, Seeger R, Jong A (1994). "Human dTMP kinase: gene expression and enzymatic activity coinciding with cell cycle progression and cell growth". DNA Cell Biol. 13 (5): 461–471. doi:10.1089/dna.1994.13.461. PMID 8024690.
  • Hurwitz J (1959). "The enzymatic incorporation of ribonucleotides into polydeoxynucleotide material". J. Biol. Chem. 234: 2351–2358. PMID 14405566.
  • 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.
This article incorporates text from the public domain Pfam and InterPro: IPR000062


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