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Thymidylate kinase

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(Redirected from DTMP kinase)
thymidylate kinase
Thymidylate kinase dimer, Human
Identifiers
EC no.2.7.4.9
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins
Thymidylate kinase
Identifiers
SymbolThymidylate_kin
PfamPF02223
InterProIPR000062
PROSITEPDOC01034
Available protein structures:
PDB  PDB: 1e2d PDB: 1e2e PDB: 1e2f PDB: 1e2g PDB: 1e2q PDB: 1e98 PDB: 1e99 PDB: 1e9a PDB: 1e9b PDB: 1e9c IPR000062 PF02223 (ECOD; PDBsum)  
AlphaFold

Thymidylate kinase (EC 2.7.4.9; dTMP kinase) catalyzes the phosphorylation of thymidine monophosphate (dTMP) to form thymidine diphosphate (dTDP) by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP):

The enzyme characterised from Escherichia coli and mouse hepatoma requires magnesium ion Mg2+.[1][2][3]

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.[4]

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

Human protein DTYMK contains this domain.

Structural studies

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As of late 2007, 40 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1E2D, PDB: 1E2E, PDB: 1E2F, PDB: 1E2G, PDB: 1E2Q, PDB: 1E98, PDB: 1E99, PDB: 1E9A, PDB: 1E9B, PDB: 1E9C, PDB: 1E9D, PDB: 1E9E, PDB: 1E9F, PDB: 1G3U, PDB: 1GSI, PDB: 1GTV, PDB: 1MRN, PDB: 1MRS, PDB: 1N5I, PDB: 1N5J, PDB: 1N5K, PDB: 1N5L, PDB: 1NMX, PDB: 1NMY, PDB: 1NMZ, PDB: 1NN0, PDB: 1NN1, PDB: 1NN3, PDB: 1NN5, PDB: 1TMK, PDB: 1W2G, PDB: 1W2H, PDB: 2CCG, PDB: 2CCJ, PDB: 2CCK, PDB: 2PBR, PDB: 2TMK, PDB: 3TMK, PDB: 4TMK, and PDB: 5TMP.

See also

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References

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  1. Hurwitz J (1959). "The enzymatic incorporation of ribonucleotides into polydeoxynucleotide material". J. Biol. Chem. 234 (9): 2351–2358. doi:10.1016/S0021-9258(18)69813-8. PMID 14405566.
  2. Nelson DJ, Carter CE (1969). "Purification and characterization of Thymidine 5-monophosphate kinase from Escherichia coli B". J. Biol. Chem. 244 (19): 5254–62. doi:10.1016/S0021-9258(18)63654-3. PMID 4899016.
  3. Kielley RK (1970). "Purification and properties of thymidine monophosphate kinase from mouse hepatoma". J. Biol. Chem. 245 (16): 4204–12. doi:10.1016/S0021-9258(18)62905-9. PMID 4323166.
  4. 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.
This article incorporates text from the public domain Pfam and InterPro: IPR000062