thymidylate kinase

{{infobox enzyme

| Name = thymidylate kinase

| EC_number = 2.7.4.9

| GO_code = 0004798

| image = 1e2d.jpg

| width = 270

| caption = Thymidylate kinase dimer, Human

}}

{{Pfam box |Symbol = Thymidylate_kin |Name = Thymidylate kinase |Pfam = PF02223 |InterPro = IPR000062 |PROSITE = PDOC01034 |PDB = {{PDB|1e2d}} {{PDB|1e2e}} {{PDB|1e2f}} {{PDB|1e2g}} {{PDB|1e2q}} {{PDB|1e98}} {{PDB|1e99}} {{PDB|1e9a}} {{PDB|1e9b}} {{PDB|1e9c}} }}

Thymidylate kinase ({{EC number|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 $\rightleftharpoons$ ADP + thymidine 5'-diphosphate

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.{{cite journal |vauthors=Li C, Huang SH, Tang A, Drisco B, Zhang SQ, Seeger R, Jong A |title=Human dTMP kinase: gene expression and enzymatic activity coinciding with cell cycle progression and cell growth |journal=DNA Cell Biol. |volume=13 |issue=5 |pages=461–471 |year=1994 |pmid=8024690 |doi=10.1089/dna.1994.13.461}}

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 {{PDB link|1E2D}}, {{PDB link|1E2E}}, {{PDB link|1E2F}}, {{PDB link|1E2G}}, {{PDB link|1E2Q}}, {{PDB link|1E98}}, {{PDB link|1E99}}, {{PDB link|1E9A}}, {{PDB link|1E9B}}, {{PDB link|1E9C}}, {{PDB link|1E9D}}, {{PDB link|1E9E}}, {{PDB link|1E9F}}, {{PDB link|1G3U}}, {{PDB link|1GSI}}, {{PDB link|1GTV}}, {{PDB link|1MRN}}, {{PDB link|1MRS}}, {{PDB link|1N5I}}, {{PDB link|1N5J}}, {{PDB link|1N5K}}, {{PDB link|1N5L}}, {{PDB link|1NMX}}, {{PDB link|1NMY}}, {{PDB link|1NMZ}}, {{PDB link|1NN0}}, {{PDB link|1NN1}}, {{PDB link|1NN3}}, {{PDB link|1NN5}}, {{PDB link|1TMK}}, {{PDB link|1W2G}}, {{PDB link|1W2H}}, {{PDB link|2CCG}}, {{PDB link|2CCJ}}, {{PDB link|2CCK}}, {{PDB link|2PBR}}, {{PDB link|2TMK}}, {{PDB link|3TMK}}, {{PDB link|4TMK}}, and {{PDB link|5TMP}}.

References

{{cite journal | author = Hurwitz J | date = 1959 | title = The enzymatic incorporation of ribonucleotides into polydeoxynucleotide material | journal = J. Biol. Chem. | volume = 234 | issue = 9 | pages = 2351–2358 | doi = 10.1016/S0021-9258(18)69813-8 | pmid = 14405566 | doi-access = free }}
{{cite journal | author = Kielley RK | date = 1970 | title = Purification and properties of thymidine monophosphate kinase from mouse hepatoma | journal = J. Biol. Chem. | volume = 245 | pages = 4204–12 | pmid = 4323166 | issue = 16 | doi = 10.1016/S0021-9258(18)62905-9 | doi-access = free }}
{{cite journal |vauthors=Nelson DJ, Carter CE | date = 1969 | title = Purification and characterization of Thymidine 5-monophosphate kinase from Escherichia coli B | journal = J. Biol. Chem. | volume = 244 | pages = 5254–62 | pmid = 4899016 | issue = 19 | doi = 10.1016/S0021-9258(18)63654-3 | doi-access = free }}

Category:Protein families

Category:EC 2.7.4

Category:Enzymes of known structure

thymidylate kinase

Structural studies

See also

References