Thiamine-diphosphate kinase

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In enzymology, a thiamine-diphosphate kinase (EC 2.7.4.15) is an enzyme that catalyzes the chemical reaction

ATP + thiamine diphosphate $\rightleftharpoons$ ADP + thiamine triphosphate

Thus, the two substrates of this enzyme are ATP and thiamine diphosphate, whereas its two products are ADP and thiamine triphosphate.

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:thiamine-diphosphate phosphotransferase. Other names in common use include ATP:thiamin-diphosphate phosphotransferase, TDP kinase, thiamin diphosphate kinase, thiamin diphosphate phosphotransferase, thiamin pyrophosphate kinase, thiamine diphosphate kinase, and protein bound thiamin diphosphate:ATP phosphoryltransferase. This enzyme participates in thiamine metabolism.

[edit] References

IUBMB entry for 2.7.4.15
BRENDA references for 2.7.4.15 (Recommended.)
PubMed references for 2.7.4.15
PubMed Central references for 2.7.4.15
Google Scholar references for 2.7.4.15
Itokawa Y, Cooper JR (1968). "The enzymatic synthesis of triphosphothiamin". Biochim. Biophys. Acta. 158: 180–2. PMID 5661031.
Kikuchi M and Ikawa T (Tokyo). "Presence of an enzyme mediating transfer of phosphate from thiamine triphosphate to ADP in germinating maize". Bot. Mag.: 193–205.