Thiamine-phosphate kinase

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In enzymology, a thiamine-phosphate kinase (EC 2.7.4.16) is an enzyme that catalyzes the chemical reaction

ATP + thiamine phosphate ADP + thiamine diphosphate

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

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-phosphate phosphotransferase. Other names in common use include thiamin-monophosphate kinase, thiamin monophosphatase, and thiamin monophosphokinase. This enzyme participates in thiamine metabolism.

Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1VQV.

References

  • IUBMB entry for 2.7.4.16
  • BRENDA references for 2.7.4.16 (Recommended.)
  • PubMed references for 2.7.4.16
  • PubMed Central references for 2.7.4.16
  • Google Scholar references for 2.7.4.16
  • Nishino H (Tokyo). "Biogenesis of cocarboxylase in Escherichia coli. Partial purification and some properties of thiamine monophosphate kinase". J. Biochem.: 1093&ndash, 100. PMID 4567662. Check date values in: |date= (help)

External links

The CAS registry number for this enzyme class is 9068-23-9.

Gene Ontology (GO) codes


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