Thiamine kinase

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In enzymology, a thiamine kinase (EC 2.7.1.89) is an enzyme that catalyzes the chemical reaction

ATP + thiamine ADP + thiamine phosphate

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

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:thiamine phosphotransferase. Other names in common use include thiamin kinase (phosphorylating), thiamin phosphokinase, ATP:thiamin phosphotransferase, and thiamin kinase. This enzyme participates in thiamine metabolism.

References

  • IUBMB entry for 2.7.1.89
  • BRENDA references for 2.7.1.89 (Recommended.)
  • PubMed references for 2.7.1.89
  • PubMed Central references for 2.7.1.89
  • Google Scholar references for 2.7.1.89
  • Iwashima A, Nishino H, Nose Y (1972). "Conversion of thiamine to thiamine monophosphate by cell-free extracts of Escherichia coli". Biochim. Biophys. Acta. 258: 333&ndash, 6. PMID 4550803.

External links

The CAS registry number for this enzyme class is 62213-38-1.

Gene Ontology (GO) codes


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