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Thiamine-phosphate kinase

From Wikipedia, the free encyclopedia
thiamin phosphate kinase
Identifiers
EC no.2.7.4.16
CAS no.9068-23-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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

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

References

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  • Nishino H (November 1972). "Biogenesis of cocarboxylase in Escherichia coli. Partial purification and some properties of thiamine monophosphate kinase". Journal of Biochemistry. 72 (5): 1093–100. doi:10.1093/oxfordjournals.jbchem.a129996. PMID 4567662.