Thiamine-phosphate kinase

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thiamin phosphate kinase
Identifiers
EC no. 2.7.4.16
CAS no. 9068-23-9
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
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PMC articles
PubMed articles
NCBI proteins

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.

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References


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