Thiamine-phosphate kinase

Class of enzymes From Wikipedia, the free encyclopedia

Thiamine-phosphate kinase (EC 2.7.4.16) is an enzyme that catalyzes the chemical reaction

The enzyme characterised from Escherichia coli converts thiamine monophosphate to thiamine pyrophosphate by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP).[1]

Nomenclature

The enzyme is a transferase, specifically onee 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.[2]

Structural studies

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

References

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