Phosphomethylpyrimidine kinase

In enzymology, a phosphomethylpyrimidine kinase (EC number|2.7.4.7) is an enzyme that catalyzes the chemical reaction

:ATP + (4-amino-2-methylpyrimidin-5-yl)methyl phosphate $ightleftharpoons$ ADP + (4-amino-2-methylpyrimidin-5-yl)methyl diphosphate

Thus, the two substrates of this enzyme are ATP and (4-amino-2-methylpyrimidin-5-yl)methyl phosphate, whereas its two products are ADP and (4-amino-2-methylpyrimidin-5-yl)methyl 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:(4-amino-2-methylpyrimidin-5-yl)methyl-phosphate phosphotransferase. Other names in common use include hydroxymethylpyrimidine phosphokinase, and ATP:4-amino-2-methyl-5-phosphomethylpyrimidine phosphotransferase. This enzyme participates in thiamine metabolism.

tructural studies

As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes PDB link|1JXH, PDB link|1JXI, PDB link|1UB0, and PDB link|2I5B.

References

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External links

::"The CAS registry number for this enzyme class is CAS registry|37278-18-5."

Gene Ontology (GO) codes