Phosphomethylpyrimidine kinase (EC 2.7.4.7) is an enzyme that catalyzes the chemical reaction
The enzyme characterised from baker's yeast converts 4-amino-2-methyl-5-phosphooxymethylpyrimidine to 4-amino-2-methyl-5-diphosphooxymethylpyrimidine by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP). The starting material is biosynthesized from toxopyrimidine by the enzyme hydroxymethylpyrimidine kinase. These reactions are steps in the biosynthesis of thiamine (vitamin B1).
This enzyme is a transferase, specifically one 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.
Structural studies As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1JXH, PDB: 1JXI, PDB: 1UB0, and PDB: 2I5B.
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