Thiamine-phosphate diphosphorylase

In enzymology, a thiamine-phosphate diphosphorylase is an enzyme that catalyzes the chemical reaction


 * 2-methyl-4-amino-5-hydroxymethylpyrimidine diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole $$\rightleftharpoons$$ diphosphate + thiamine phosphate

Thus, the two substrates of this enzyme are 2-methyl-4-amino-5-hydroxymethylpyrimidine diphosphate and 4-methyl-5-(2-phosphono-oxyethyl)thiazole, whereas its two products are diphosphate and thiamine phosphate.

This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. The systematic name of this enzyme class is 2-methyl-4-amino-5-hydroxymethylpyrimidine-diphosphate:4-methyl-5-(2 -phosphoethyl)thiazole 2-methyl-4-aminopyrimidine-5-methenyltransferase. Other names in common use include thiamine phosphate pyrophosphorylase, thiamine monophosphate pyrophosphorylase, and TMP-PPase. This enzyme participates in thiamine metabolism.

Structural studies
As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes, , , , , , , , and.