Thiamine-phosphate diphosphorylase

In enzymology, a thiamine-phosphate diphosphorylase ( or, thiamine-phosphate pyrophosphorylase ) (EC 2.5.1.3) is an enzyme that catalyzes the chemical reaction

4-Amino-5-hydroxymethyl-2-methylpyrimidine diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole ${\displaystyle \rightleftharpoons }$ diphosphate + thiamine monophosphate

thiamin-phosphate diphosphorylase
Identifiers
EC no.	2.5.1.3
CAS no.	9030-30-2
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
Search PMC articles PubMed articles NCBI proteins

The two substrates of this enzyme are 4-Amino-5-hydroxymethyl-2-methylpyrimidine diphosphate and 4-methyl-5-(2-phosphono-oxyethyl)thiazole; its two products are diphosphate and thiamine monophosphate.

This enzyme belongs to the family of transferases, specifically those transferring aryl or alkyl groups other than methyl groups. This enzyme is on the biosynthetic pathway to thiamine.^[1][2]

Nomenclature

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 synthase,
• thiamine phosphate pyrophosphorylase,
• thiamine monophosphate pyrophosphorylase, and
• TMP-PPase.

Structural studies

As of late 2007, 9 structures have been solved for this class of enzymes, with PDB accession codes 1G4E, 1G4P, 1G4S, 1G4T, 1G67, 1G69, 1G6C, 1XI3, and 2TPS.