Thiamine-phosphate diphosphorylase
In enzymology, a thiamine-phosphate diphosphorylase (EC 2.5.1.3) is an enzyme that catalyzes the chemical reaction
- 2-methyl-4-amino-5-hydroxymethylpyrimidine diphosphate + 4-methyl-5-(2-phosphono-oxyethyl)thiazole diphosphate + thiamine phosphate
thiamin-phosphate diphosphorylase | |||||||||
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Identifiers | |||||||||
EC number | 2.5.1.3 | ||||||||
CAS number | 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 | ||||||||
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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 1G4E, 1G4P, 1G4S, 1G4T, 1G67, 1G69, 1G6C, 1XI3, and 2TPS.
References
- CAMIENER GW, BROWN GM (1960). "The biosynthesis of thiamine. 2. Fractionation of enzyme system and identification of thiazole monophosphate and thiamine monophosphate as intermediates". J. Biol. Chem. 235: 2411–7. PMID 13807175.
- Leder IG (1961). "The enzymatic synthesis of thiamine monophosphate". J. Biol. Chem. 236: 3066–3071. PMID 14463407.