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 monophosphate
thiamin-phosphate diphosphorylase
Identifiers
EC no.2.5.1.3
CAS no.9030-30-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

The two substrates of this enzyme are 2-methyl-4-amino-5-hydroxymethylpyrimidine 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.

References
  1. Caspi R (2011-09-14). "Pathway: superpathway of thiamine diphosphate biosynthesis I". MetaCyc Metabolic Pathway Database. Retrieved 2022-02-01.
  2. Ajjawi I, Tsegaye Y, Shintani D (March 2007). "Determination of the genetic, molecular, and biochemical basis of the Arabidopsis thaliana thiamin auxotroph th1". Archives of Biochemistry and Biophysics. 459 (1): 107–114. doi:10.1016/j.abb.2006.11.011. PMID 17174261.

Further reading
  • Camiener GW, Brown GM (August 1960). "The biosynthesis of thiamine. 2. Fractionation of enzyme system and identification of thiazole monophosphate and thiamine monophosphate as intermediates". The Journal of Biological Chemistry. 235: 2411–2417. PMID 13807175.
  • Leder IG (November 1961). "The enzymatic synthesis of thiamine monophosphate". The Journal of Biological Chemistry. 236: 3066–3071. PMID 14463407.


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