Phosphomethylpyrimidine kinase

Phosphomethylpyrimidine kinase
Identifiers
EC no.2.7.4.7
CAS no.37278-18-5
Databases
BRENDAenzyme data
ExPASyNiceZyme view
KEGGenzyme entry
MetaCycmetabolic pathway
Rheareactions
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

Phosphomethylpyrimidine kinase (EC 2.7.4.7) is an enzyme that catalyzes the chemical reaction

2D representation of the chemical structure of Q27102775.
4-amino-2-methyl-5-phosphooxymethylpyrimidine
 
Reversible left-right reaction arrow with minor forward substrate(s) from top left, minor forward product(s) to top right, minor reverse substrate(s) from bottom right and minor reverse product(s) to bottom left
ATP
ADP
 
2D representation of the chemical structure of Q27102006.
4-amino-2-methyl-5-diphosphooxymethylpyrimidine

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.[1] These reactions are steps in the biosynthesis of thiamine (vitamin B1).[2]

Thiamine

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.[3]

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​.

References

  1. ↑ Lewin LM, Brown GM (1961). "The biosynthesis of thiamine. III. Mechanism of enzymatic formation of the pyrophosphate ester of 2-methyl-4-amino-5-hydroxymethylpyrimidine". J. Biol. Chem. 236 (10): 2768–2771. doi:10.1016/S0021-9258(19)61734-5.
  2. ↑ Begley TP (February 2006). "Cofactor biosynthesis: an organic chemist's treasure trove". Natural Product Reports. 23 (1): 15–25. doi:10.1039/b207131m. PMID 16453030.
  3. ↑ Enzyme 2.7.4.7 at KEGG Pathway Database.