Phosphomethylpyrimidine kinase

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In enzymology, a phosphomethylpyrimidine kinase (EC 2.7.4.7) is an enzyme that catalyzes the chemical reaction

ATP + (4-amino-2-methylpyrimidin-5-yl)methyl phosphate $\rightleftharpoons$ ADP + (4-amino-2-methylpyrimidin-5-yl)methyl diphosphate

Thus, the two substrates of this enzyme are ATP and (4-amino-2-methylpyrimidin-5-yl)methyl phosphate, whereas its two products are ADP and (4-amino-2-methylpyrimidin-5-yl)methyl diphosphate.

This enzyme belongs to the family of transferases, specifically those 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. This enzyme participates in thiamine metabolism.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, 4 structures have been solved for this class of enzymes, with PDB accession codes 1JXH, 1JXI, 1UB0, and 2I5B.

[edit] References

IUBMB entry for 2.7.4.7
BRENDA references for 2.7.4.7 (Recommended.)
PubMed references for 2.7.4.7
PubMed Central references for 2.7.4.7
Google Scholar references for 2.7.4.7
Lewin LM and 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: 2768–2771.