Hydroxymethylpyrimidine kinase

In enzymology, a hydroxymethylpyrimidine kinase (EC 2.7.1.49) is an enzyme that catalyzes the chemical reaction

ATP + 4-amino-5-hydroxymethyl-2-methylpyrimidine ADP + 4-amino-5-phosphonooxymethyl-2-methylpyrimidine
hydroxymethylpyrimidine kinase
Identifiers
EC no.2.7.1.49
CAS no.9026-55-5
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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NCBIproteins

Thus, the two substrates of this enzyme are ATP and 4-amino-5-hydroxymethyl-2-methylpyrimidine, whereas its two products are ADP and 4-amino-5-phosphonooxymethyl-2-methylpyrimidine.

This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:4-amino-5-hydroxymethyl-2-methylpyrimidine 5-phosphotransferase. This enzyme is also called hydroxymethylpyrimidine kinase (phosphorylating). This enzyme participates in thiamine metabolism.

References

    • 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: 2768–2771.


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