Hydroxyethylthiazole kinase
In enzymology, a hydroxyethylthiazole kinase (EC 2.7.1.50) is an enzyme that catalyzes the chemical reaction
- ATP + 4-methyl-5-(2-hydroxyethyl)thiazole
ADP + 4-methyl-5-(2-phosphonooxyethyl)thiazole
Thus, the two substrates of this enzyme are ATP and 4-methyl-5-(2-hydroxyethyl)thiazole, whereas its two products are ADP and 4-methyl-5-(2-phosphonooxyethyl)thiazole.
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-methyl-5-(2-hydroxyethyl)thiazole 2-phosphotransferase. Other names in common use include hydroxyethylthiazole kinase (phosphorylating), and 4-methyl-5-(beta-hydroxyethyl)thiazole kinase. This enzyme participates in thiamine metabolism. Thiamine pyrophosphate (TPP), a required cofactor for many enzymes in the cell, is synthesised de novo in Salmonella typhimurium.[1]
In Saccharomyces cerevisiae, hydroxyethylthiazole kinase expression is regulated at the mRNA level by intracellular thiamin pyrophosphate.[2]
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes 1C3Q, 1EKK, 1EKQ, 1ESJ, 1ESQ, and 1V8A.
References
Further reading
- 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.
This article incorporates text from the public domain Pfam and InterPro IPR000417
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