In enzymology, a hydroxyethylthiazole kinase (EC 2.7.1.50) is an enzyme that catalyzes the chemical reaction
| hydroxyethylthiazole kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.1.50 | ||||||||
| CAS no. | 9026-56-6 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
| Hydroxyethylthiazole kinase family | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 crystal structure of native thiazole kinase in the monoclinic form | |||||||||
| Identifiers | |||||||||
| Symbol | HK | ||||||||
| Pfam | PF02110 | ||||||||
| Pfam clan | CL0118 | ||||||||
| InterPro | IPR000417 | ||||||||
| SCOP2 | 1c3q / SCOPe / SUPFAM | ||||||||
| |||||||||
- 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
editAs 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
edit- ^ Petersen LA, Downs DM (August 1997). "Identification and characterization of an operon in Salmonella typhimurium involved in thiamine biosynthesis". J. Bacteriol. 179 (15): 4894–900. doi:10.1128/jb.179.15.4894-4900.1997. PMC 179339. PMID 9244280.
- ^ Nosaka K, Nishimura H, Kawasaki Y, Tsujihara T, Iwashima A (December 1994). "Isolation and characterization of the THI6 gene encoding a bifunctional thiamin-phosphate pyrophosphorylase/hydroxyethylthiazole kinase from Saccharomyces cerevisiae". J. Biol. Chem. 269 (48): 30510–6. doi:10.1016/S0021-9258(18)43843-4. PMID 7982968.
Further reading
edit- 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.
