Hydroxyethylthiazole kinase
| Hydroxyethylthiazole kinase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 2.7.1.50 | ||||||||
| CAS no. | 9026-56-6 | ||||||||
| Databases | |||||||||
| BRENDA | enzyme data | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | enzyme entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| Rhea | reactions | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
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| 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 | ||||||
| |||||||
Hydroxyethylthiazole kinase (EC 2.7.1.50) is an enzyme that catalyzes the chemical reaction
The enzyme characterised from baker's yeast converts 4-methyl-5-thiazoleethanol to 4-methyl-5-hydroxyethylthiazole phosphate by transferring a phosphate group from the cofactor, adenosine triphosphate (ATP), which is converted to adenosine diphosphate (ADP). This reaction is a step in the biosynthesis of thiamine (vitamin B1), together with that catalysed by hydroxymethylpyrimidine kinase.[1][2][3] Hydroxyethylthiazole kinase expression is regulated at the mRNA level by intracellular thiamin pyrophosphate.[4] Thiamine pyrophosphate, a required cofactor for many enzymes in the cell, is synthesised de novo in Salmonella typhimurium.[5]
This enzyme is a transferase, specifically one 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.[6]
Structural studies
As of late 2007, 6 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1C3Q, PDB: 1EKK, PDB: 1EKQ, PDB: 1ESJ, PDB: 1ESQ, and PDB: 1V8A.
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 (10): 2768–2771. doi:10.1016/S0021-9258(19)61734-5.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ 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.
- ↑ Enzyme 2.7.1.50 at KEGG Pathway Database.
External links
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