Hydroxyethylthiazole kinase

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hydroxyethylthiazole kinase
Identifiers
EC no. 2.7.1.50
CAS no. 9026-56-6
Databases
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BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum
Gene Ontology AmiGO / QuickGO
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PMC articles
PubMed articles
NCBI proteins
Hydroxyethylthiazole kinase family
PDB 1c3q EBI.jpg
crystal structure of native thiazole kinase in the monoclinic form
Identifiers
SymbolHK
Pfam PF02110
Pfam clan CL0118
InterPro IPR000417
SCOP2 1c3q / SCOPe / SUPFAM
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

In enzymology, a hydroxyethylthiazole kinase (EC 2.7.1.50) is an enzyme that catalyzes the chemical reaction

Contents

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.

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References

  1. 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.
  2. 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

This article incorporates text from the public domain Pfam and InterPro: IPR000417