Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Dyguda, E.; Szefczyk, B.; Sokalski, W.A.
    The mechanism of phosphoryl transfer reaction and the role of active site residues on the basis of ribokinase-like kinases (2004), Int. J. Mol. Sci., 5, 141-153.
No PubMed abstract available

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.1.50 Mg2+ stabilizes the transition state and the phosphoryl goup Bacillus subtilis

Organism

EC Number Organism UniProt Comment Textmining
2.7.1.50 Bacillus subtilis
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.1.50 ATP + 4-methyl-5-(2-hydroxyethyl)thiazole = ADP + 4-methyl-5-(2-phosphooxyethyl)thiazole catalytic mechanism of phosphoryl transfer reaction and role of active site residues, e.g. R121 and C198, calculated on the basis of data on crystal structures of ribokinase-like kinases, transition state stabilization involves an oxyanion hole and a magnesium ion Bacillus subtilis
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.1.50 ATP + 4-methyl-5-(2-hydroxyethyl)thiazole
-
 Bacillus subtilis ADP + 4-methyl-5-(2-phosphoethyl)thiazole
-
 ?
2.7.1.50 additional information ATP-dependent phosphorylation of small molecules containing hydroxymethyl groups, reaction pathway mapping, molecular mechanism optimization and quantum mechanis calculations on the basis of enzyme crystal structure, PDB code 1C3Q and 1ESQ, overview Bacillus subtilis ?
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.7.1.50 4-methyl-5-beta-hydroxyethylthiazole kinase
-
 Bacillus subtilis
2.7.1.50 More the enzyme belongs to the family of ribokinase-like carbohydrate kinases Bacillus subtilis
2.7.1.50 ThiK
-
 Bacillus subtilis
2.7.1.50 THZ kinase
-
 Bacillus subtilis