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Literature summary for 2.7.1.50 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
Search for more literature for 2.7.1.50

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
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Reaction

Reaction Comment Organism Reaction ID
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)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + 4-methyl-5-(2-hydroxyethyl)thiazole
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 Bacillus subtilis ADP + 4-methyl-5-(2-phosphoethyl)thiazole
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 ?
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 ?
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 ?

Synonyms

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