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Literature summary for 4.2.3.1 extracted from

  • Skarstedt, M.T.; Greer, S.B.
    Threonine synthetase of Bacillus subtilis. The nature of an associated dehydratase activity (1973), J. Biol. Chem., 248, 1032-1044.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
L-cysteine
-
Bacillus subtilis
sulfate
-
Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
wild type and various mutant enzymes
-

Purification (Commentary)

Purification (Comment) Organism
partial Bacillus subtilis

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.014
-
mutation Ile-3 Bacillus subtilis
0.018
-
wild type Bacillus subtilis
8.8
-
mutation SprA-44 Bacillus subtilis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
O-phospho-L-homoserine + H2O
-
Bacillus subtilis L-threonine + phosphate
-
ir
threonine genetic evidence for identity of protein with both activities Bacillus subtilis 2-oxobutyrate + NH3
-
ir

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
enzyme assay at Bacillus subtilis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
enzyme assay at Bacillus subtilis

Cofactor

Cofactor Comment Organism Structure
pyridoxal 5'-phosphate
-
Bacillus subtilis