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Literature summary for 2.2.1.6 extracted from

  • Atsumi, S.; Li, Z.; Liao, J.C.
    Acetolactate synthase from Bacillus subtilis serves as a 2-ketoisovalerate decarboxylase for isobutanol biosynthesis in Escherichia coli (2009), Appl. Environ. Microbiol., 75, 6306-6311.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 2.2.1.6

Protein Variants

Protein Variants Comment Organism
Q487A mutation diminishes decarboxylase activity but maintains the synthase activity Bacillus subtilis
Q487A wild-type additionally catalyzes the decarboxylation of 2-oxoisovalerate. Mutation diminishes only the decarboxylase activity but maintains the acetolactate synthase activity Bacillus subtilis
Q487G mutation diminishes decarboxylase activity but maintains the synthase activity Bacillus subtilis
Q487G wild-type additionally catalyzes the decarboxylation of 2-oxoisovalerate. Mutation diminishes only the decarboxylase activity but maintains the acetolactate synthase activity Bacillus subtilis
Q487I complete loss of synthase activity Bacillus subtilis
Q487I loss of acetolactate synthase activity, decrease in decarboxylase activity Bacillus subtilis
Q487L complete loss of synthase activity Bacillus subtilis
Q487L loss of acetolactate synthase activity, decrease in decarboxylase activity Bacillus subtilis
Q487S mutation diminishes decarboxylase activity but maintains the synthase activity Bacillus subtilis
Q487S wild-type additionally catalyzes the decarboxylation of 2-oxoisovalerate. Mutation diminishes only the decarboxylase activity but maintains the acetolactate synthase activity Bacillus subtilis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1
-
 pyruvate mutant Q487S, pH 7.0, 37°C Bacillus subtilis
1.6
-
 pyruvate mutant Q487G, pH 7.0, 37°C Bacillus subtilis
8.7
-
 pyruvate mutant Q487A, pH 7.0, 37°C Bacillus subtilis
13.6
-
 pyruvate wild-type, pH 7.0, 37°C Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis
-
-
-
Bacillus subtilis Q04789
-
-
Bacillus subtilis 168 Q04789
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2 pyruvate
-
 Bacillus subtilis 2-acetolactate + CO2
-
 ?
2 pyruvate
-
 Bacillus subtilis 168 2-acetolactate + CO2
-
 ?
additional information enzyme additionallly displays 2-ketoisovalerate decarboxylase activity Bacillus subtilis ?
-
 ?
additional information acetolactate synthase AlsS is able to catalyze the decarboxylation of 2-oxoisovalerate both in vivo and in vitro Bacillus subtilis ?
-
 ?
additional information acetolactate synthase AlsS is able to catalyze the decarboxylation of 2-oxoisovalerate both in vivo and in vitro Bacillus subtilis 168 ?
-
 ?
pyruvate
-
 Bacillus subtilis (S)-2-acetolactate + CO2
-
 ?

Synonyms

Synonyms Comment Organism
AlsS
-
 Bacillus subtilis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
11
-
 pyruvate mutant Q487G, pH 7.0, 37°C Bacillus subtilis
11
-
 pyruvate mutant Q487S, pH 7.0, 37°C Bacillus subtilis
58
-
 pyruvate mutant Q487A, pH 7.0, 37°C Bacillus subtilis
121
-
 pyruvate wild-type, pH 7.0, 37°C Bacillus subtilis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
6.7
-
 pyruvate mutant Q487A, pH 7.0, 37°C Bacillus subtilis
6.9
-
 pyruvate mutant Q487G, pH 7.0, 37°C Bacillus subtilis
8.9
-
 pyruvate wild-type, pH 7.0, 37°C Bacillus subtilis
10
-
 pyruvate mutant Q487S, pH 7.0, 37°C Bacillus subtilis