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Literature summary for 4.1.1.72 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

Protein Variants

Protein Variants Comment Organism
Q487A mutation diminishes the decarboxylase activity but maintains the acetolactate synthase activity Bacillus subtilis
Q487G mutation diminishes only the decarboxylase activity but maintains the acetolactate synthase activity Bacillus subtilis
Q487I loss of acetolactate synthase activity, decrease in decarboxylase activity Bacillus subtilis
Q487L loss of acetolactate synthase activity, decrease in decarboxylase activity Bacillus subtilis
Q487S 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
154
-
2-oxoisovalerate mutant Q487S, pH 7.0, 37°C Bacillus subtilis
175
-
2-oxoisovalerate mutant Q487G, pH 7.0, 37°C Bacillus subtilis
186
-
2-oxoisovalerate mutant Q487A, pH 7.0, 37°C Bacillus subtilis
300
-
2-oxoisovalerate wild-type, pH 7.0, 37°C Bacillus subtilis
323
-
2-oxoisovalerate mutant Q487I, pH 7.0, 37°C Bacillus subtilis
342
-
2-oxoisovalerate mutant Q487L, pH 7.0, 37°C Bacillus subtilis

Organism

Organism UniProt Comment Textmining
Bacillus subtilis Q04789 cf. EC 2.2.1.6
-
Bacillus subtilis 168 Q04789 cf. EC 2.2.1.6
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-oxoisovalerate
-
Bacillus subtilis isobutanal + CO2
-
?
2-oxoisovalerate
-
Bacillus subtilis 168 isobutanal + CO2
-
?
additional information acetolactate synthase AlsS, EC 2.2.1.6, is able to catalyze the decarboxylation of 2-oxoisovalerate both in vivo and in vitro Bacillus subtilis ?
-
?
additional information acetolactate synthase AlsS, EC 2.2.1.6, is able to catalyze the decarboxylation of 2-oxoisovalerate both in vivo and in vitro Bacillus subtilis 168 ?
-
?

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
0.8
-
2-oxoisovalerate mutant Q487G, pH 7.0, 37°C Bacillus subtilis
0.8
-
2-oxoisovalerate mutant Q487S, pH 7.0, 37°C Bacillus subtilis
1.1
-
2-oxoisovalerate mutant Q487A, pH 7.0, 37°C Bacillus subtilis
4.8
-
2-oxoisovalerate mutant Q487I, pH 7.0, 37°C Bacillus subtilis
5.4
-
2-oxoisovalerate mutant Q487L, pH 7.0, 37°C Bacillus subtilis
8.9
-
2-oxoisovalerate 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
0.005
-
2-oxoisovalerate mutant Q487G, pH 7.0, 37°C Bacillus subtilis
0.005
-
2-oxoisovalerate mutant Q487S, pH 7.0, 37°C Bacillus subtilis
0.006
-
2-oxoisovalerate mutant Q487A, pH 7.0, 37°C Bacillus subtilis
0.01
-
2-oxoisovalerate mutant Q487I, pH 7.0, 37°C Bacillus subtilis
0.02
-
2-oxoisovalerate mutant Q487L, pH 7.0, 37°C Bacillus subtilis
0.03
-
2-oxoisovalerate wild-type, pH 7.0, 37°C Bacillus subtilis