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Literature summary extracted from

  • Belenky, I.; Steinmetz, A.; Vyazmensky, M.; Barak, Z.; Tittmann, K.; Chipman, D.M.
    Many of the functional differences between acetohydroxyacid synthase (AHAS) isozyme I and other AHASs are a result of the rapid formation and breakdown of the covalent acetolactate-thiamin diphosphate adduct in AHAS I (2012), FEBS J., 279, 1967-1979.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
2.2.1.6 C83A about 91% of wild-type activity Escherichia coli
2.2.1.6 C83S about 126% of wild-type activity Escherichia coli
2.2.1.6 C83T about 41% of wild-type activity Escherichia coli
2.2.1.6 E60A about 48% of wild-type activity Escherichia coli
2.2.1.6 E60Q about 1% of wild-type activity Escherichia coli
2.2.1.6 L476M about 34% of wild-type activity Escherichia coli
2.2.1.6 L476M/Q480W about 47% of wild-type activity Escherichia coli
2.2.1.6 M263A about 16% of wild-type activity Escherichia coli
2.2.1.6 Q480W about 22% of wild-type activity Escherichia coli
2.2.1.6 R269Q about 0.5% of wild-type activity Escherichia coli
2.2.1.6 R289K about 11% of wild-type activity Escherichia coli
2.2.1.6 V391A about 3% of wild-type activity Escherichia coli
2.2.1.6 V477I about 8% of wild-type activity Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.2.1.6 sulfometuron methyl
-
 Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.2.1.6 0.33
-
 pyruvate mutant C83T, pH 7.6, 37°C Escherichia coli
2.2.1.6 1.2
-
 pyruvate mutant C83S, pH 7.6, 37°C Escherichia coli
2.2.1.6 1.5
-
 pyruvate mutant C83A, pH 7.6, 37°C Escherichia coli
2.2.1.6 3.6
-
 pyruvate mutant L476M/Q480W, pH 7.6, 37°C Escherichia coli
2.2.1.6 4.7
-
 pyruvate mutant Q480W, pH 7.6, 37°C Escherichia coli
2.2.1.6 4.8
-
 pyruvate wild-type, pH 7.6, 37°C Escherichia coli
2.2.1.6 8
-
 pyruvate mutant V477I, pH 7.6, 37°C Escherichia coli
2.2.1.6 13
-
 pyruvate mutant L476M, pH 7.6, 37°C Escherichia coli
2.2.1.6 17.9
-
 pyruvate mutant V391A, pH 7.6, 37°C Escherichia coli
2.2.1.6 21
-
 pyruvate mutant E60Q, pH 7.6, 37°C Escherichia coli
2.2.1.6 26
-
 pyruvate mutant M263A, pH 7.6, 37°C Escherichia coli
2.2.1.6 28
-
 pyruvate mutant E60A, pH 7.6, 37°C Escherichia coli
2.2.1.6 50
-
 pyruvate mutant R289K, pH 7.6, 37°C Escherichia coli
2.2.1.6 124
-
 pyruvate mutant R289Q, pH 7.6, 37°C Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.2.1.6 Escherichia coli
-
 isozyme I
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.2.1.6 2 pyruvate
-
 Escherichia coli 2-acetolactate + CO2
-
 ?
2.2.1.6 2-oxobutanoate + pyruvate
-
 Escherichia coli 2-hydroxy-2-methyl-3-oxopentanoate + CO2
-
 ?
2.2.1.6 additional information isozyme I is not specific for 2-oxobutanoate over pyruvate as an acceptor substrate. Residues Gln480 and Met476 in AHAS I replace the Trp and Leu residues conserved in other acetohydroxyacid synthases and lead to accelerated ligation and product release steps. This difference in kinetics accounts for the unique specificity, reversibility and allosteric response of AHAS I Escherichia coli ?
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.2.1.6 2
-
 pyruvate mutant C83T, pH 7.6, 37°C Escherichia coli
2.2.1.6 2
-
 pyruvate mutant E60A, pH 7.6, 37°C Escherichia coli
2.2.1.6 2
-
 pyruvate mutant E60Q, pH 7.6, 37°C Escherichia coli
2.2.1.6 6
-
 pyruvate mutant R289Q, pH 7.6, 37°C Escherichia coli
2.2.1.6 8
-
 pyruvate mutant V391A, pH 7.6, 37°C Escherichia coli
2.2.1.6 9
-
 pyruvate mutant V477I, pH 7.6, 37°C Escherichia coli
2.2.1.6 15
-
 pyruvate mutant Q480W, pH 7.6, 37°C Escherichia coli
2.2.1.6 20
-
 pyruvate mutant C83A, pH 7.6, 37°C Escherichia coli
2.2.1.6 23
-
 pyruvate mutant C83S, pH 7.6, 37°C Escherichia coli
2.2.1.6 25
-
 pyruvate mutant L476M/Q480W, pH 7.6, 37°C Escherichia coli
2.2.1.6 62
-
 pyruvate mutant M263A, pH 7.6, 37°C Escherichia coli
2.2.1.6 65
-
 pyruvate mutant L476M, pH 7.6, 37°C Escherichia coli
2.2.1.6 71
-
 pyruvate wild-type, pH 7.6, 37°C Escherichia coli
2.2.1.6 86
-
 pyruvate mutant R289K, pH 7.6, 37°C Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.2.1.6 0.0044
-
 sulfometuron methyl mutant Q480W, pH 7.6, 37°C Escherichia coli
2.2.1.6 0.041
-
 sulfometuron methyl mutant L476M/Q480W, pH 7.6, 37°C Escherichia coli

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
2.2.1.6 0.05
-
 pyruvate mutant R289Q, pH 7.6, 37°C Escherichia coli
2.2.1.6 0.07
-
 pyruvate mutant E60A, pH 7.6, 37°C Escherichia coli
2.2.1.6 0.1
-
 pyruvate mutant E60Q, pH 7.6, 37°C Escherichia coli
2.2.1.6 0.46
-
 pyruvate mutant V391A, pH 7.6, 37°C Escherichia coli
2.2.1.6 1.2
-
 pyruvate mutant V477I, pH 7.6, 37°C Escherichia coli
2.2.1.6 1.7
-
 pyruvate mutant R289K, pH 7.6, 37°C Escherichia coli
2.2.1.6 2.4
-
 pyruvate mutant M263A, pH 7.6, 37°C Escherichia coli
2.2.1.6 3.3
-
 pyruvate mutant Q480W, pH 7.6, 37°C Escherichia coli
2.2.1.6 5
-
 pyruvate mutant L476M, pH 7.6, 37°C Escherichia coli
2.2.1.6 6.1
-
 pyruvate mutant C83T, pH 7.6, 37°C Escherichia coli
2.2.1.6 6.9
-
 pyruvate mutant L476M/Q480W, pH 7.6, 37°C Escherichia coli
2.2.1.6 13.5
-
 pyruvate mutant C83A, pH 7.6, 37°C Escherichia coli
2.2.1.6 14.9
-
 pyruvate wild-type, pH 7.6, 37°C Escherichia coli
2.2.1.6 18.8
-
 pyruvate mutant C83S, pH 7.6, 37°C Escherichia coli