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Literature summary extracted from

  • Choi, K.; Pham, C.N.; Jung, H.; Han, S.; Choi, J.; Kim, J.; Yoon, M.
    Expression of acetohydroxyacid synthase from Bacillus anthracis and its potent inhibitors (2007), Bull. Korean Chem. Soc., 28, 1109-1113.
No PubMed abstract available

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.2.1.6 gene AHAS, expression of the His-tagged enzyme in Escherichia coli strain BL21(DE3), the enzyme contains additional 34 residues, MGSSHHHHHHSSGLVPRGSHMASMTGGQQMGRGS, at the N-terminus Bacillus anthracis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.2.1.6 Cadre an imidazolinone herbicide Bacillus anthracis
2.2.1.6 Londax a sulfonylurea herbicide Bacillus anthracis
2.2.1.6 additional information AHAS from Bacillus anthracis shows strong resistance to three classes of herbicides, the sulfonylurea Londax, the imidazolinone Cadre, and the triazolopyrimidine TP Bacillus anthracis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.2.1.6 0.28
-
 thiamine diphosphate
-
 Bacillus anthracis
2.2.1.6 4.8
-
 pyruvate pH 7.4, 37°C, recombinant enzyme Bacillus anthracis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.2.1.6 Mg2+ K0.5 is 1.160 mM Bacillus anthracis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.2.1.6 65000
-
 x * 65000, recombinant enzyme, SDS-PAGE Bacillus anthracis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.2.1.6 2 pyruvate Bacillus anthracis acetohydroxyacid synthase is the enzyme that catalyses the first step in the common pathway of the biosynthesis of the branched chain amino acids, valine, leucine and isoleucine 2-acetolactate + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
2.2.1.6 Bacillus anthracis
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.2.1.6 His-tagged recombinant enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography to 96% purity Bacillus anthracis

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.2.1.6 1.5
-
 calculated per subunit, purified recombinant His-tagged enzyme Bacillus anthracis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.2.1.6 2 pyruvate
-
 Bacillus anthracis 2-acetolactate + CO2
-
 ?
2.2.1.6 2 pyruvate acetohydroxyacid synthase is the enzyme that catalyses the first step in the common pathway of the biosynthesis of the branched chain amino acids, valine, leucine and isoleucine Bacillus anthracis 2-acetolactate + CO2
-
 ?

Subunits

EC Number Subunits Comment Organism
2.2.1.6 ? x * 65000, recombinant enzyme, SDS-PAGE Bacillus anthracis

Synonyms

EC Number Synonyms Comment Organism
2.2.1.6 acetohydroxyacid synthase
-
 Bacillus anthracis
2.2.1.6 AHAS
-
 Bacillus anthracis

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.2.1.6 37
-
-
 Bacillus anthracis

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
2.2.1.6 10 50 30°C: about 50% of maximal activity, 50°C: about 65% of maximal activity, temperature profile Bacillus anthracis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.2.1.6 7.5
-
-
 Bacillus anthracis

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.2.1.6 5 10 pH 6.5: about 40% of maximal activity, pH 10.0: about 65% of maximal activity, pH profile Bacillus anthracis

Cofactor

EC Number Cofactor Comment Organism Structure
2.2.1.6 FAD
-
 Bacillus anthracis
2.2.1.6 thiamine diphosphate
-
 Bacillus anthracis