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Literature summary extracted from

  • Kaplun, A.; Vyazmensky, M.; Zherdev, Y.; Belenky, I.; Slutzker, A.; Mendel, S.; Barak, Z.; Chipman, D.M.; Shaanan, B.
    Structure of the regulatory subunit of acetohydroxyacid synthase isozyme III from Escherichia coli (2006), J. Mol. Biol., 357, 951-963.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.2.1.6 gene ilvH, encoding the regulatory subunit SSU, expression of wild-type and mutants, and of the selenomethionine variant Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.2.1.6 purified recombinant wild-type and selenomethionine-labeled isozyme AHAS III in complex with valine, hanging drop vapour diffusion method, room temperature, 0.0036 ml of protein solution containing 10-25 mg/ml protein and 0.5 M MgCl2, is mixed with reservoir solution containing 30-40% PEG 400, 0.4-0.6 M MgCl2, 100 mM Tris-HCl, pH 8.5, tetragonal or orthorhombic crystals, X-ray diffraction structure determination and analysis at 1.75-2.5 A resolution Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
2.2.1.6 A36V site-directed mutagenesis of the regulatory subunit, the mutant is resistant to inhibition by valine Escherichia coli
2.2.1.6 G14A site-directed mutagenesis of the regulatory subunit, the mutant is resistant to inhibition by valine Escherichia coli
2.2.1.6 G14D site-directed mutagenesis of the regulatory subunit, the mutant is resistant to inhibition by valine Escherichia coli
2.2.1.6 L131R site-directed mutagenesis of the regulatory subunit, the mutant is resistant to inhibition by valine Escherichia coli
2.2.1.6 L16A site-directed mutagenesis of the regulatory subunit, the mutant shows increased sensitivity to valine inhibition compared to the wild-type subunit Escherichia coli
2.2.1.6 L9A site-directed mutagenesis of the regulatory subunit, the mutant shows slightly decreased sensitivity to valine inhibition compared to the wild-type subunit Escherichia coli
2.2.1.6 L9H site-directed mutagenesis of the regulatory subunit, the mutant is resistant to inhibition by valine Escherichia coli
2.2.1.6 L9V site-directed mutagenesis of the regulatory subunit, the mutant shows slightly decreased sensitivity to valine inhibition compared to the wild-type subunit Escherichia coli
2.2.1.6 additional information the truncated mutant DELTA80 is resistant to inhibition by valine Escherichia coli
2.2.1.6 N11A site-directed mutagenesis of the regulatory subunit, the mutant is resistant to inhibition by valine Escherichia coli
2.2.1.6 N11D site-directed mutagenesis of the regulatory subunit, the mutant shows highly decreased sensitivity to valine inhibition compared to the wild-type subunit Escherichia coli
2.2.1.6 N11H site-directed mutagenesis of the regulatory subunit, the mutant shows highly decreased sensitivity to valine inhibition compared to the wild-type subunit Escherichia coli
2.2.1.6 N29D site-directed mutagenesis of the regulatory subunit, the mutant shows highly decreased sensitivity to valine inhibition compared to the wild-type subunit Escherichia coli
2.2.1.6 N29H site-directed mutagenesis of the regulatory subunit, the mutant shows highly decreased sensitivity to valine inhibition compared to the wild-type subunit Escherichia coli
2.2.1.6 T34C site-directed mutagenesis of the regulatory subunit, the mutant shows decreased sensitivity to valine inhibition compared to the wild-type subunit Escherichia coli
2.2.1.6 T34I site-directed mutagenesis of the regulatory subunit, the mutant shows highly decreased sensitivity to valine inhibition compared to the wild-type subunit Escherichia coli
2.2.1.6 T47C site-directed mutagenesis of the regulatory subunit, the mutant shows decreased sensitivity to valine inhibition compared to the wild-type subunit Escherichia coli
2.2.1.6 V153D site-directed mutagenesis of the regulatory subunit, the mutant is resistant to inhibition by valine Escherichia coli
2.2.1.6 V35A site-directed mutagenesis of the regulatory subunit, the mutant shows decreased sensitivity to valine inhibition compared to the wild-type subunit Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.2.1.6 valine binding site structure, inhibition mechanism Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.2.1.6 Mg2+ activates, binding structure at the regulatory subunit Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.2.1.6 pyruvate Escherichia coli the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine 2-acetolactate + CO2
-
 ?

Organism

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

Renatured (Commentary)

EC Number Renatured (Comment) Organism
2.2.1.6 reconstitution of the holoenzyme from recombinant small and large subunits, not highly dependent on MgCl2, but when no extraneous magnesium is added the enzyme does not reach its full potential for activity Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.2.1.6 pyruvate
-
 Escherichia coli 2-acetolactate + CO2
-
 ?
2.2.1.6 pyruvate the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine Escherichia coli 2-acetolactate + CO2
-
 ?

Subunits

EC Number Subunits Comment Organism
2.2.1.6 More enzymes in the AHAS family generally consist of regulatory and catalytic subunits, subunit composition, dimeric structure analysis of the regulatory subunit of isozyme AHAS III, overview Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
2.2.1.6 acetohydroxy acid synthase
-
 Escherichia coli
2.2.1.6 AHAS
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
2.2.1.6 FAD
-
 Escherichia coli
2.2.1.6 thiamine diphosphate
-
 Escherichia coli