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Literature summary extracted from

  • Vinogradov, V.; Vyazmensky, M.; Engel, S.; Belenky, I.; Kaplun, A.; Kryukov, O.; Barak, Z.; Chipman, D.M.
    Acetohydroxyacid synthase isozyme I from Escherichia coli has unique catalytic and regulatory properties (2006), Biochim. Biophys. Acta, 1760, 356-363.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.2.1.6 isozyme I subunit-encoding genes ilvB and ilvN, DNA and amino acid sequence determination and analysis, expression of His-tagged holoenzyme or individual subunits in strain BL21 Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.2.1.6 benzaldehyde inhibits isozyme AHAS II, not isozyme AHAS I Escherichia coli
2.2.1.6 additional information inhibition kinetics or recombinant wild.type and reconstituted isozymes AHAS I Escherichia coli
2.2.1.6 valine isozyme AHAS I, cooperative feedback inhibition Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.2.1.6 additional information
-
additional information kinetics or recombinant wild-type and reconstituted isozymes AHAS I, exclusive binding model Escherichia coli
2.2.1.6 4
-
pyruvate 37°C, reconstituted, recombinant holoenzyme Escherichia coli
2.2.1.6 4.8
-
pyruvate 37°C, recombinant holoenzyme Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.2.1.6 Mg2+ required 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 additional information Escherichia coli mechanism of expression regulation, overview ?
-
?
2.2.1.6 pyruvate Escherichia coli first step in the biosynthesis of valine, overview 2-acetolactate + CO2
-
r

Organism

EC Number Organism UniProt Comment Textmining
2.2.1.6 Escherichia coli
-
isozymes I-III, subunit-encoding genes ilvB and ilvN
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.2.1.6 recombinant His-tagged isozyme I holoenzyme or individual subunits from strain BL21 by affinity chromatography Escherichia coli

Reaction

EC Number Reaction Comment Organism Reaction ID
2.2.1.6 2 pyruvate = 2-acetolactate + CO2 the enzyme catalyzes the decarboxylation of bound pyruvate to form a hydroxyethyl-thiamine diphosphate anion/enamine intermediate, which normally reacts with a second molecule of an alpha-ketoacid to form an acetohydroxyacid, but can also perform several side reactions proceeding through the hydroxyethyl-thiamine diphosphate anion/enamine intermediate Escherichia coli

Renatured (Commentary)

EC Number Renatured (Comment) Organism
2.2.1.6 reconstitution of the holoenzyme from recombinantly expressed, purified subunits encoded by genes ilvB and ilvN Escherichia coli

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 additional information
-
-
Escherichia coli
2.2.1.6 60.5
-
reconstituted, recombinant holoenzyme Escherichia coli
2.2.1.6 63.6
-
recombinant holoenzyme Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.2.1.6 additional information mechanism of expression regulation, overview Escherichia coli ?
-
?
2.2.1.6 additional information acetohydroxybutyrate is preferably formed, isozyme AHAS I can also form peracetate from synthetic acetolactate Escherichia coli ?
-
?
2.2.1.6 pyruvate
-
Escherichia coli 2-acetolactate + CO2
-
r
2.2.1.6 pyruvate first step in the biosynthesis of valine, overview Escherichia coli 2-acetolactate + CO2
-
r
2.2.1.6 pyruvate + benzaldehyde stereospecific reaction, isozymes AHAS I and II Escherichia coli (R)-phenylacetylcarbinol + CO2
-
?

Synonyms

EC Number Synonyms Comment Organism
2.2.1.6 acetohydroxyacid synthase
-
Escherichia coli
2.2.1.6 AHAS
-
Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.2.1.6 37
-
assay at Escherichia coli

Cofactor

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

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.2.1.6 1.4
-
benzaldehyde isozyme AHAS II Escherichia coli