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Literature summary for 2.2.1.6 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)

Cloned (Comment) Organism
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

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

KM Value [mM]

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

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
additional information Escherichia coli mechanism of expression regulation, overview ?
-
?
pyruvate Escherichia coli first step in the biosynthesis of valine, overview 2-acetolactate + CO2
-
r

Organism

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

Purification (Commentary)

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

Reaction

Reaction Comment Organism Reaction ID
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)

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

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Escherichia coli
60.5
-
reconstituted, recombinant holoenzyme Escherichia coli
63.6
-
recombinant holoenzyme Escherichia coli

Substrates and Products (Substrate)

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

Synonyms

Synonyms Comment Organism
acetohydroxyacid synthase
-
Escherichia coli
AHAS
-
Escherichia coli

Temperature Optimum [°C]

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

Cofactor

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

Ki Value [mM]

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