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Literature summary extracted from

  • Choi, K.J.; Yu, Y.G.; Hahn, H.G.; Choi, J.D.; Yoon, M.Y.
    Characterization of acetohydroxyacid synthase from Mycobacterium tuberculosis and the identification of its new inhibitor from the screening of a chemical library (2005), FEBS Lett., 579, 4903-4910.
    View publication on PubMed

Application

EC Number Application Comment Organism
2.2.1.6 pharmacology AHAS might be a target protein for the development of anti-tuberculosis therapeutics Mycobacterium tuberculosis

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.2.1.6 inducible overexpression of the His-tagged enzyme subunits in Escherichia coli strain BL21(DE3) Mycobacterium tuberculosis

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.2.1.6 KHG20612 inhibition kinetics and antimycobacterial activity, overview Mycobacterium tuberculosis
2.2.1.6 additional information screening of chemical libraries for effective inhibitors of the enzyme, overview Mycobacterium tuberculosis
2.2.1.6 pyrazosulfuron ethyl IC50: 870 nM Mycobacterium tuberculosis
2.2.1.6 valine
-
Mycobacterium tuberculosis

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 Mycobacterium tuberculosis
2.2.1.6 1.56
-
pyruvate pH 7.0, 37°C, holoenzyme Mycobacterium tuberculosis
2.2.1.6 2.76
-
pyruvate pH 7.0, 37°C, catalytic subunit Mycobacterium tuberculosis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.2.1.6 Mg2+ activates Mycobacterium tuberculosis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.2.1.6 20400
-
x * 68300, recombinant His-tagged catalytic subunit, + x * 20400, recombinant His-tagged regulatory subunit, SDS-PAGE Mycobacterium tuberculosis
2.2.1.6 68300
-
x * 68300, recombinant His-tagged catalytic subunit, + x * 20400, recombinant His-tagged regulatory subunit, SDS-PAGE Mycobacterium tuberculosis
2.2.1.6 300000
-
above, recombinant holoenzyme, gel filtration Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.2.1.6 pyruvate Mycobacterium tuberculosis the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine 2-acetolactate + CO2
-
?
2.2.1.6 pyruvate Mycobacterium tuberculosis H37Rv 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 Mycobacterium tuberculosis
-
-
-
2.2.1.6 Mycobacterium tuberculosis H37Rv
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.2.1.6 recombinant His-tagged enzyme subunits from Escherichia coli to homogeneity by nickel affinity chromatography and dialysis Mycobacterium tuberculosis

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 2.8
-
purified catalytic subunit Mycobacterium tuberculosis
2.2.1.6 4.6
-
purified holoenzyme Mycobacterium tuberculosis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.2.1.6 pyruvate
-
Mycobacterium tuberculosis 2-acetolactate + CO2
-
?
2.2.1.6 pyruvate the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine Mycobacterium tuberculosis 2-acetolactate + CO2
-
?
2.2.1.6 pyruvate
-
Mycobacterium tuberculosis H37Rv 2-acetolactate + CO2
-
?
2.2.1.6 pyruvate the enzyme catalyzes the first committed step in the biosynthesis of valine, leucine, and isoleucine Mycobacterium tuberculosis H37Rv 2-acetolactate + CO2
-
?

Subunits

EC Number Subunits Comment Organism
2.2.1.6 oligomer x * 68300, recombinant His-tagged catalytic subunit, + x * 20400, recombinant His-tagged regulatory subunit, SDS-PAGE Mycobacterium tuberculosis

Synonyms

EC Number Synonyms Comment Organism
2.2.1.6 acetohydroxy acid synthase
-
Mycobacterium tuberculosis
2.2.1.6 AHAS
-
Mycobacterium tuberculosis

Temperature Optimum [°C]

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

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.2.1.6 6 8 catalytic subunit Mycobacterium tuberculosis
2.2.1.6 7
-
holoenzyme Mycobacterium tuberculosis

Cofactor

EC Number Cofactor Comment Organism Structure
2.2.1.6 FAD
-
Mycobacterium tuberculosis
2.2.1.6 thiamine diphosphate binding kinetics Mycobacterium tuberculosis

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.2.1.6 16.3
-
valine pH 7.0, 37°C, holoenzyme Mycobacterium tuberculosis

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
2.2.1.6 0.00087
-
IC50: 870 nM Mycobacterium tuberculosis pyrazosulfuron ethyl