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Literature summary for 2.2.1.6 extracted from

  • Singh, B.K.; Stidham, M.A.; Shaner, D.L.
    Assay of acetohydroxyacid synthase (1988), Anal. Biochem., 171, 173-179.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5
-
pyruvate
-
Zea mays

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ saturated at 1 mM MgCl2 Zea mays

Organism

Organism UniProt Comment Textmining
Zea mays
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
cell suspension culture
-
Zea mays
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
spectrophotometric assay involving an indirect detection of the product acetolactate Zea mays

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate
-
Zea mays 2-acetolactate + CO2
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
46 50
-
Zea mays

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6 7
-
Zea mays

pH Range

pH Minimum pH Maximum Comment Organism
5.5 8
-
Zea mays

Cofactor

Cofactor Comment Organism Structure
FAD 0.005 mM, 35-40% enhancement of activity Zea mays
thiamine diphosphate required as cofactor Zea mays
thiamine diphosphate saturated at 0.5 mM thiamine diphosphate Zea mays