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Literature summary for 2.2.1.6 extracted from

  • Durner, J.; Böger, P.
    Acetolactate synthase from barley (Hordeum vulgare L.): purification and partial characterization (1988), Z. Naturforsch. C, 43, 850-856.
No PubMed abstract available

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
5.5
-
pyruvate
-
Hordeum vulgare

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
58000
-
x * 58000, SDS-PAGE with urea Hordeum vulgare
190000 210000 another enzyme species with MW of 430000-460000 Da is detected, gel filtration Hordeum vulgare
430000 460000 another enzyme species with MW of 190000-210000 Da is detected, gel filtration Hordeum vulgare

Organism

Organism UniProt Comment Textmining
Hordeum vulgare
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Hordeum vulgare

Source Tissue

Source Tissue Comment Organism Textmining
shoot
-
Hordeum vulgare
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.59
-
-
Hordeum vulgare

Substrates and Products (Substrate)

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

Subunits

Subunits Comment Organism
? x * 58000, SDS-PAGE with urea Hordeum vulgare

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6 8.5 enzyme from green barley extract Hordeum vulgare
6.5
-
enzyme from etiolated preparations Hordeum vulgare