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Literature summary for 2.2.1.6 extracted from

  • Carroll, N.M.; Ross, R.P.; Kelly, S.M.; Price, N.C.; Sheehan, D.; Cogan, T.M.
    Characterization of recombinant acetolactate synthase from Leuconostoc lactis NCW1 (1999), Enzyme Microb. Technol., 25, 61-67.
No PubMed abstract available
Search for more literature for 2.2.1.6

Cloned(Commentary)

Cloned (Comment) Organism
overexpression in Escherichia coli Leuconostoc lactis

Inhibitors

Inhibitors Comment Organism Structure
EDTA 20 mM, no residual activity Leuconostoc lactis
additional information no effect: Mn2+, Mg2+, Ca2+ Leuconostoc lactis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
8
-
 pyruvate 30°C, 120 ng protein in assay Leuconostoc lactis
10
-
 pyruvate 30°C, 60 ng protein in assay Leuconostoc lactis

Metals/Ions

Metals/Ions Comment Organism Structure
additional information no effect: Mn2+, Mg2+, Ca2+ Leuconostoc lactis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
50000
-
 PAGE Leuconostoc lactis
120000
-
 PAGE Leuconostoc lactis
182000
-
 PAGE Leuconostoc lactis

Organism

Organism UniProt Comment Textmining
Leuconostoc lactis
-
 overexpression in Escherichia coli
-
Leuconostoc lactis NCW1
-
 overexpression in Escherichia coli
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
 specific activity also depends on protein concentration, with lower concentration giving lower activity, activity may be generally increased by pre-incubation at 30°C prior to assay Leuconostoc lactis
150
-
 30°C, 60 ng protein per assay Leuconostoc lactis
267
-
 30°C, 90 ng protein per assay Leuconostoc lactis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
pyruvate
-
 Leuconostoc lactis 2-acetolactate + CO2
-
 ?
pyruvate
-
 Leuconostoc lactis NCW1 2-acetolactate + CO2
-
 ?

Subunits

Subunits Comment Organism
dimer 2 * 50000, SDS-PAGE, enzyme exists simultaneously as monomer, dimer and trimer Leuconostoc lactis
monomer 1 * 50000, SDS-PAGE, enzyme exists simultaneously as monomer, dimer and trimer Leuconostoc lactis
More N-terminal sequence analysis Leuconostoc lactis
trimer 3 * 50000, SDS-PAGE, enzyme exists simultaneously as monomer, dimer and trimer Leuconostoc lactis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
30
-
 1 hour, no loss of activity Leuconostoc lactis