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Literature summary for 1.1.1.86 extracted from

  • Reisse, S.; Garbe, D.; Brueck, T.
    Identification and optimization of a novel thermo- and solvent stable ketol-acid reductoisomerase for cell free isobutanol biosynthesis (2015), Biochimie, 108, 76-84.
    View publication on PubMed
Search for more literature for 1.1.1.86

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Rosetta (DE3) cells Meiothermus ruber

Protein Variants

Protein Variants Comment Organism
T84S the mutant shows increased catalytic efficiency compared to the wild type enzyme Meiothermus ruber

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.02
-
 NADPH wild type enzyme, at pH 7.0 and 50°C Meiothermus ruber
0.04
-
 (S)-2-acetolactate mutant enzyme T84S, with NADH as cosubstrate, at pH 7.0 and 50°C Meiothermus ruber
0.08
-
 (S)-2-acetolactate wild type enzyme, with NADPH as cosubstrate, at pH 7.0 and 50°C Meiothermus ruber
0.15
-
 (S)-2-acetolactate mutant enzyme T84S, with NADPH as cosubstrate, at pH 7.0 and 50°C Meiothermus ruber
0.24
-
 (S)-2-acetolactate wild type enzyme, with NADH as cosubstrate, at pH 7.0 and 50°C Meiothermus ruber

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
39000
-
-
 Meiothermus ruber
40000
-
 1 * 40000, SDS-PAGE Meiothermus ruber

Organism

Organism UniProt Comment Textmining
Meiothermus ruber D3PT81
-
-
Meiothermus ruber DSM 1279 D3PT81
-
-

Purification (Commentary)

Purification (Comment) Organism
Ni-NTA column chromatography Meiothermus ruber

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(S)-2-acetolactate + NADH + H+
-
 Meiothermus ruber (R)-2,3-dihydroxyisovalerate + NAD+
-
 r
(S)-2-acetolactate + NADH + H+
-
 Meiothermus ruber DSM 1279 (R)-2,3-dihydroxyisovalerate + NAD+
-
 r
(S)-2-acetolactate + NADPH + H+
-
 Meiothermus ruber (R)-2,3-dihydroxyisovalerate + NADP+
-
 r
(S)-2-acetolactate + NADPH + H+
-
 Meiothermus ruber DSM 1279 (R)-2,3-dihydroxyisovalerate + NADP+
-
 r

Subunits

Subunits Comment Organism
monomer 1 * 40000, SDS-PAGE Meiothermus ruber
monomer 1 * 39000, calculated from amino acid sequence Meiothermus ruber

Synonyms

Synonyms Comment Organism
KARI
-
 Meiothermus ruber

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
65
-
-
 Meiothermus ruber

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
50
-
 at 50°C, the enzyme shows an half-life of 71 h Meiothermus ruber

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
0.77
-
 (S)-2-acetolactate wild type enzyme, with NADPH as cosubstrate, at pH 7.0 and 50°C Meiothermus ruber
0.98
-
 NADPH wild type enzyme, at pH 7.0 and 50°C Meiothermus ruber
1.09
-
 (S)-2-acetolactate wild type enzyme, with NADH as cosubstrate, at pH 7.0 and 50°C Meiothermus ruber
1.3
-
 (S)-2-acetolactate mutant enzyme T84S, with NADH as cosubstrate, at pH 7.0 and 50°C Meiothermus ruber
3.81
-
 (S)-2-acetolactate mutant enzyme T84S, with NADPH as cosubstrate, at pH 7.0 and 50°C Meiothermus ruber

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7
-
-
 Meiothermus ruber

Cofactor

Cofactor Comment Organism Structure
NADH prefers NADPH over NADH Meiothermus ruber
NADPH prefers NADPH over NADH Meiothermus ruber

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.6
-
 (S)-2-acetolactate wild type enzyme, with NADH as cosubstrate, at pH 7.0 and 50°C Meiothermus ruber
10.2
-
 (S)-2-acetolactate wild type enzyme, with NADPH as cosubstrate, at pH 7.0 and 50°C Meiothermus ruber
25.9
-
 (S)-2-acetolactate mutant enzyme T84S, with NADPH as cosubstrate, at pH 7.0 and 50°C Meiothermus ruber
34.1
-
 (S)-2-acetolactate mutant enzyme T84S, with NADH as cosubstrate, at pH 7.0 and 50°C Meiothermus ruber
54.5
-
 NADPH wild type enzyme, at pH 7.0 and 50°C Meiothermus ruber