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Literature summary extracted from

  • Flores, H.; Ellington, A.D.
    A modified consensus approach to mutagenesis inverts the cofactor specificity of Bacillus stearothermophilus lactate dehydrogenase (2005), Protein Eng. Des. Sel., 18, 369-377.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
1.1.1.27 D-fructose 1,6-diphosphate activates wild-type enzyme and mutant enzymes F16Q/I37K/D38SC81S/N85R and F16Q/C81S/N85R Geobacillus stearothermophilus

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.27 F16Q/C81S/N85R catalytic efficiency is higher than that of wild-type enzyme, utilizes NAD+ better than wild-type enzyme, weakly active wth NADP+ Geobacillus stearothermophilus
1.1.1.27 F16Q/I37K/D38S/C81S/N85R utilizes NADP+ better than wild-type enzyme, prefers NADP+ to NAD+ Geobacillus stearothermophilus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.27 0.0081
-
 NAD+ 25°C, pH 8, mutant enzyme F16Q/C81S/N85R, activated by fructose 1,6-diphosphate Geobacillus stearothermophilus
1.1.1.27 0.105
-
 NAD+ 25°C, pH 8, wild-type enzyme, activated by fructose 1,6-diphosphate Geobacillus stearothermophilus
1.1.1.27 4.7
-
 NADP+ 25°C, pH 8, mutant enzyme F16Q/I37K/D38SC81S/N85R, activated by fructose 1,6-diphosphate Geobacillus stearothermophilus

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.27 Geobacillus stearothermophilus P00344
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.27 (S)-lactate + NAD+ wild-type enzyme is specific for NAD+. Mutant enzyme F16Q/I37K/D38SC81S/N85R utilizes NADP+ better than wild-type enzyme, prefers NADP+ to NAD+. Mutant F16Q/C81S/N85R utilizes NAD+ better than wild-type enzyme, weakly active with NADP+ Geobacillus stearothermophilus pyruvate + NADH + H+
-
 ?
1.1.1.27 (S)-lactate + NADP+ wild-type enzyme is specific for NAD+. Mutant enzyme F16Q/I37K/D38SC81S/N85R utilizes NADP+ better than wild-type enzyme, prefers NADP+ to NAD+. Mutant F16Q/C81S/N85R utilizes NAD+ better than wild-type enzyme, weakly active with NADP+ Geobacillus stearothermophilus pyruvate + NADPH + H+
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.27 23
-
 NAD+ 25°C, pH 8, mutant enzyme F16Q/C81S/N85R, activated by fructose 1,6-diphosphate Geobacillus stearothermophilus
1.1.1.27 23
-
 NAD+ 25°C, pH 8, mutant enzyme F16Q/I37K/D38SC81S/N85R, activated by fructose 1,6-diphosphate Geobacillus stearothermophilus
1.1.1.27 32
-
 NAD+ 25°C, pH 8, wild-type enzyme, activated by fructose 1,6-diphosphate Geobacillus stearothermophilus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.27 NAD+ wild-type enzyme is specific for NAD+. Mutant enzyme F16Q/I37K/D38SC81S/N85R utilizes NADP+ better than wild-type enzyme, prefers NADP+ to NAD+. Mutant F16Q/C81S/N85R utilizes NAD+ better than wild-type enzyme, weakly active wth NADP+ Geobacillus stearothermophilus
1.1.1.27 NADP+ wild-type enzyme is specific for NAD+. Mutant enzyme F16Q/I37K/D38SC81S/N85R utilizes NADP+ better than wild-type enzyme, prefers NADP+ to NAD+. Mutant F16Q/C81S/N85R utilizes NAD+ better than wild-type enzyme, weakly active wth NADP+ Geobacillus stearothermophilus