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Literature summary extracted from

  • Sekimoto, T.; Fukui, T.; Tanizawa, K.
    Involvement of conserved lysine 68 of Bacillus stearothermophilus leucine dehydrogenase in substrate binding (1994), J. Biol. Chem., 269, 7262-7266.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.4.1.9 K68A nearly complete loss of activity in the oxidative deamination, marked increase in Km-values for both amino acid substrates and oxo acid substrates. An ionizable group in the wild-type enzyme with a pKa value of 10.1-10.7, which must be protonated for binding of substrate and competitive inhibitor with an alpha-carboxyl group, is unobservable in mutant enzyme Geobacillus stearothermophilus
1.4.1.9 K68R nearly complete loss of activity in the oxidative deamination. An ionizable group in the wild-type enzyme with a pKa value of 10.1-10.7, which must be protonated for binding of substrate and competitive inhibitor with an alpha-carboxyl group, is unobservable in mutant enzyme Geobacillus stearothermophilus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.1.9 0.021
-
 NADH mutant enzyme K68R Geobacillus stearothermophilus
1.4.1.9 0.035
-
 NADH wild-type enzyme Geobacillus stearothermophilus
1.4.1.9 0.053
-
 NADH mutant enzyme K68A Geobacillus stearothermophilus
1.4.1.9 0.055
-
 NAD+ mutant enzyme K68R Geobacillus stearothermophilus
1.4.1.9 0.063
-
 NAD+ wild-type enzyme Geobacillus stearothermophilus
1.4.1.9 0.11
-
 NAD+ mutant enzyme K68A Geobacillus stearothermophilus
1.4.1.9 0.88
-
 2-Oxoisohexanoate wild-type enzyme Geobacillus stearothermophilus
1.4.1.9 1.2
-
 4-methyl-2-oxopentanoate mutant enzyme K68R Geobacillus stearothermophilus
1.4.1.9 3.2
-
 L-Leu mutant enzyme K68R Geobacillus stearothermophilus
1.4.1.9 5.1
-
 L-Leu wild-type enzyme Geobacillus stearothermophilus
1.4.1.9 130
-
 L-Leu mutant enzyme K68A Geobacillus stearothermophilus
1.4.1.9 140
-
 4-methyl-2-oxopentanoate mutant enzyme K68A Geobacillus stearothermophilus

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.9 Geobacillus stearothermophilus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.1.9 mutant enzymes K68A and K68R Geobacillus stearothermophilus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.1.9 L-Leu + H2O + NAD+
-
 Geobacillus stearothermophilus 4-methyl-2-oxopentanoate + NH3 + NADH
-
 r

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.4.1.9 additional information
-
 additional information turnover numbers of wild-type enzyme and mutant enzymes Geobacillus stearothermophilus

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.1.9 NAD+
-
 Geobacillus stearothermophilus
1.4.1.9 NADH
-
 Geobacillus stearothermophilus