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Literature summary for 1.4.1.9 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

Protein Variants Comment Organism
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
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]

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

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus
-
-
-

Purification (Commentary)

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

Substrates and Products (Substrate)

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

Turnover Number [1/s]

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

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Geobacillus stearothermophilus
NADH
-
Geobacillus stearothermophilus