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Literature summary for 1.4.1.9 extracted from

  • Sekimoto, T.; Matsuyama, T.; Fukui, T.; Tanizawa, K.
    Evidence for lysine 80 as general base catalyst of leucine dehydrogenase (1993), J. Biol. Chem., 268, 27039-27045.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
K80A markedly reduced activity in oxidative deamination, nearly 90% of the wild-type activity in reductive amination. Km-value for 2-oxoisohexanoate is 11fold higher than that of the wild-type enzyme, Km-value for L-Leu is lower than that of the wild-type enzyme Geobacillus stearothermophilus
K80Q markedly reduced activity in oxidative deamination. Km-value for 2-oxoisohexanoate is 28fold higher than that of the wild-type enzyme, Km-value for L-Leu is about 3times larger than that of the wild-type enzyme Geobacillus stearothermophilus
K80R markedly reduced activity in oxidative deamination, 0.6% of the wild-type activity in reductive amination, Km-value for L-Leu is lower than that of the wild-type enzyme Geobacillus stearothermophilus

Inhibitors

Inhibitors Comment Organism Structure
4-methyl-2-pentanone competitive inhibition of wild-type enzyme, noncompetitive inhibition of mutant enzyme K80A Geobacillus stearothermophilus
4-methylpentanoate
-
Geobacillus stearothermophilus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.022
-
NADH mutant enzyme K80A Geobacillus stearothermophilus
0.034
-
NAD+ mutant enzyme K80Q Geobacillus stearothermophilus
0.035
-
NADH wild-type enzyme Geobacillus stearothermophilus
0.037
-
NADH mutant enzyme K80R Geobacillus stearothermophilus
0.045
-
NADH mutant enzyme K80Q Geobacillus stearothermophilus
0.063
-
NAD+ wild-type enzyme Geobacillus stearothermophilus
0.074
-
NAD+ mutant enzyme K80R Geobacillus stearothermophilus
0.14
-
NAD+ mutant enzyme K80A Geobacillus stearothermophilus
0.88
-
2-Oxoisohexanoate wild-type enzyme Geobacillus stearothermophilus
0.99
-
2-Oxoisohexanoate mutant enzyme K80R Geobacillus stearothermophilus
2.8
-
NAD+ mutant enzyme K80R Geobacillus stearothermophilus
3.7
-
L-Leu mutant enzyme K80A Geobacillus stearothermophilus
5.1
-
L-Leu wild-type enzyme Geobacillus stearothermophilus
9.8
-
2-Oxoisohexanoate mutant enzyme K80A Geobacillus stearothermophilus
17
-
NAD+ mutant enzyme K80Q Geobacillus stearothermophilus
25
-
2-Oxoisohexanoate mutant enzyme K80Q Geobacillus stearothermophilus

Organism

Organism UniProt Comment Textmining
Geobacillus stearothermophilus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
75
-
unfolding temperature of mutant enzyme K80A Geobacillus stearothermophilus
79
-
unfolding temperature of mutant enzyme K80R and K80Q Geobacillus stearothermophilus
80
-
unfolding temperature of the wild-type enzyme Geobacillus stearothermophilus

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

pH Stability

pH Stability pH Stability Maximum Comment Organism
7 11.2 25°C, 30 min, wild-type enzyme and mutant enzymes K80A, K80R and K80Q Geobacillus stearothermophilus

Cofactor

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

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
25
-
4-methylpentanoate wild-type enzyme Geobacillus stearothermophilus
33
-
4-methylpentanoate mutant enzyme K80A Geobacillus stearothermophilus
140
-
4-methyl-2-pentanone wild-type enzyme Geobacillus stearothermophilus