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2-keto-beta-methylvalerate + NH3 + NADH
? + H2O + NAD+
-
as active as 2-ketoisocaproate, wild-type enzyme
-
-
?
2-keto-gamma-methylthiobutanoate + NH3 + NADH
L-Met + H2O + NAD+
-
15% of the activity with 2-ketoisocaproate, wild-type enzyme
-
-
?
2-ketobutyrate + NH3 + NADH
L-2-aminobutyrate + H2O + NAD+
2-ketocaproate + NH3 + NADH
L-2-aminohexanoate + H2O + NAD+
-
69% of the activity with 2-ketoisocaproate
-
-
?
2-ketoisocaproate + NH3 + NADH
L-Ile + H2O + NAD+
2-ketoisovalerate + NH3 + NADH
L-Val + H2O + NAD+
-
150% of the activity with 2-ketoisocaproate
-
-
?
2-ketovalerate + NH3 + NADH
L-norvaline + H2O + NAD+
2-oxo-3,3-dimethylbutanoate + NH3 + NADH
L-2-amino-3,3-dimethylbutanoate + NAD+ + H2O
-
-
-
-
?
2-oxo-3-methylbutanoate + NH3 + NADH + H+
L-2-amino-3-methylbutanoate + H2O + NAD+
2-oxo-4-methylselenobutyrate + NH3 + NADH
L-selenomethionine + H2O + NAD+
-
-
-
?
2-oxobutanoate + NH3 + NADH
L-2-aminobutanoate + H2O + NAD+
-
11% activity 2-oxobutanoate compared to 4-methyl-2-oxopentanoate
-
-
r
2-oxobutanoate + NH3 + NADH + H+
L-2-aminobutanoate + H2O + NAD+
2-oxohexanoate + NH3 + NADH
L-norleucine + H2O + NAD+
-
-
-
-
r
2-oxohexanoate + NH3 + NADH + H+
L-norleucine + H2O + NAD+
2-oxopentanoate + NH3 + NADH
L-norvaline + H2O + NAD+
-
25% activity with 2-oxopentanoate compared to 4-methyl-2-oxopentanoate
-
-
r
2-oxopentanoate + NH3 + NADH + H+
L-2-aminopentanoate + H2O + NAD+
2-oxopentanoate + NH3 + NADH + H+
L-norvaline + H2O + NAD+
-
-
-
-
r
2-oxophenylacetic acid + NH3 + NADH + H+
2-aminophenylacetic acid + H2O + NAD+
-
-
-
-
r
2-oxopropanoate + NH3 + NADH + H+
L-alanine + H2O + NAD+
Roseibium aggregatum
-
-
-
-
?
3,3-dimethyl-2-oxobutanoate + NH3 + NADH
L-tert-Leu + H2O + NAD+
3,3-dimethyl-2-oxobutanoate + NH3 + NADH + H+
L-tert-Leu + H2O + NAD+
-
-
-
-
r
3-methyl-2-oxobutanoate + NH3 + NADH + H+
L-valine + H2O + NAD+
-
-
-
-
r
3-methyl-2-oxopentanoate + NH3 + NADH
L-Ile + H2O + NAD+
-
64% activity with 3-methyl-2-oxopentanoate compared to 4-methyl-2-oxopentanoate
-
-
r
4-(methylsulfanyl)-2-oxobutanoate + NH3 + NADH + H+
L-methionine + H2O + NAD+
4-methyl-2-oxo-5,5,5-trifluoropentanoate + NH3 + NADH
2-amino-4-methyl-5,5,5-trifluoropentanoate + NAD+ + H2O
-
-
-
-
?
4-methyl-2-oxopentanoate + NH3 + NADH
L-Leu + H2O + NAD+
-
100% activity with 4-methyl-2-oxopentanoate
-
-
r
4-methyl-2-oxopentanoate + NH3 + NADH + H+
L-4-methyl-2-aminopentanoate + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH + H+
L-leucine + H2O + NAD+
4-methylthio-2-oxobutyrate + NH3 + NADH
L-Met + H2O + NAD+
-
19% activity with 4-methylthio-2-oxobutyrate compared to 4-methyl-2-oxopentanoate
-
-
r
alpha-keto beta-methylvalerate + NH3 + NADH + H+
L-isoleucine + H2O + NAD+
yield: 95%
-
-
?
alpha-ketocaproate + NH3 + NADH + H+
L-norleucine + H2O + NAD+
yield: 80%
-
-
?
alpha-ketoisocaproate + NH3 + NADH + H+
L-leucine + H2O + NAD+
yield: 92.5%
-
-
?
alpha-ketoisovalerate + NH3 + NADH + H+
L-valine + H2O + NAD+
yield: 90%
-
-
?
alpha-ketovalerate + NH3 + NADH + H+
L-norvaline + H2O + NAD+
yield: 92%
-
-
?
amino(phenyl)acetate + H2O + NAD+
oxo(phenyl)acetate + NH3 + NADH + H+
-
-
-
-
r
DL-methionine + H2O + NAD+
3-methylthio-2-oxobutanoate + NH3 + NADH + H+
-
-
-
?
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
L-2-aminobutyrate + H2O + NAD+
2-oxobutanoate + NH3 + NADH
-
32% of the activity with L-Leu
-
-
?
L-Ala + H2O + NAD+
2-oxopropanoate + NH3 + NADH
L-arginine + H2O + NAD+
5-[(diaminomethyl)amino]-2-oxopentanoic acid + NH3 + NADH + H+
-
-
-
?
L-Ile + H2O + NAD+
3-methyl-2-oxopentanoate + NH3 + NADH
L-isoleucine + H2O + NAD+
3-methyl-2-oxopentanoate + NH3 + NADH + H+
L-isoleucine + NH3 + NADH + H+
3-methyl-2-oxopentanoate + H2O + NAD+
-
-
-
?
L-Leu + H2O + 3-acetylpyridine-deamino-NAD+
4-methyl-2-oxopentanoate + NH3 + 3-acetylpyridine-deamino-NADH
-
as effective as NAD+
-
-
?
L-Leu + H2O + 3-acetylpyridine-NAD+
4-methyl-2-oxopentanoate + NH3 + 3-acetylpyridine-NADH
-
166% of the activity with NAD+
-
-
?
L-Leu + H2O + 3-pyridinealdehyde-NAD+
4-methyl-2-oxopentanoate + NH3 + 3-pyridinealdehyde-NADH
-
19% of the activity with NAD+
-
-
?
L-Leu + H2O + deamino-NAD+
4-methyl-2-oxopentanoate + NH3 + deamino-NADH
-
81% of the activity with NAD+
-
-
?
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
L-Leu + H2O + thionicotinamide-NAD+
4-methyl-2-oxopentanoate + NH3 + thionicotinamide-NADH
-
21% of the activity with NAD+
-
-
?
L-leucine + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH + H+
L-leucine + H2O + NADP+
4-methyl-2-oxopentanoate + NH3 + NADPH + H+
-
-
-
-
r
L-lysine + H2O + NAD+
6-amino-2-oxohexanoate + NH3 + NADH + H+
-
69% of the activity with L-leucine
-
-
?
L-Met + H2O + NAD+
4-methylthio-2-oxobutyrate + NH3 + NADH + H+
L-norleucine + H2O + NAD+
2-oxohexanoate + NH3 + NADH
L-norleucine + H2O + NAD+
? + NH3 + NADH
-
14% the activity with L-Leu, wild-type enzyme
-
-
?
L-norvaline + H2O + NAD+
2-ketovalerate + NH3 + NADH
-
56% the activity with L-Leu, wild-type enzyme
-
-
?
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH + H+
L-Phe + H2O + NAD+
phenylpyruvate + NH3 + NADH
-
no activity of wild-type enzyme activity with mutant enzymes A113G, A113G/V291L
-
-
?
L-proline + H2O + NAD+
? + NH3 + NADH + H+
-
-
-
?
L-S-methylcysteine + H2O + NAD+
3-methylthio-2-oxopropionate + NH3 + NADH
-
19% of the activity with L-Leu
-
-
?
L-tert-Leu + H2O + NAD+
3,3-dimethyl-2-oxobutanoate + NH3 + NADH
L-tert-leucine + H2O + NAD+
trimethylpyruvate + NH3 + NADH + H+
L-tyrosine + H2O + NAD+
? + NH3 + NADH + H+
-
-
-
?
L-Val + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
L-valine + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH + H+
L-valine + NH3 + NADH + H+
2-hydroxy-3-methylbutanoate + H2O + NAD+
-
-
-
?
oxo(phenyl)acetate + NH3 + NADH + H+
amino(phenyl)acetate + H2O + NAD+
phenylglyoxylate + NH3 + NADH + H+
amino(phenyl)acetate + H2O + NAD+
-
-
-
?
phenylpyruvate + NH3 + NADH
L-Phe + H2O + NAD+
-
15% of the activity with 2-ketoisocaproate, wild-type enzyme
-
-
?
pyruvate + NH3 + NADH + H+
L-alanine + H2O + NAD+
S-methyl-L-cysteine + H2O + NAD+
3-methylthio-2-oxopropanoate + NH3 + NADH
-
19% the activity with L-Leu
-
-
?
trimethylpyruvate + NH3 + NADH + H+
L-tert-leucine + H2O + NAD+
trimethylpyruvic acid + NADH + NH3 + H+
L-tert-leucine + NAD+ + H2O
-
-
-
-
?
additional information
?
-
2-ketobutyrate + NH3 + NADH
L-2-aminobutyrate + H2O + NAD+
-
47% of the activity with 2-ketoisocaproate, wild-type enzyme
-
-
?
2-ketobutyrate + NH3 + NADH
L-2-aminobutyrate + H2O + NAD+
-
70% of the activity with 2-ketoisocaproate
-
-
?
2-ketobutyrate + NH3 + NADH
L-2-aminobutyrate + H2O + NAD+
-
70% of the activity with 2-ketoisocaproate
-
-
?
2-ketoisocaproate + NH3 + NADH
L-Ile + H2O + NAD+
-
-
-
-
?
2-ketoisocaproate + NH3 + NADH
L-Ile + H2O + NAD+
-
-
-
-
?
2-ketovalerate + NH3 + NADH
L-norvaline + H2O + NAD+
-
86% of the activity with 2-ketoisocaproate, wild-type enzyme
-
-
?
2-ketovalerate + NH3 + NADH
L-norvaline + H2O + NAD+
-
96% of the activity with 2-ketoisocaproate
-
-
?
2-oxo-3-methylbutanoate + NH3 + NADH + H+
L-2-amino-3-methylbutanoate + H2O + NAD+
-
-
-
?
2-oxo-3-methylbutanoate + NH3 + NADH + H+
L-2-amino-3-methylbutanoate + H2O + NAD+
-
-
-
?
2-oxobutanoate + NH3 + NADH + H+
L-2-aminobutanoate + H2O + NAD+
-
-
-
-
?, r
2-oxobutanoate + NH3 + NADH + H+
L-2-aminobutanoate + H2O + NAD+
-
-
-
?
2-oxobutanoate + NH3 + NADH + H+
L-2-aminobutanoate + H2O + NAD+
-
-
-
?
2-oxobutanoate + NH3 + NADH + H+
L-2-aminobutanoate + H2O + NAD+
-
-
-
-
r
2-oxobutanoate + NH3 + NADH + H+
L-2-aminobutanoate + H2O + NAD+
-
-
-
?
2-oxobutanoate + NH3 + NADH + H+
L-2-aminobutanoate + H2O + NAD+
-
-
-
?
2-oxobutanoate + NH3 + NADH + H+
L-2-aminobutanoate + H2O + NAD+
-
-
-
-
r
2-oxobutanoate + NH3 + NADH + H+
L-2-aminobutanoate + H2O + NAD+
Roseibium aggregatum
-
-
-
-
?
2-oxohexanoate + NH3 + NADH + H+
L-norleucine + H2O + NAD+
-
-
-
-
r
2-oxohexanoate + NH3 + NADH + H+
L-norleucine + H2O + NAD+
-
46% activity compared to 2-oxoisocaproate
-
-
r
2-oxopentanoate + NH3 + NADH + H+
L-2-aminopentanoate + H2O + NAD+
-
-
-
?
2-oxopentanoate + NH3 + NADH + H+
L-2-aminopentanoate + H2O + NAD+
-
-
-
?
2-oxopentanoate + NH3 + NADH + H+
L-2-aminopentanoate + H2O + NAD+
Roseibium aggregatum
-
-
-
-
?
2-oxopentanoate + NH3 + NADH + H+
L-2-aminopentanoate + H2O + NAD+
-
-
-
-
?
2-oxopentanoate + NH3 + NADH + H+
L-2-aminopentanoate + H2O + NAD+
-
-
-
-
?
3,3-dimethyl-2-oxobutanoate + NH3 + NADH
L-tert-Leu + H2O + NAD+
-
-
-
-
?
3,3-dimethyl-2-oxobutanoate + NH3 + NADH
L-tert-Leu + H2O + NAD+
-
-
-
-
?
3,3-dimethyl-2-oxobutanoate + NH3 + NADH
L-tert-Leu + H2O + NAD+
-
-
-
?
3,3-dimethyl-2-oxobutanoate + NH3 + NADH
L-tert-Leu + H2O + NAD+
-
-
-
?
4-(methylsulfanyl)-2-oxobutanoate + NH3 + NADH + H+
L-methionine + H2O + NAD+
-
-
-
-
r
4-(methylsulfanyl)-2-oxobutanoate + NH3 + NADH + H+
L-methionine + H2O + NAD+
-
-
-
-
r
4-methyl-2-oxopentanoate + NH3 + NADH + H+
L-4-methyl-2-aminopentanoate + H2O + NAD+
-
-
-
?
4-methyl-2-oxopentanoate + NH3 + NADH + H+
L-4-methyl-2-aminopentanoate + H2O + NAD+
-
-
-
?
4-methyl-2-oxopentanoate + NH3 + NADH + H+
L-4-methyl-2-aminopentanoate + H2O + NAD+
Roseibium aggregatum
-
-
-
-
?
4-methyl-2-oxopentanoate + NH3 + NADH + H+
L-leucine + H2O + NAD+
-
-
-
-
r
4-methyl-2-oxopentanoate + NH3 + NADH + H+
L-leucine + H2O + NAD+
-
-
-
?
4-methyl-2-oxopentanoate + NH3 + NADH + H+
L-leucine + H2O + NAD+
-
-
-
?
4-methyl-2-oxopentanoate + NH3 + NADH + H+
L-leucine + H2O + NAD+
-
-
-
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
-
-
-
?
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
-
-
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
-
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
-
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
32% of the activity with L-Leu
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
-
-
-
?
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
-
-
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
-
-
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
41% of the activity with L-Leu
-
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
14% of the activity with L-Leu
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
5.7% activity wit L-2-aminobutanoate compared to L-Leu
-
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
5.7% activity wit L-2-aminobutanoate compared to L-Leu
-
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
11% of the activity with L-Leu
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
19% of the activity with L-Leu
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
-
-
-
?
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
-
-
r
L-2-aminobutanoate + H2O + NAD+
2-oxobutanoate + NH3 + NADH + H+
-
-
-
r
L-Ala + H2O + NAD+
2-oxopropanoate + NH3 + NADH
-
10% of the activity with L-Leu
-
-
?
L-Ala + H2O + NAD+
2-oxopropanoate + NH3 + NADH
-
3.4% activity with L-Ala compared to L-Leu
-
-
r
L-Ile + H2O + NAD+
3-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Ile + H2O + NAD+
3-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
-
r
L-Ile + H2O + NAD+
3-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Ile + H2O + NAD+
3-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
-
r
L-Ile + H2O + NAD+
3-methyl-2-oxopentanoate + NH3 + NADH
-
72% of the activity with L-Leu
-
r
L-Ile + H2O + NAD+
3-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
-
r
L-Ile + H2O + NAD+
3-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
-
r
L-Ile + H2O + NAD+
3-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Ile + H2O + NAD+
3-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
-
r
L-Ile + H2O + NAD+
3-methyl-2-oxopentanoate + NH3 + NADH
-
73% of the activity with L-Leu
-
-
r
L-Ile + H2O + NAD+
3-methyl-2-oxopentanoate + NH3 + NADH
-
54% of the activity with L-Leu, wild-type enzyme
-
-
?
L-Ile + H2O + NAD+
3-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
-
r
L-Ile + H2O + NAD+
3-methyl-2-oxopentanoate + NH3 + NADH
-
58% of the activity with L-Leu
-
-
r
L-Ile + H2O + NAD+
3-methyl-2-oxopentanoate + NH3 + NADH
-
72.4% activity with L-Ile compared to L-Leu
-
-
r
L-Ile + H2O + NAD+
3-methyl-2-oxopentanoate + NH3 + NADH
-
72.4% activity with L-Ile compared to L-Leu
-
-
r
L-Ile + H2O + NAD+
3-methyl-2-oxopentanoate + NH3 + NADH
-
88% of the activity with L-Leu
-
r
L-Ile + H2O + NAD+
3-methyl-2-oxopentanoate + NH3 + NADH
-
72% of the activity with L-Leu
-
-
?
L-Ile + H2O + NAD+
3-methyl-2-oxopentanoate + NH3 + NADH
-
72% of the activity with L-Leu
-
-
?
L-Ile + H2O + NAD+
3-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
-
?
L-Ile + H2O + NAD+
3-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Ile + H2O + NAD+
3-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-isoleucine + H2O + NAD+
3-methyl-2-oxopentanoate + NH3 + NADH + H+
-
-
-
-
r
L-isoleucine + H2O + NAD+
3-methyl-2-oxopentanoate + NH3 + NADH + H+
-
69% of the activity with L-leucine
-
-
?
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
the equilibrium favors synthesis of L-Leu
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
Bacillus niger
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
the enzyme may have a function in spore germination
-
?
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
the enzyme may have a function in spore germination
-
?
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
-
?
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
100% activity with L-Leu
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
100% activity with L-Leu
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
-
?
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
-
?
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-Leu + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
r
L-leucine + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH + H+
-
-
-
-
r
L-leucine + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH + H+
-
-
-
-
?
L-leucine + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH + H+
-
-
-
-
?
L-leucine + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH + H+
-
-
-
-
r
L-leucine + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH + H+
-
-
-
?
L-leucine + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH + H+
-
-
-
?
L-leucine + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH + H+
-
-
-
-
?
L-leucine + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH + H+
-
-
-
-
r
L-leucine + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH + H+
-
-
-
?
L-leucine + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH + H+
-
-
-
-
?
L-leucine + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH + H+
-
-
-
-
?
L-leucine + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH + H+
-
-
-
-
?
L-Met + H2O + NAD+
4-methylthio-2-oxobutyrate + NH3 + NADH + H+
-
-
-
r
L-Met + H2O + NAD+
4-methylthio-2-oxobutyrate + NH3 + NADH + H+
-
-
-
r
L-Met + H2O + NAD+
4-methylthio-2-oxobutyrate + NH3 + NADH + H+
-
no activity
-
-
?
L-Met + H2O + NAD+
4-methylthio-2-oxobutyrate + NH3 + NADH + H+
-
0.7% the activity with L-Leu, wild-type enzyme
-
-
?
L-Met + H2O + NAD+
4-methylthio-2-oxobutyrate + NH3 + NADH + H+
-
1.2% activity with L-Met compared to L-Leu
-
-
r
L-Met + H2O + NAD+
4-methylthio-2-oxobutyrate + NH3 + NADH + H+
-
-
-
-
?
L-norleucine + H2O + NAD+
2-oxohexanoate + NH3 + NADH
-
-
-
-
?
L-norleucine + H2O + NAD+
2-oxohexanoate + NH3 + NADH
-
-
-
r
L-norleucine + H2O + NAD+
2-oxohexanoate + NH3 + NADH
-
-
-
r
L-norleucine + H2O + NAD+
2-oxohexanoate + NH3 + NADH
-
7% of the activity with L-Leu
-
r
L-norleucine + H2O + NAD+
2-oxohexanoate + NH3 + NADH
-
-
-
-
?
L-norleucine + H2O + NAD+
2-oxohexanoate + NH3 + NADH
-
-
-
-
?
L-norleucine + H2O + NAD+
2-oxohexanoate + NH3 + NADH
-
-
-
-
r
L-norleucine + H2O + NAD+
2-oxohexanoate + NH3 + NADH
-
74% of the activity with L-Leu
-
r
L-norleucine + H2O + NAD+
2-oxohexanoate + NH3 + NADH
-
15% of the activity with L-Leu
-
r
L-norleucine + H2O + NAD+
2-oxohexanoate + NH3 + NADH
-
-
-
r
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH
-
36.8% activity with L-norvaline compared to L-Leu
-
-
r
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH
-
36.8% activity with L-norvaline compared to L-Leu
-
-
r
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH
-
7% the activity with L-Leu
-
-
?
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH
-
7% the activity with L-Leu
-
-
?
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH + H+
-
-
-
-
r
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH + H+
-
-
-
-
r
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH + H+
-
-
-
-
r
L-tert-Leu + H2O + NAD+
3,3-dimethyl-2-oxobutanoate + NH3 + NADH
-
-
-
-
?
L-tert-Leu + H2O + NAD+
3,3-dimethyl-2-oxobutanoate + NH3 + NADH
-
-
-
-
?
L-tert-leucine + H2O + NAD+
trimethylpyruvate + NH3 + NADH + H+
-
-
-
-
r
L-tert-leucine + H2O + NAD+
trimethylpyruvate + NH3 + NADH + H+
Roseibium aggregatum
-
-
-
-
?
L-Val + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
-
-
-
-
?
L-Val + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
-
-
-
r
L-Val + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
-
-
-
-
r
L-Val + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
-
-
-
r
L-Val + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
-
59% of the activity with L-Leu
-
r
L-Val + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
-
-
-
-
?
L-Val + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
-
-
-
-
?
L-Val + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
-
-
-
-
r
L-Val + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
-
98% of the activity with L-Leu
-
r
L-Val + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
-
39% of the activity with L-Leu, wild-type enzyme
-
-
?
L-Val + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
-
-
-
-
?
L-Val + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
-
-
-
-
r
L-Val + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
-
74% of the activity with L-Leu
-
-
?
L-Val + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
-
93% of the activity with L-Leu
-
r
L-Val + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
-
59% of the activity with L-Leu
-
-
?
L-Val + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
-
59% of the activity with L-Leu
-
-
?
L-Val + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
-
-
-
r
L-Val + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
-
-
-
r
L-valine + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH + H+
-
-
-
-
r
L-valine + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH + H+
-
69% of the activity with L-leucine
-
-
?
L-valine + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH + H+
-
-
-
-
r
oxo(phenyl)acetate + NH3 + NADH + H+
amino(phenyl)acetate + H2O + NAD+
-
-
-
?
oxo(phenyl)acetate + NH3 + NADH + H+
amino(phenyl)acetate + H2O + NAD+
-
-
-
-
r
oxo(phenyl)acetate + NH3 + NADH + H+
amino(phenyl)acetate + H2O + NAD+
Roseibium aggregatum
-
-
-
-
?
pyruvate + NH3 + NADH + H+
L-alanine + H2O + NAD+
-
-
-
?
pyruvate + NH3 + NADH + H+
L-alanine + H2O + NAD+
-
-
-
?
trimethylpyruvate + NH3 + NADH + H+
L-tert-leucine + H2O + NAD+
-
-
-
?
trimethylpyruvate + NH3 + NADH + H+
L-tert-leucine + H2O + NAD+
-
-
-
?
trimethylpyruvate + NH3 + NADH + H+
L-tert-leucine + H2O + NAD+
-
-
-
?
trimethylpyruvate + NH3 + NADH + H+
L-tert-leucine + H2O + NAD+
-
-
-
?
trimethylpyruvate + NH3 + NADH + H+
L-tert-leucine + H2O + NAD+
-
-
-
?
trimethylpyruvate + NH3 + NADH + H+
L-tert-leucine + H2O + NAD+
-
-
-
?
trimethylpyruvate + NH3 + NADH + H+
L-tert-leucine + H2O + NAD+
-
-
-
?
trimethylpyruvate + NH3 + NADH + H+
L-tert-leucine + H2O + NAD+
-
-
-
-
r
trimethylpyruvate + NH3 + NADH + H+
L-tert-leucine + H2O + NAD+
Roseibium aggregatum
-
-
-
-
?
additional information
?
-
-
enzyme liberates ammonium ions from branched chain amino acids when supplied as the sole nitrogen source. It synthesizes from L-Ile, L-Leu, L-Val the branched chain alpha-oxo acids which are precursors of branched chain fatty acid biosynthesis
-
-
?
additional information
?
-
-
no substrates: D-leucine, L-arginine, aspartate, glycine, L-threonine
-
-
?
additional information
?
-
-
no substrates: D-leucine, L-arginine, aspartate, glycine, L-threonine
-
-
?
additional information
?
-
-
substrate specificity of the chimeric enzyme consisting of an amino-terminal domain of phenylalanine dehydrogenase and a carboxy-terminal domain of leucine dehydrogenase
-
-
?
additional information
?
-
-
the enzyme is B-stereospecific
-
-
?
additional information
?
-
-
reductive amination proceeds through a sequential ordered ternary-binary mechanism
-
-
?
additional information
?
-
-
antitumor activity, the enzyme is highly inhibitory to Ehrlich ascites carcinoma cells
-
-
?
additional information
?
-
-
no activity with L-Cys, L-Phe, 2-oxo-3-phenylpropionic acid, 3-(2'-nitrophenyl)-2-oxopropionic acid, and 3-(3'-indolyl)-2-oxopropionic acid
-
-
?
additional information
?
-
-
no activity with L-Cys, L-Phe, 2-oxo-3-phenylpropionic acid, 3-(2'-nitrophenyl)-2-oxopropionic acid, and 3-(3'-indolyl)-2-oxopropionic acid
-
-
?
additional information
?
-
-
the enzyme is B-stereospecific
-
-
?
additional information
?
-
-
synthesis of (S)-1-cyclopropyl-2-methoxyethanamine starting from methylcyclopropyl ketone. Permanganate oxidation of the ketone gives cyclopropylglyoxylic acid, which is converted to (S)-cyclopropylglycine by reductive amination using leucine dehydrogenase from Thermoactinomyces intermedius with NADH cofactor recycling by formate dehydrogenase from Pichia pastoris
-
-
?
additional information
?
-
-
comparing extract activities with 5 mM 2-oxoisovalerate (3282 U/mL) versus 5 mM cyclopropylglyoxylic acid (86 U/mL), leucine dehydrogenase is 38fold more active with the natural substrate
-
-
?
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4
2-ketoisocaproate
-
pH 9.5, 30°C
19
2-oxo-3,3-dimethylbutanoate
-
-
0.73 - 2.54
2-oxo-3-methylbutanoate
0.9 - 2.2
2-oxo-3-methylpentanoate
13
2-oxo-4-methylselenobutanoate
-
-
0.705 - 22.74
2-oxobutanoate
0.88 - 25
2-Oxoisohexanoate
0.4 - 2.4
2-oxopentanoate
2.6 - 217.7
3,3-dimethyl-2-oxobutanoate
2.41
3-acetylpyridine-deamino-NAD+
-
-
0.77
3-acetylpyridine-NAD+
-
-
1.4 - 4.4
3-methyl-2-oxobutanoate
0.38
3-methyl-2-oxopentanoate
-
in 100 mM glycine-KCl-KOH buffer (pH 10), at 25°C
2.1
3-methylthio-2-oxobutanoate
-
-
6.7 - 8.1
4-(methylsulfanyl)-2-oxobutanoate
2.7
4-methyl-2-oxo-5,5,5-trifluoropentanoate
-
-
0.31 - 140
4-methyl-2-oxopentanoate
3.8 - 69
alpha-keto-beta-methylvalerate
0.88 - 30
alpha-keto-isocaproate
0.75
DL-methionine
pH 9, 30°C
1.5 - 22
L-2-aminobutanoate
0.84
L-arginine
pH 9, 30°C
0.64
L-proline
pH 9, 30°C
5.05
L-tert-leucine
Roseibium aggregatum
-
wild-type, pH 8, 30°C
0.48
L-tyrosine
pH 9, 30°C
0.75 - 9.38
oxo(phenyl)acetate
-
0.09 - 60.8
trimethylpyruvate
0.73
2-oxo-3-methylbutanoate
mutant E116V, pH 9.5, 35°C
0.93
2-oxo-3-methylbutanoate
mutant T45M/E116V, pH 9.5, 35°C
2.47
2-oxo-3-methylbutanoate
wild-type, pH 9.5, 35°C
2.54
2-oxo-3-methylbutanoate
mutant T45M, pH 9.5, 35°C
0.9
2-oxo-3-methylpentanoate
-
-
0.9
2-oxo-3-methylpentanoate
-
-
1.9
2-oxo-3-methylpentanoate
-
-
2.2
2-oxo-3-methylpentanoate
-
-
0.705
2-oxobutanoate
mutant E116V, pH 9.5, 35°C
1.7
2-oxobutanoate
mutant T45M, pH 9.5, 35°C
1.89
2-oxobutanoate
wild-type, pH 9.5, 35°C
2.65
2-oxobutanoate
mutant T45M/E116V, pH 9.5, 35°C
13.5
2-oxobutanoate
-
mutant Q358N, pH 7.5, 37°C
13.53
2-oxobutanoate
-
mutant Q358N, pH 7.5, 37°C
16.8
2-oxobutanoate
-
mutant M347G/Q358N, pH 7.5, 37°C
21.3
2-oxobutanoate
-
mutant M374G, pH 7.5, 37°C
21.33
2-oxobutanoate
-
mutant M347G, pH 7.5, 37°C
22.7
2-oxobutanoate
-
wild-type, pH 7.5, 37°C
22.74
2-oxobutanoate
-
wild-type, pH 7.5, 37°C
1.2
2-Oxohexanoate
-
-
2
2-Oxohexanoate
-
mutant enzyme A113A
4.7
2-Oxohexanoate
-
wild-type enzyme
28
2-Oxohexanoate
-
mutant enzyme A113A/V291L
0.88
2-Oxoisohexanoate
-
wild-type enzyme
0.99
2-Oxoisohexanoate
-
mutant enzyme K80R
5.5
2-Oxoisohexanoate
-
mutant enzyme G77A
5.6
2-Oxoisohexanoate
-
mutant enzyme G79A
7.7
2-Oxoisohexanoate
-
mutant enzyme G78A
9.8
2-Oxoisohexanoate
-
mutant enzyme K80A
25
2-Oxoisohexanoate
-
mutant enzyme K80Q
0.4
2-oxopentanoate
-
-
0.41
2-oxopentanoate
mutant T45M/E116V, pH 9.5, 35°C
1.08
2-oxopentanoate
-
in 100 mM glycine-KCl-KOH buffer (pH 10), at 25°C
1.14
2-oxopentanoate
mutant E116V, pH 9.5, 35°C
1.37
2-oxopentanoate
-
pH 8, 50°C
1.43
2-oxopentanoate
wild-type, pH 9.5, 35°C
1.99
2-oxopentanoate
mutant T45M, pH 9.5, 35°C
2.6
3,3-dimethyl-2-oxobutanoate
mutant A43V/D124E , pH 10.0, 30°C
12
3,3-dimethyl-2-oxobutanoate
wild-type, pH 10.0, 30°C
16.8
3,3-dimethyl-2-oxobutanoate
-
pH 9.5, 30°C
100
3,3-dimethyl-2-oxobutanoate
-
pH 7.0, temperature not specified in the publication
153.6
3,3-dimethyl-2-oxobutanoate
-
enzyme coupled to dockerin from Clostridium thermocellum, pH 9.0, 25°C
217.7
3,3-dimethyl-2-oxobutanoate
-
His-tagged enzyme, pH 9.0, 25°C
1.4
3-methyl-2-oxobutanoate
-
-
2.1
3-methyl-2-oxobutanoate
-
-
2.2
3-methyl-2-oxobutanoate
-
-
2.2
3-methyl-2-oxobutanoate
-
-
2.4
3-methyl-2-oxobutanoate
-
-
3.3
3-methyl-2-oxobutanoate
-
-
3.8
3-methyl-2-oxobutanoate
-
-
4
3-methyl-2-oxobutanoate
-
-
4.4
3-methyl-2-oxobutanoate
-
-
6.7
4-(methylsulfanyl)-2-oxobutanoate
-
-
8.1
4-(methylsulfanyl)-2-oxobutanoate
-
-
0.31
4-methyl-2-oxopentanoate
-
-
0.38
4-methyl-2-oxopentanoate
mutant E116V, pH 9.5, 35°C
0.45
4-methyl-2-oxopentanoate
-
-
0.6
4-methyl-2-oxopentanoate
-
-
0.63
4-methyl-2-oxopentanoate
-
-
0.7
4-methyl-2-oxopentanoate
-
-
0.8
4-methyl-2-oxopentanoate
-
-
0.89
4-methyl-2-oxopentanoate
mutant T45M/E116V, pH 9.5, 35°C
1
4-methyl-2-oxopentanoate
-
-
1.2
4-methyl-2-oxopentanoate
-
mutant enzyme K68R
1.41
4-methyl-2-oxopentanoate
wild-type, pH 9.5, 35°C
1.55
4-methyl-2-oxopentanoate
-
in 100 mM glycine-KCl-KOH buffer (pH 10), at 25°C
1.72
4-methyl-2-oxopentanoate
mutant T45M, pH 9.5, 35°C
140
4-methyl-2-oxopentanoate
-
mutant enzyme K68A
3.8
alpha-keto-beta-methylvalerate
-
wild-type enzyme
9.4
alpha-keto-beta-methylvalerate
-
mutant enzyme A113A
69
alpha-keto-beta-methylvalerate
-
mutant enzyme A113A/V291L
0.88
alpha-keto-isocaproate
-
wild-type enzyme
1.7
alpha-keto-isocaproate
-
mutant enzyme A113A
30
alpha-keto-isocaproate
-
mutant enzyme A113A/V291L
1.5
L-2-aminobutanoate
-
-
8.9
L-2-aminobutanoate
-
-
10
L-2-aminobutanoate
-
-
22
L-2-aminobutanoate
-
-
0.4
L-Ile
-
-
0.66
L-Ile
-
pH 9.5, 30°C, in presence of 4 M NaCL
0.78
L-Ile
-
in 100 mM glycine-KCl-KOH buffer (pH 10), at 25°C
2.4
L-Ile
-
wild-type enzyme
7.8
L-Ile
-
mutant enzyme A113A
33
L-Ile
-
mutant enzyme A113A/V291L
0.69
L-Leu
-
pH 9.5, 30°C
1.12
L-Leu
-
in 100 mM glycine-KCl-KOH buffer (pH 10), at 25°C
1.4
L-Leu
-
mutant enzyme A113A
3.2
L-Leu
-
mutant enzyme K68R
3.3
L-Leu
-
native enzyme
3.5
L-Leu
-
mutant enzyme G77A
3.6
L-Leu
-
mutant enzyme G79A
3.7
L-Leu
-
mutant enzyme K80A
4.3
L-Leu
-
mutant enzyme G78A
5.1
L-Leu
-
wild-type enzyme
11
L-Leu
-
mutant enzyme LeuDEL4
35
L-Leu
-
mutant enzyme A113A/V291L
130
L-Leu
-
mutant enzyme K68A
0.1
L-leucine
-
pH 9.5, 30°C
0.33
L-leucine
pH 9, 30°C
0.65
L-leucine
-
pH 10.5, 20°C
0.8
L-leucine
-
pH 9.5, 30°C
0.88
L-leucine
pH 8.5, 30°C
1.2
L-leucine
-
pH not specified in the publication, temperature not specified in the publication
1.4
L-leucine
-
pH 10.5, 25°C
23
L-Met
-
-
1.27
L-norleucine
-
in 100 mM glycine-KCl-KOH buffer (pH 10), at 25°C
4.1
L-norleucine
-
mutant enzyme A113A
4.4
L-norleucine
-
wild-type enzyme
24
L-norleucine
-
mutant enzyme A113A/V291L
0.98
L-norvaline
-
in 100 mM glycine-KCl-KOH buffer (pH 10), at 25°C
7.8
L-norvaline
-
wild-type enzyme
27
L-norvaline
-
mutant enzyme A113A
70
L-norvaline
-
mutant enzyme A113A/V291L
31
L-Phe
-
mutant enzyme A113A
66
L-Phe
-
mutant enzyme A113A/V291L
0.71
L-Val
-
pH 9.5, 30°C, in presence of 4 M NaCL
3.8
L-Val
-
native enzyme
25
L-Val
-
mutant enzyme LeuDEL4
0.015
NAD+
-
pH 10.5, 20°C
0.034
NAD+
-
mutant enzyme K80Q
0.039
NAD+
-
mutant enzyme G77A
0.055
NAD+
-
mutant enzyme K68R
0.059
NAD+
-
mutant enzyme G78A
0.063
NAD+
-
wild-type enzyme
0.071
NAD+
-
mutant enzyme G79A
0.074
NAD+
-
mutant enzyme K80R
0.076
NAD+
-
mutant enzyme A113A
0.078
NAD+
Roseibium aggregatum
-
wild-type, pH 8, 30°C
0.094
NAD+
-
pH 10.5, 25°C
0.11
NAD+
-
mutant enzyme K68A
0.14
NAD+
-
mutant enzyme K80A
0.28
NAD+
-
mutant enzyme A113A/V291L
0.48
NAD+
-
native enzyme
1.25
NAD+
-
mutant enzyme LeuDEL4
2.8
NAD+
-
mutant enzyme K80R
17
NAD+
-
mutant enzyme K80Q
0.017
NADH
-
mutant enzyme A113A/V291L
0.02
NADH
Roseibium aggregatum
-
mutant D153N/H191N, pH 8, 30°C
0.021
NADH
-
mutant enzyme K68R
0.022
NADH
-
mutant enzyme K80A
0.0223
NADH
pH 10.0, 30°C, fusion enzyme F-S1_L
0.0279
NADH
pH 10.0, 30°C, fusion enzyme F-R3-L
0.0349
NADH
pH 10.0, 30°C, fusion enzyme F-S3-L
0.035
NADH
-
wild-type enzyme
0.037
NADH
-
mutant enzyme K80R
0.038
NADH
-
mutant enzyme G77A
0.04
NADH
mutant A43V/D124E , pH 10.0, 30°C
0.04
NADH
Roseibium aggregatum
-
mutant D153N, pH 8, 30°C
0.0415
NADH
pH 10.0, 30°C, fusion enzyme F-DL-L
0.042
NADH
-
mutant enzyme A113A
0.0436
NADH
pH 10.0, 30°C, fusion enzyme F-R2-L
0.045
NADH
-
mutant enzyme K80Q
0.05
NADH
Roseibium aggregatum
-
mutant P130V, pH 8, 30°C
0.051
NADH
pH 10.0, 30°C, fusion enzyme F-R1-L
0.053
NADH
-
mutant enzyme K68A
0.054
NADH
-
mutant enzyme G78A
0.055
NADH
-
mutant enzyme G79A
0.0605
NADH
pH 10.0, 30°C, wild-type enzyme
0.061
NADH
-
enzyme coupled to dockerin from Clostridium thermocellum, pH 9.0, 25°C
0.07
NADH
mutant E116V, pH 9.5, 35°C
0.07
NADH
Roseibium aggregatum
-
mutant H191N, pH 8, 30°C
0.077
NADH
-
pH 9.5, 30°C
0.09
NADH
mutant T45M/E116V, pH 9.5, 35°C
0.1
NADH
-
pH 7.0, temperature not specified in the publication
0.1
NADH
mutant E24V/E116V, pH 8.5, 30°C
0.151
NADH
pH 10.0, 30°C, fusion enzyme F-S2_L
0.154
NADH
mutant E24A/D126E, pH 8.5, 30°C
0.17
NADH
wild-type, pH 9.5, 35°C
0.2
NADH
wild-type, pH 10.0, 30°C
0.22
NADH
mutant T45M, pH 9.5, 35°C
0.248
NADH
-
His-tagged enzyme, pH 9.0, 25°C
0.25
NADH
mutant E116V, pH 8.5, 30°C
0.27
NADH
mutant D126E, pH 8.5, 30°C
0.28
NADH
wild-type, pH 8.5, 30°C
0.43
NADH
Roseibium aggregatum
-
wild-type, pH 8, 30°C
2.5
NADP+
-
mutant D203A/I204R/D210R
2.8
NADP+
-
mutant enzyme D203A/I204R
220
NH3
-
pH 9.5, 30°C
13
NH4+
-
-
75
NH4+
-
wild-type enzyme
210
NH4+
-
mutant enzyme G77A
290
NH4+
-
mutant enzyme G79A
750
NH4+
-
mutant enzyme G78A
0.75
oxo(phenyl)acetate
mutant E116V, pH 9.5, 35°C
-
1.12
oxo(phenyl)acetate
mutant T45M/E116V, pH 9.5, 35°C
-
1.99
oxo(phenyl)acetate
mutant T45M, pH 9.5, 35°C
-
9.38
oxo(phenyl)acetate
wild-type, pH 9.5, 35°C
-
7.1
phenylpyruvate
-
mutant enzyme A113A
9.9
phenylpyruvate
-
mutant enzyme A113A/V291L
0.09
trimethylpyruvate
Roseibium aggregatum
-
mutant H191N, pH 8, 30°C
0.096
trimethylpyruvate
Roseibium aggregatum
-
wild-type, pH 8, 30°C
0.1
trimethylpyruvate
Roseibium aggregatum
-
mutant D153N/H191N, pH 8, 30°C
0.12
trimethylpyruvate
Roseibium aggregatum
-
mutant D153N, pH 8, 30°C
0.3
trimethylpyruvate
Roseibium aggregatum
-
mutant P130V, pH 8, 30°C
1.15
trimethylpyruvate
mutant T45M, pH 9.5, 35°C
1.71
trimethylpyruvate
mutant E116V, pH 9.5, 35°C
2.65
trimethylpyruvate
mutant T45M/E116V, pH 9.5, 35°C
3.08
trimethylpyruvate
-
pH 9.5, 30°C
3.7 - 5
trimethylpyruvate
wild-type, pH 9.5, 35°C
5.96
trimethylpyruvate
pH 8.5, 30°C
7.9
trimethylpyruvate
mutant E24V/E116V, pH 8.5, 30°C
10.7
trimethylpyruvate
mutant E116V, pH 8.5, 30°C
17.6
trimethylpyruvate
mutant E24A/D126E, pH 8.5, 30°C
23.2
trimethylpyruvate
mutant D126E, pH 8.5, 30°C
60.8
trimethylpyruvate
wild-type, pH 8.5, 30°C
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Ohshima, T.; Wandrey, C.; Sugiura, M.; Soda, K.
Screening of thermostable leucine and alanine dehydrogenases in thermophilic Bacillus strains
Biotechnol. Lett.
7
871-876
1985
Bacillus sp. (in: Bacteria), Lysinibacillus sphaericus
-
brenda
Kataoka, K.; Takada, H.; Tanizawa, K.; Yoshimura, T.; Esaki, N.; Ohshima, T.; Soda, K.
Construction and characterization of chimeric enzyme consisting of an amino-terminal domain of phenylalanine dehydrogenase and a carboxy-terminal domain of leucine dehydrogenase
J. Biochem.
116
931-936
1994
Geobacillus stearothermophilus
brenda
Zink, M.W.; Sanwal, B.D.
L-Leucine dehydrogenase (Bacillus cereus)
Methods Enzymol.
17A
799-802
1970
Bacillus cereus
-
brenda
Sanwal, B.D.; Zink, M.W.
L-Leucine dehydrogenase of Bacillus cereus
Arch. Biochem. Biophys.
94
430-435
1961
Bacillus cereus
brenda
Zink, M.W.; Sanwal, B.D.
The distribution and substrate specificity of L-Leucine dehydrogenase
Arch. Biochem. Biophys.
99
72-77
1962
Bacillus cereus, Priestia megaterium, Bacillus subtilis, Bacillus pumilus, Bacillus mycoides, Bacillus niger, Lysinibacillus sphaericus
-
brenda
Schuette, H.; Hummel, W.; Tsai, H.; Kula, M.R.
L-Leucine dehydrogenase from Bacillus cereus
Appl. Microbiol. Biotechnol.
22
306-317
1985
Bacillus cereus
-
brenda
Ohshima, T.; Nagata, S.; Soda, K.
Purification and characterization of thermostable leucine dehydrogenase from Bacillus stearothermophilus
Arch. Microbiol.
141
407-411
1985
Geobacillus stearothermophilus
-
brenda
Livesey, G.; Lund, P.
Isolation and characterization of leucine dehydrogenase from Bacillus subtilis
Methods Enzymol.
166
282-288
1988
Bacillus subtilis
brenda
Kaerst, U.; Schuette, H.; Baydoun, H.; Tsai, H.
Purification and characterization of leucine dehydrogenase from the thermophile Bacillus caldolyticus
J. Gen. Microbiol.
135
1305-1313
1989
[Bacillus] caldolyticus
-
brenda
Ohshima, T.; Misono, H.; Soda, K.
Properties of crystalline leucine dehydrogenase from Bacillus sphaericus
J. Biol. Chem.
253
5719-5725
1978
Brevibacillus brevis, Bacillus cereus, Priestia megaterium, Bacillus subtilis, Bacillus pumilus, Lysinibacillus sphaericus
brenda
Obermeier, N.; Poralla, K.
Some physiological functions of the L-leucine dehydrogenase in Bacillus subtilis
Arch. Microbiol.
109
59-63
1976
Bacillus subtilis
brenda
Ohshima, T.; Yamamoto, T.; Misono, H.; Soda, K.
Leucine dehydrogenase of bacillus sphaericus: sulfhydryl groups and catalytic sites
Agric. Biol. Chem.
42
1739-1743
1978
Lysinibacillus sphaericus
-
brenda
Hummel, W.; Schuette, H.; Kula, M.R.
Leucine dehydrogenase from Bacillus sphaericus. Optimized production conditions and efficient method for its large-scale purification
Eur. J. Appl. Microbiol. Biotechnol.
12
22-27
1981
Lysinibacillus sphaericus
-
brenda
Nagata, S.; Tanizawa, K.; Esaki, N.; Sakamoto, Y.; Ohshima, T.; Tanaka, H.; Soda, K.
Gene cloning and sequence determination of leucine dehydrogenase from Bacillus stearothermophilus and structural comparison with other NAD(P)+-dependent dehydrogenases
Biochemistry
27
9056-9062
1988
Geobacillus stearothermophilus
brenda
Schustolla, D.; Hustedt, H.
Gene cloning and sequence determination of leucine dehydrogenase from Bacillus stearothermophilus and structural comparison with other NAD(P)+-dependent dehydrogenases
DECHEMA Biotechnol. Conf.
3
1097-1101
1989
Bacillus cereus
-
brenda
Obermeier, N.; Poralla, K.
Experiments on the role of leucine dehydrogenase in initiation of Bacillus subtilis spore germination
FEMS Microbiol. Lett.
5
81-83
1979
Bacillus subtilis, Bacillus subtilis 168M
-
brenda
Oki, T.; Shirai, M.
Antitumor activities of bacterial leucine dehydrogenase and glutaminase A
FEBS Lett.
33
286-288
1973
Lysinibacillus sphaericus
brenda
Ohshima, T.; Soda, K.
Modification of leucine dehydrogenase by pyridoxal 5'-phosphate
Agric. Biol. Chem.
48
349-354
1984
Lysinibacillus sphaericus
-
brenda
Oka, M.; Yang, Y.S.; Nagata, S.; Esaki, N.; Tanaka, H.; Soda, K.
Overproduction of thermostable leucine dehydrogenase of Bacillus stearothermophilus and its one-step purification from recombinant cells of Escherichia coli
Biotechnol. Appl. Biochem.
11
307-311
1989
Geobacillus stearothermophilus
brenda
Soda, K.; Misono, H.; Mori, K.; Sakato, H.
Crystalline L-leucine dehydrogenase
Biochem. Biophys. Res. Commun.
44
931-935
1971
Lysinibacillus sphaericus
brenda
Esaki, N.; Shimoi, H.; Yang, Y.S.; Tanaka, H.; Soda, K.
Enantioselective synthesis of L-selenomethionine with leucine dehydrogenase
Biotechnol. Appl. Biochem.
11
312-317
1989
Geobacillus stearothermophilus
-
brenda
Kiba, N.; Hori, S.; Furusawa, M.
Flow-injection determination of branched-chain L-amino acids with immobilized leucine dehydrogenase
Anal. Chim. Acta
218
161-166
1989
Bacillus cereus, Bacillus sp. (in: Bacteria)
-
brenda
Warth, A.D.
Heat stability of Bacillus cereus enzymes within spores and in extracts
J. Bacteriol.
143
27-34
1980
Bacillus cereus
brenda
Shimoi, H.; Nagata, S.; Esaki, N.; Tanaka, H.; Soda, K.
Leucine dehydrogenase of a thermophilic anaerobe, Clostridium thermoaceticum: gene cloning, purification and characterization
Agric. Biol. Chem.
51
3375-3381
1987
Moorella thermoacetica
-
brenda
Nagata, S.; Misono, H.; Nagasaki, S.; Esaki, N.; Tanaka, H.; Soda, K.
Gene cloning, purification, and characterization of the highly thermostable leucine dehydrogenase of bacillus sp.
J. Ferment. Bioeng.
69
199-203
1990
Bacillus sp. (in: Bacteria)
-
brenda
Nagata, S.; Bakthavatsalam, S.; Galkin, A.G.; Asada, H.; Sakai, S.; Esaki, N.; Soda, K.; Ohshima, T.; Nagasaki, S.; Misono, H.
Gene cloning, purification, and characterization of thermostable and halophilic leucine dehydrogenase from a halophilic thermophile, Bacillus licheniformis TSN9
Appl. Microbiol. Biotechnol.
44
432-438
1995
Bacillus licheniformis
brenda
Ansorge, M.B.; Kula, M.R.
Production of recombinant L-leucine dehydrogenase from Bacillus cereus in pilot scale using the runaway replication system E. coli[pIET98]
Biotechnol. Bioeng.
68
557-562
2000
Bacillus cereus
brenda
Ohshima, T.; Nishida, N.; Bakthavatsalam, S.; Kataoka, K.; Takada, H.; Yoshimura, T.; Esaki, N.; Soda, K.
The purification, characterization, cloning and sequencing of the gene for a halostable and thermostable leucine dehydrogenase from Thermoactinomyces intermedius
Eur. J. Biochem.
222
305-312
1994
Thermoactinomyces intermedius
brenda
Galkin, A.; Kulakova, L.; Ohshima, T.; Esaki, N.; Soda, K.
Construction of a new leucine dehydrogenase with preferred specificity for NADP+ by site-directed mutagenesis of the strictly NAD+-specific enzyme
Protein Eng.
10
687-690
1997
Thermoactinomyces intermedius
brenda
Sekimoto, T.; Fukui, T.; Tanizawa, K.
Role of the conserved glycyl residues located at the active site of leucine dehydrogenase from Bacillus stearothermophilus
J. Biochem.
116
176-182
1994
Geobacillus stearothermophilus
brenda
Baker, P.J.; Turnbull, A.P.; Sedelnikova, S.E.; Stillman, T.J.; Rice, D.W.
A role for quaternary structure in the substrate specificity of leucine dehydrogenase
Structure
3
693-705
1995
Lysinibacillus sphaericus
brenda
Kiba, N.; Oyama, Y.; Kato, A.; Furusawa, M.
Postcolumn co-immobilized leucine dehydrogenase-NADH oxidase reactor for the determination of branched-chain amino acids by high-performance liquid chromatography with chemiluminescence detection
J. Chromatogr. A
724
354-357
1996
Geobacillus stearothermophilus
-
brenda
Sekimoto, T.; Fukui, T.; Tanizawa, K.
Involvement of conserved lysine 68 of Bacillus stearothermophilus leucine dehydrogenase in substrate binding
J. Biol. Chem.
269
7262-7266
1994
Geobacillus stearothermophilus
brenda
Sekimoto, T.; Matsuyama, T.; Fukui, T.; Tanizawa, K.
Evidence for lysine 80 as general base catalyst of leucine dehydrogenase
J. Biol. Chem.
268
27039-27045
1993
Geobacillus stearothermophilus
brenda
Muranova, T.A.; Ruzheinikov, S.N.; Sedelnikova, S.E.; Baker, P.J.; Pasquo, A.; Galkin, A.; Esaki, N.; Ohshima, T.; Soda, K.; Rice, D.W.
Crystallization and preliminary X-ray analysis of substrate complexes of leucine dehydrogenase from Thermoactinomyces intermedius
Acta Crystallogr. Sect. D
58
1059-1062
2002
Lysinibacillus sphaericus, Thermoactinomyces intermedius
brenda
Turnbull, A.P.; Ashford, S.R.; Baker, P.J.; Rice, D.W.; Rodgers, F.H.; Stillman, T.J.; Hanson, R.L.
Crystallization and quaternary structure analysis of the NAD+-dependent leucine dehydrogenase from Bacillus sphaericus
J. Mol. Biol.
236
663-665
1994
Lysinibacillus sphaericus
brenda
Oikawa, T.; Kataoka, K.; Jin, Y.; Suzuki, S.; Soda, K.
Fragmentary form of thermostable leucine dehydrogenase of Bacillus stearothermophilus: its construction and reconstitution of active fragmentary enzyme
Biochem. Biophys. Res. Commun.
280
1177-1182
2001
Geobacillus stearothermophilus
brenda
Gu, K.F.; Chang, M.S.
Production of essential L-branched-chain amino acids in bioreactors containing artificial cells immobilized multienzyme system and dextran-NAD+
Biotechnol. Bioeng.
36
263-269
1990
Bacillus sp. (in: Bacteria)
brenda
Gu, K.F.; Chang, M.S.
Conversion of ammonia or urea into essential amino acids, L-leucine, L-valine, and L-isoleucine, using artificial cells containing as immobilized multienzyme system and dextran-NAD+
Biotechnol. Appl. Biochem.
12
227-236
1990
Bacillus sp. (in: Bacteria)
brenda
Livesey, G.; Lund, P.
Determination of branched-chain amino and keto acids with leucine dehydrogenase
Methods Enzymol.
166
3-10
1988
Bacillus subtilis, Lysinibacillus sphaericus
brenda
Morishita, Y.; Nakane, K.; Fukatsu, T.; Nakashima, N.; Tsuji, K.; Soya, Y.; Yoneda, K.; Asano, S.; Kawamura, Y.
Kinetic assay of serum and urine for urea with use of urease and leucine dehydrogenase
Clin. Chem.
43
1932-11936
1997
Bacillus subtilis
brenda
Kiba, N.; Muto, M.; Furusawa, M.
High-performance liquid chromatographic determination of branched-chain alpha-keto acids in serum using immobilized leucine dehydrogenase as post-column reactor
J. Chromatogr.
497
236-242
1989
Bacillus subtilis
brenda
Katoh, R.; Ngata, S.; Ozawa, A.; Ohshima, T.; Kamekura, M.; Misono, H.
Purification and characterization of leucine dehydrogenase from an alkalophilic halophile, Natronobacterium magadii MS-3
J. Mol. Catal. B
23
231-238
2003
Natrialba magadii, Natrialba magadii MS-3
-
brenda
Katoh, R.; Nagata, S.; Misono, H.
Cloning and sequencing of the leucine dehydrogenase gene from Bacillus sphaericus IFO 3525 and importance of the C-terminal region for the enzyme activity
J. Mol. Catal. B
23
239-247
2003
Lysinibacillus sphaericus
-
brenda
Kataoka, K.; Tanizawa, K.
Alteration of substrate specificity of leucine dehydrogenase by site-directed mutagenesis
J. Mol. Catal. B
23
299-309
2003
Geobacillus stearothermophilus
-
brenda
Bradshaw, C.W.; Wong, C.H.; Hummel, W.; Kula, M.R.
Enzyme-catalyzed asymetric synthesis of (S)-2-amino-4-phenylbutanoic acid and (R)-2-hydroxy-4-phenylbutanoic acid
Bioorg. Chem.
19
29-39
1991
Lysinibacillus sphaericus
-
brenda
Chiriac, M.; Lupan, I.; Bucurenci, N.; Popescu, O.; Palibroda, N.
Stereoselective synthesis of L-[15N] amino acids with glucose dehydrogenase and galactose mutarotase as NADH regenerating system
J. Labelled Compd. Radiopharm.
51
171-174
2008
Geobacillus stearothermophilus (P13154)
-
brenda
Li, H.; Zhu, D.; Hyatt, B.A.; Malik, F.M.; Biehl, E.R.; Hua, L.
Cloning, protein sequence clarification, and substrate specificity of a leucine dehydrogenase from Bacillus sphaericus ATCC4525
Appl. Biochem. Biotechnol.
158
343-351
2008
Lysinibacillus sphaericus, Lysinibacillus sphaericus ATCC 4525
brenda
Zhao, Y.; Wakamatsu, T.; Doi, K.; Sakuraba, H.; Ohshima, T.
A psychrophilic leucine dehydrogenase from Sporosarcina psychrophila: purification, characterization, gene sequencing and crystal structure analysis
J. Mol. Catal. B
83
65-72
2012
Sporosarcina psychrophila, Sporosarcina psychrophila DSM 3
-
brenda
Parker, W.; Hanson, R.; Goldberg, S.; Tully, T.; Goswami, A.
Preparation of (S)-1-cyclopropyl-2-methoxyethanamine by a chemoenzymatic route using leucine dehydrogenase
Org. Process Res. Dev.
16
464-469
2012
Thermoactinomyces intermedius
-
brenda
Lu, J.; Zhang, Y.; Sun, D.; Jiang, W.; Wang, S.; Fang, B.
The development of leucine dehydrogenase and formate dehydrogenase bifunctional enzyme cascade improves the biosynthsis of L-tert-teucine
Appl. Biochem. Biotechnol.
180
1180-1195
2016
Bacillus cereus
brenda
Xu, J.M.; Cheng, F.; Fu, F.T.; Hu, H.F.; Zheng, Y.G.
Semi-rational engineering of leucine dehydrogenase for L-2-aminobutyric acid production
Appl. Biochem. Biotechnol.
182
898-909
2016
Bacillus cereus
brenda
Zhu, L.; Wu, Z.; Jin, J.M.; Tang, S.Y.
Directed evolution of leucine dehydrogenase for improved efficiency of L-tert-leucine synthesis
Appl. Microbiol. Biotechnol.
100
5805-5813
2016
Lysinibacillus sphaericus (Q76GS2), Lysinibacillus sphaericus
brenda
Liu, W.; Ma, H.; Luo, J.; Shen, W.; Xu, X.; Li, S.; Hu, Y.; Huang, H.
Efficient synthesis of L-tert-leucine through reductive amination using leucine dehydrogenase and formate dehydrogenase coexpressed in recombinant E. coli
Biochem. Eng. J.
91
204-209
2014
Lysinibacillus sphaericus (Q76GS2), Lysinibacillus sphaericus CGMCC 1.1677 (Q76GS2)
-
brenda
Tao, R.; Jiang, Y.; Zhu, F.; Yang, S.
A one-pot system for production of L-2-aminobutyric acid from L-threonine by L-threonine deaminase and a NADH-regeneration system based on L-leucine dehydrogenase and formate dehydrogenase
Biotechnol. Lett.
36
835-841
2014
Bacillus cereus (P0A392), Bacillus cereus, Bacillus cereus DSM 31 (P0A392)
brenda
Zhu, W.; Li, Y.; Jia, H.; Wei, P.; Zhou, H.; Jiang, M.
Expression, purification and characterization of a thermostable leucine dehydrogenase from the halophilic thermophile Laceyella sacchari
Biotechnol. Lett.
38
855-861
2016
Laceyella sacchari
brenda
Jiang, W.; Sun, D.; Lu, J.; Wang, Y.; Wang, S.; Zhang, Y.; Fang, B.
A cold-adapted leucine dehydrogenase from marine bacterium Alcanivorax dieselolei Characterization and l-tert-leucine production
Eng. Life Sci.
16
283-289
2016
Alcanivorax dieselolei
-
brenda
Zhang, Y.; Wang, Y.; Wang, S.; Fang, B.
Engineering bi-functional enzyme complex of formate dehydrogenase and leucine dehydrogenase by peptide linker mediated fusion for accelerating cofactor regeneration
Eng. Life Sci.
17
989-996
2017
Bacillus cereus (Q731C9), Bacillus cereus ATCC 10987 (Q731C9)
-
brenda
Mahdizadehdehosta, R.; Kianmehr, A.; Khalili, A.
Isolation and characterization of leucine dehydrogenase from a thermophilic Citrobacter freundii JK-91 strain isolated from Jask Port
Iran. J. Microbiol.
5
278-284
2013
Citrobacter freundii, Citrobacter freundii JK-91
brenda
Li, J.; Pan, J.; Zhang, J.; Xu, J.
Stereoselective synthesis of L-tert-leucine by a newly cloned leucine dehydrogenase from Exiguobacterium sibiricum
J. Mol. Catal. B
105
11-17
2014
Exiguobacterium sibiricum
-
brenda
Zhou, F.; Mu, X.; Nie, Y.; Xu, Y.
Enhanced catalytic efficiency and coenzyme affinity of leucine dehydrogenase by comprehensive screening strategy for L-tert-leucine synthesis
Appl. Microbiol. Biotechnol.
105
3625-3634
2021
Bacillus cereus (A0A068FCF1), Bacillus cereus
brenda
Chen, J.; Zhu, R.; Zhou, J.; Yang, T.; Zhang, X.; Xu, M.; Rao, Z.
Efficient single whole-cell biotransformation for L-2-aminobutyric acid production through engineering of leucine dehydrogenase combined with expression regulation
Biores. Technol.
326
124665
2021
Exiguobacterium sibiricum (B1YLR3), Exiguobacterium sibiricum DSM 17290 (B1YLR3)
brenda
Zhou, J.; Wang, Y.; Chen, J.; Xu, M.; Yang, T.; Zheng, J.; Zhang, X.; Rao, Z.
Rational engineering of Bacillus cereus leucine dehydrogenase towards alpha-keto acid reduction for improving unnatural amino acid production
Biotechnol. J.
14
e1800253
2019
Bacillus cereus (P0A392), Bacillus cereus, Bacillus cereus DSM 31 (P0A392)
brenda
Meng, X.; Yang, L.; Liu, Y.; Wang, H.; Shen, Y.; Wei, D.
Identification and rational engineering of a high substrate-tolerant leucine dehydrogenase effective for the synthesis of L-tert-leucine
ChemCatChem
13
3340-3349
2021
Roseibium aggregatum
-
brenda
Wang, L.; Zhu, W.; Gao, Z.; Zhou, H.; Cao, F.; Jiang, M.; Li, Y.; Jia, H.; Wei, P.
Biosynthetic L-tert-leucine using Escherichia coli co-expressing a novel NADH-dependent leucine dehydrogenase and a formate dehydrogenase
Electron. J. Biotechnol.
47
83-88
2020
Laceyella sacchari
-
brenda
Luo, W.; Zhu, J.; Zhao, Y.; Zhang, H.; Yang, X.; Liu, Y.; Rao, Z.; Yu, X.
Cloning and expression of a novel leucine dehydrogenase characterization and L-tert-leucine production
Front. Bioeng. Biotechnol.
8
186
2020
Exiguobacterium sibiricum (B1YLR3), Exiguobacterium sibiricum, Exiguobacterium sibiricum DSM 17290 (B1YLR3)
brenda
Jia, Y.Y.; Xie, Y.L.; Yang, L.L.; Shi, H.L.; Lu, Y.F.; Zhang, S.P.; Tang, C.D.; Yao, L.G.; Kan, Y.C.
Expression of novel L-leucine dehydrogenase and high-level production of L-tert-leucine catalyzed by engineered Escherichia coli
Front. Bioeng. Biotechnol.
9
655522
2021
Planifilum fimeticola
brenda
Savrasova, E.A.; Stoynova, N.V.
Application of leucine dehydrogenase Bcd from Bacillus subtilis for L-valine synthesis in Escherichia coli under microaerobic conditions
Heliyon
5
e01406
2019
Bacillus subtilis
brenda
Yamaguchi, H.; Kamegawa, A.; Nakata, K.; Kashiwagi, T.; Mizukoshi, T.; Fujiyoshi, Y.; Tani, K.
Structural insights into thermostabilization of leucine dehydrogenase from its atomic structure by cryo-electron microscopy
J. Struct. Biol.
205
11-21
2019
Geobacillus stearothermophilus (P13154), Geobacillus stearothermophilus
brenda
Wang, Y.; Hou, Y.; Wang, Y.; Zheng, L.; Xu, X.; Pan, K.; Li, R.; Wang, Q.
A novel cold-adapted leucine dehydrogenase from antarctic sea-ice bacterium Pseudoalteromonas sp. ANT178
Mar. Drugs
16
359
2018
Pseudoalteromonas sp. ANT 178 (A0A385GJJ6)
brenda
Liao, L.; Zhang, Y.; Wang, Y.; Fu, Y.; Zhang, A.; Qiu, R.; Yang, S.; Fang, B.
Construction and characterization of a novel glucose dehydrogenase-leucine dehydrogenase fusion enzyme for the biosynthesis of L-tert-leucine
Microb. Cell Fact.
20
003
2021
Lysinibacillus sphaericus (Q7SIB4)
brenda
Ouyang, S.; Li, X.; Sun, X.; Ouyang, J.; Yong, Q.
A thermostable leucine dehydrogenase from Bacillus coagulans NL01 Expression, purification and characterization
Process Biochem.
90
89-96
2020
Weizmannia coagulans, Weizmannia coagulans NL01
-
brenda
Yamaguchi, H.; Kamegawa, A.; Nakata, K.; Kashiwagi, T.; Fujiyoshi, Y.; Tani, K.; Mizukoshi, T.
Leucine Dehydrogenase structure and thermostability
Subcell. Biochem.
96
355-372
2021
Geobacillus stearothermophilus (A0A0K2HC96), Geobacillus stearothermophilus, Geobacillus stearothermophilus DSM 13240 (A0A0K2HC96)
brenda