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2-(3-hydroxy-1-adamantyl)-2-oxoethanoic acid + NH3 + NADH
(S)-3-hydroxyadamantylglycine + H2O + NAD+
-
modified PDH which contains two amino acid changes at the C-terminus and a 12 amino acid extension of the C-terminus is more effective with keto acid 2-(3-hydroxy-1-adamantyl)-2-oxoethanoic acid and less effective with phenylpyruvate than the wild type PDH
-
-
?
2-chloro-phenylpyruvate + NH3 + NADH
2-chloro-L-phenylalanine + H2O + NAD+
-
7% of activity with phenylpyruvate
-
-
?
2-fluoro-phenylpyruvate + NH3 + NADH
2-fluoro-L-phenylalanine + H2O + NAD+
-
6.6% of activity with phenylpyruvate
-
-
?
2-oxo-4-methylpentanoate + NH3 + NADH
L-Ile + NAD+ + H2O
2-oxo-4-methylthiobutanoate + NH3 + NADH
L-Met + NAD+ + H2O
2-oxo-4-phenylbutanoic acid + NH3 + NADH + H+
(S)-2-amino-4-phenylbutyric acid + H2O + NAD+
2-oxo-4-phenylbutanoic acid + NH3 + NADH + H+
L-homophenylalanine + H2O + NAD+
-
-
-
?
2-oxobutanoate + NH3 + NADH
2-aminobutanoate + NAD+ + H2O
-
5.5% of the activity with phenylpyruvate
-
-
?
2-oxohexanoate + NH3 + NADH
2-aminohexanoate + H2O + NAD+
2-oxoisohexanoate + NH3 + NADH
L-Leu + NAD+ + H2O
2-oxopentanoate + NH3 + NADH
L-norvaline + NAD+ + H2O
3-chloro-phenylpyruvate + NH3 + NADH
3-chloro-L-phenylalanine + H2O + NAD+
-
0.8% of activity with phenylpyruvate
-
-
?
3-cyclohexyl-2-oxopropionic acid + NH3 + NADH
3-cyclohexyl-2-aminopropionic acid + H2O + NAD+
-
6.1% of activity with phenylpyruvate
-
-
?
3-fluoro-phenylpyruvate + NH3 + NADH
3-fluoro-L-phenylalanine + H2O + NAD+
-
23% of activity with phenylpyruvate
-
-
?
4-chloro-L-phenylalanine + H2O + NAD+
4-chloro-phenylpyruvate + NH3 + NADH
-
-
-
-
?
4-chloro-phenylpyruvate + NH3 + NADH
4-chloro-L-phenylalanine + H2O + NAD+
-
62% of activity with phenylpyruvate
-
-
?
4-fluoro-L-phenylalanine + H2O + NAD+
4-fluoro-phenylpyruvate + NH3 + NADH
-
-
-
-
?
4-fluoro-phenylpyruvate + NH3 + NADH
4-fluoro-L-phenylalanine + H2O + NAD+
4-hydroxyphenylpyruvate + NH3 + NADH
L-Tyr + NAD+ + H2O
4-hydroxyphenylpyruvate + NH3 + NADH + H+
L-tyrosine + NAD+ + H2O
4-methoxy-L-phenylalanine + H2O + NAD+
4-methoxy-phenylpyruvate + NH3 + NADH
-
-
-
-
?
4-methoxy-phenylpyruvate + NH3 + NADH
4-methoxy-L-phenylalanine + H2O + NAD+
4-methyl-2-oxopentanoate + NH3 + NADH + H+
L-leucine + NAD+ + H2O
-
-
-
-
r
4-methyl-L-phenylalanine + H2O + NAD+
4-methyl-phenylpyruvate + NH3 + NADH
-
-
-
-
?
4-methyl-phenylpyruvate + NH3 + NADH
4-methyl-L-phenylalanine + H2O + NAD+
-
15% of activity with phenylpyruvate
-
-
?
4-nitro-L-phenylalanine + H2O + NAD+
4-nitro-phenylpyruvate + NH3 + NADH
-
-
-
-
?
4-nitro-phenylpyruvate + NH3 + NADH
4-nitro-L-phenylalanine + H2O + NAD+
-
reaction with the immobilized mutant enzyme N145A
-
-
?
4-phenyl-2-butanone + NH3 + NADH + H+
(R)-1-methyl-3-phenylpropylamine + H2O + NAD+
substrate for mutant enzyme K66Q/S149G/N262C
-
-
?
4-pyridyl-phenylpyruvate + NH3 + NADH
4-pyridyl-L-phenylalanine + H2O + NAD+
-
9% of activity with phenylpyruvate
-
-
?
4-trifluoromethyl-phenylpyruvate + NH3 + NADH
4-trifluoromethyl-L-phenylalanine + H2O + NAD+
alloisoleucine + H2O + NAD+
3-methyl-2-oxopentanoate + NADH + NH3
alpha-ketocaproic acid + NH3 + NADH
alpha-aminocaproic acid + H2O + NAD+
-
12.8% of activity with phenylpyruvate
-
-
?
DL-propargylglycine + phenazine ethosulfate + 2-(4-iodophenyl)-3-(4-nitrophenyl)-5-phenyltetrazolium chloridehydrate + NAD+
? + NADH
-
substrate is poorly fertilized by wild type enzyme, but using muteins with different mutations higher turnover can be achieved
-
-
?
indole-3-pyruvate + NH3 + NADH + H+
L-Trp + NAD+ + H2O
indolepyruvate + NH3 + NADH
?
L-2-amino-n-butyric acid + H2O + NAD+
2-oxobutanoate + NADH + NH3
-
1.0% of the activity with L-Phe
-
-
?
L-2-aminohexanoic acid + H2O + NAD+
2-oxohexanoate + NADH + NH3
-
19% of the activity with L-Phe
-
-
?
L-alpha-amino-beta-phenylbutyrate + H2O + NAD+
2-oxo-3-phenylbutyrate + NADH + NH3
-
7.0% of the activity with L-Phe
-
-
?
L-ethionine + H2O + NAD+
4-ethylthio-2-oxobutanoate + NH3 + NADH
L-isoleucine + H2O + NAD+
3-methyl-2-oxopentanoate + NH3 + NADH
-
-
-
-
r
L-Leu + H2O + NAD+
3-methyl-2-oxopentanoic acid + NH3 + NADH
L-leucine + H2O + NAD+
3,3-dimethyl-2-oxo-butanoate + NH3 + NADH
L-Met + H2O + NAD+
2-oxo-4-methylthiobutanoate + NH3 + NADH
L-methionine + H2O + NAD+
(4-methylsulfanyl)-2-oxobutanoate + NH3 + NADH
L-norleucine + H2O + NAD+
2-oxohexanoate + NH3 + NADH
L-norleucine + H2O + NAD+
2-oxohexanoic acid + NADH + NH3
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH
L-Phe + H2O + NAD+
phenylpyruvate + NH3 + NADH
L-phenylalanine + H2O + 3-acetylpyridine-NAD+
phenylpyruvate + NH3 + acetylpyridine-NADH
L-phenylalanine + H2O + 3-pyridinealdehyde-NAD+
phenylpyruvate + NH3 + 3-pyridinealdehyde-NADH
L-phenylalanine + H2O + deamino-NAD+
phenylpyruvate + NH3 + deamino-NADH
L-phenylalanine + H2O + NAD+
phenylpyruvate + NH3 + NADH
L-phenylalanine + H2O + NAD+
phenylpyruvate + NH3 + NADH + H+
L-phenylalanine + H2O + NADP+
phenylpyruvate + NH3 + NADPH
L-phenylalanine + H2O + oxidized beta-nicotinamide guanine dinucleotide
phenylpyruvate + NH3 + reduced beta-nicotinamide guanine dinucleotide
-
at 86% of the activity with NAD+
-
?
L-phenylalanine + H2O + oxidized beta-nicotinamide hypoxanthine dinucleotide
phenylpyruvate + NH3 + reduced beta-nicotinamide hypoxanthine dinucleotide
-
at 86% of the activity with NAD+
-
?
L-phenylalanine + H2O + thio-NAD+
phenylpyruvate + NH3 + thio-NADH
-
at 86% of the activity with NAD+
-
?
L-phenylalanine + H2O + thionicotinamide-NAD+
phenylpyruvate + NH3 + thionicotinamide-NADH
L-phenylalanine methyl ester + H2O + NAD+
phenylpyruvic acid methyl ester + NH3 + NADH
L-phenylalaninol + H2O + NAD+
1-hydroxyacetone + NADH + NH3
-
9.4% of the activity with L-Phe
-
-
?
L-Trp + H2O + NAD+
indole-3-pyruvate + NH3 + NADH
L-tryptophan + H2O + NAD+
3-(1H-indol-3-yl)-2-oxopropanoate + NH3 + NADH
-
2% of activity with L-phenylalanine
-
-
r
L-Tyr + H2O + NAD+
4-hydroxyphenylpyruvate + NH3 + NADH
L-tyrosine + H2O + NAD+
(4-hydroxyphenyl)pyruvate + NH3 + NADH
L-tyrosine + H2O + NAD+
(4-hydroxyphenyl)pyruvate + NH3 + NADH + H+
-
-
-
?
L-Val + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
L-valine + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
m-fluoro-DL-phenylalanine + H2O + NAD+
3-(3-fluorophenyl)-2-oxopropionate + NADH + NH3
o-fluoro-DL-phenylalanine + H2O + NAD+
3-(2-fluorophenyl)-2-oxopropionate + NADH + NH3
p-amino-L-phenylalanine + H2O + NAD+
?
-
-
-
-
?
p-fluoro-DL-phenylalanine + H2O + NAD+
(4-fluorophenyl)-2-oxopropionate + NADH + NH3
phenylacetone + NH3 + NADH + H+
(R)-amphetamine + H2O + NAD+
substrate for mutant enzyme K66Q/S149G/N262C
-
-
?
phenylalaninamide + H2O + NAD+
2-oxo-3-phenylpropionamide + NADH + NH3
-
9.0% of the activity with L-Phe
-
-
?
phenylalanine hydroxamate + H2O + NAD+
2-oxo-3-phenylpropionic acid hydroxamate + NADH + NH3
-
1.0% of the activity with L-Phe
-
-
?
phenylpyruvate + NH3 + NADH
L-Phe + H2O + NAD+
-
-
-
-
r
phenylpyruvate + NH3 + NADH
L-phenylalanine + H2O + NAD+
-
-
-
-
?
phenylpyruvate + NH3 + NADH + H+
L-phenylalanine + H2O + NAD+
additional information
?
-
-
specific activity of the chimeric enzyme is 6% of that of the parental phenylalanine dehydrogenase and shows a broad substrate specificity in the oxidative deamination, like phenylalanine dehydrogenase. However, it acts much more effectively than phenylalanine dehydrogenase on Ile and Val. The parent enzyme and the chimeric enzyme belong to the pro-S specific dehydrogenase
-
-
?
2-oxo-4-methylpentanoate + NH3 + NADH
L-Ile + NAD+ + H2O
-
13% of the activity with phenylpyruvate
-
-
?
2-oxo-4-methylpentanoate + NH3 + NADH
L-Ile + NAD+ + H2O
-
-
-
-
?
2-oxo-4-methylpentanoate + NH3 + NADH
L-Ile + NAD+ + H2O
-
16% of the activity with phenylpyruvate
-
-
?
2-oxo-4-methylthiobutanoate + NH3 + NADH
L-Met + NAD+ + H2O
-
16% of the activity with phenylpyruvate
-
-
?
2-oxo-4-methylthiobutanoate + NH3 + NADH
L-Met + NAD+ + H2O
-
33% of the activity with L-Phe
-
-
?
2-oxo-4-methylthiobutanoate + NH3 + NADH
L-Met + NAD+ + H2O
-
-
-
-
?
2-oxo-4-methylthiobutanoate + NH3 + NADH
L-Met + NAD+ + H2O
-
55% of the activity with phenylpyruvate
-
-
?
2-oxo-4-phenylbutanoic acid + NH3 + NADH + H+
(S)-2-amino-4-phenylbutyric acid + H2O + NAD+
-
-
-
-
r
2-oxo-4-phenylbutanoic acid + NH3 + NADH + H+
(S)-2-amino-4-phenylbutyric acid + H2O + NAD+
-
-
-
-
r
2-oxohexanoate + NH3 + NADH
2-aminohexanoate + H2O + NAD+
-
31% of the activity with phenylpyruvate
-
-
?
2-oxohexanoate + NH3 + NADH
2-aminohexanoate + H2O + NAD+
-
240% of the activity with phenylpyruvate
-
-
?
2-oxohexanoate + NH3 + NADH
2-aminohexanoate + H2O + NAD+
-
240% of the activity with phenylpyruvate
-
-
?
2-oxohexanoate + NH3 + NADH
2-aminohexanoate + H2O + NAD+
-
-
-
-
?
2-oxohexanoate + NH3 + NADH
2-aminohexanoate + H2O + NAD+
-
-
-
-
?
2-oxohexanoate + NH3 + NADH
2-aminohexanoate + H2O + NAD+
-
130% of the activity with phenylpyruvate
-
-
?
2-oxoisohexanoate + NH3 + NADH
L-Leu + NAD+ + H2O
-
-
-
-
?
2-oxoisohexanoate + NH3 + NADH
L-Leu + NAD+ + H2O
-
47% of the activity with phenylpyruvate
-
-
?
2-oxopentanoate + NH3 + NADH
L-norvaline + NAD+ + H2O
-
12% of the activity with phenylpyruvate
-
-
?
2-oxopentanoate + NH3 + NADH
L-norvaline + NAD+ + H2O
-
-
-
-
?
2-oxopentanoate + NH3 + NADH
L-norvaline + NAD+ + H2O
-
37% of the activity with phenylpyruvate
-
-
?
4-fluoro-phenylpyruvate + NH3 + NADH
4-fluoro-L-phenylalanine + H2O + NAD+
-
114% of activity with phenylpyruvate
-
-
?
4-fluoro-phenylpyruvate + NH3 + NADH
4-fluoro-L-phenylalanine + H2O + NAD+
-
preferred substrate of mutant N145V
-
-
r
4-hydroxyphenylpyruvate + NH3 + NADH
L-Tyr + NAD+ + H2O
-
53% of the activity with phenylpyruvate
-
-
?
4-hydroxyphenylpyruvate + NH3 + NADH
L-Tyr + NAD+ + H2O
-
-
-
-
?
4-hydroxyphenylpyruvate + NH3 + NADH
L-Tyr + NAD+ + H2O
-
28% of the activity with phenylpyruvate
-
-
?
4-hydroxyphenylpyruvate + NH3 + NADH
L-Tyr + NAD+ + H2O
-
28% of the activity with phenylpyruvate
-
-
?
4-hydroxyphenylpyruvate + NH3 + NADH
L-Tyr + NAD+ + H2O
-
-
-
-
?
4-hydroxyphenylpyruvate + NH3 + NADH
L-Tyr + NAD+ + H2O
-
5% of the activity with L-Phe
-
-
?
4-hydroxyphenylpyruvate + NH3 + NADH
L-Tyr + NAD+ + H2O
-
5% of the activity with L-Phe
-
-
?
4-hydroxyphenylpyruvate + NH3 + NADH
L-Tyr + NAD+ + H2O
-
-
-
-
?
4-hydroxyphenylpyruvate + NH3 + NADH
L-Tyr + NAD+ + H2O
-
80% of the activity with phenylpyruvate
-
-
?
4-hydroxyphenylpyruvate + NH3 + NADH + H+
L-tyrosine + NAD+ + H2O
-
-
-
-
r
4-hydroxyphenylpyruvate + NH3 + NADH + H+
L-tyrosine + NAD+ + H2O
-
-
-
-
r
4-methoxy-phenylpyruvate + NH3 + NADH
4-methoxy-L-phenylalanine + H2O + NAD+
-
15% of activity with phenylpyruvate
-
-
?
4-methoxy-phenylpyruvate + NH3 + NADH
4-methoxy-L-phenylalanine + H2O + NAD+
-
preferred substrate of mutant N145L
-
-
r
4-trifluoromethyl-phenylpyruvate + NH3 + NADH
4-trifluoromethyl-L-phenylalanine + H2O + NAD+
-
0.9% of activity with phenylpyruvate
-
-
?
4-trifluoromethyl-phenylpyruvate + NH3 + NADH
4-trifluoromethyl-L-phenylalanine + H2O + NAD+
-
preferred substrate of mutant N145A
-
-
r
alloisoleucine + H2O + NAD+
3-methyl-2-oxopentanoate + NADH + NH3
-
4.3% of the activity with L-Phe
-
-
?
alloisoleucine + H2O + NAD+
3-methyl-2-oxopentanoate + NADH + NH3
-
26% of the activity with L-Phe
-
-
?
indole-3-pyruvate + NH3 + NADH + H+
L-Trp + NAD+ + H2O
-
54% of the activity with phenylpyruvate
-
-
?
indole-3-pyruvate + NH3 + NADH + H+
L-Trp + NAD+ + H2O
-
54% of the activity with phenylpyruvate
-
-
?
indolepyruvate + NH3 + NADH
?
-
-
-
-
?
indolepyruvate + NH3 + NADH
?
-
3% of the activity with L-Phe
-
-
?
L-ethionine + H2O + NAD+
4-ethylthio-2-oxobutanoate + NH3 + NADH
-
7.0% of the activity with L-Phe
-
-
?
L-ethionine + H2O + NAD+
4-ethylthio-2-oxobutanoate + NH3 + NADH
-
13.0% of the activity with L-Phe
-
-
?
L-ethionine + H2O + NAD+
4-ethylthio-2-oxobutanoate + NH3 + NADH
-
-
-
-
?
L-Leu + H2O + NAD+
3-methyl-2-oxopentanoic acid + NH3 + NADH
-
3.0% of the activity with L-Phe
-
-
?
L-Leu + H2O + NAD+
3-methyl-2-oxopentanoic acid + NH3 + NADH
-
-
-
-
?
L-Leu + H2O + NAD+
3-methyl-2-oxopentanoic acid + NH3 + NADH
-
-
-
-
?
L-Leu + H2O + NAD+
3-methyl-2-oxopentanoic acid + NH3 + NADH
-
-
-
-
?
L-Leu + H2O + NAD+
3-methyl-2-oxopentanoic acid + NH3 + NADH
-
-
-
-
?
L-leucine + H2O + NAD+
3,3-dimethyl-2-oxo-butanoate + NH3 + NADH
-
-
-
-
r
L-leucine + H2O + NAD+
3,3-dimethyl-2-oxo-butanoate + NH3 + NADH
-
1% of activity with L-phenylalanine
-
-
r
L-Met + H2O + NAD+
2-oxo-4-methylthiobutanoate + NH3 + NADH
-
8.0% of the activity with L-Phe
-
-
?
L-Met + H2O + NAD+
2-oxo-4-methylthiobutanoate + NH3 + NADH
-
-
-
-
?
L-Met + H2O + NAD+
2-oxo-4-methylthiobutanoate + NH3 + NADH
-
-
-
-
?
L-Met + H2O + NAD+
2-oxo-4-methylthiobutanoate + NH3 + NADH
-
4% of the activity with L-Phe
-
-
?
L-Met + H2O + NAD+
2-oxo-4-methylthiobutanoate + NH3 + NADH
-
4% of the activity with L-Phe
-
-
?
L-Met + H2O + NAD+
2-oxo-4-methylthiobutanoate + NH3 + NADH
-
-
-
-
?
L-Met + H2O + NAD+
2-oxo-4-methylthiobutanoate + NH3 + NADH
-
2.2% of the activity with L-Phe
-
-
?
L-methionine + H2O + NAD+
(4-methylsulfanyl)-2-oxobutanoate + NH3 + NADH
-
-
-
-
r
L-methionine + H2O + NAD+
(4-methylsulfanyl)-2-oxobutanoate + NH3 + NADH
-
3% of activity with L-phenylalanine
-
-
r
L-norleucine + H2O + NAD+
2-oxohexanoate + NH3 + NADH
-
-
-
-
r
L-norleucine + H2O + NAD+
2-oxohexanoate + NH3 + NADH
-
4.5% of activity with L-phenylalanine
-
-
r
L-norleucine + H2O + NAD+
2-oxohexanoic acid + NADH + NH3
-
19% of the activity with L-Phe
-
-
?
L-norleucine + H2O + NAD+
2-oxohexanoic acid + NADH + NH3
-
15.6% of the activity with L-Phe
-
-
?
L-norleucine + H2O + NAD+
2-oxohexanoic acid + NADH + NH3
-
-
-
-
?
L-norleucine + H2O + NAD+
2-oxohexanoic acid + NADH + NH3
-
-
-
-
?
L-norleucine + H2O + NAD+
2-oxohexanoic acid + NADH + NH3
-
-
-
-
?
L-norleucine + H2O + NAD+
2-oxohexanoic acid + NADH + NH3
-
-
-
-
?
L-norleucine + H2O + NAD+
2-oxohexanoic acid + NADH + NH3
-
30% of the activity with L-Phe
-
-
?
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH
-
5.0% of the activity with L-Phe
-
-
?
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH
-
-
-
-
r
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH
-
-
-
-
?
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH
-
-
-
-
?
L-norvaline + H2O + NAD+
2-oxopentanoate + NH3 + NADH
-
28% of the activity with L-Phe
-
-
?
L-Phe + H2O + NAD+
phenylpyruvate + NH3 + NADH
-
-
-
-
?
L-Phe + H2O + NAD+
phenylpyruvate + NH3 + NADH
-
-
-
-
r
L-Phe + H2O + NAD+
phenylpyruvate + NH3 + NADH
-
-
-
-
r
L-Phe + H2O + NAD+
phenylpyruvate + NH3 + NADH
-
the equilibrium favors L-Phe formation
-
-
r
L-Phe + H2O + NAD+
phenylpyruvate + NH3 + NADH
-
the enzyme is involved in the degradation of Phe
-
?
L-Phe + H2O + NAD+
phenylpyruvate + NH3 + NADH
-
the reductive amination proceeds through a sequential ordered ternary-binary mechanism
-
-
r
L-Phe + H2O + NAD+
phenylpyruvate + NH3 + NADH
-
the reductive amination proceeds through a sequential ordered ternary-binary mechanism
-
-
r
L-Phe + H2O + NAD+
phenylpyruvate + NH3 + NADH
-
-
-
-
?
L-Phe + H2O + NAD+
phenylpyruvate + NH3 + NADH
-
-
-
r
L-Phe + H2O + NAD+
phenylpyruvate + NH3 + NADH
-
-
-
-
r
L-Phe + H2O + NAD+
phenylpyruvate + NH3 + NADH
-
-
-
r
L-Phe + H2O + NAD+
phenylpyruvate + NH3 + NADH
-
-
-
-
r
L-Phe + H2O + NAD+
phenylpyruvate + NH3 + NADH
-
-
-
-
r
L-Phe + H2O + NAD+
phenylpyruvate + NH3 + NADH
-
-
-
-
r
L-Phe + H2O + NAD+
phenylpyruvate + NH3 + NADH
-
-
-
-
r
L-Phe + H2O + NAD+
phenylpyruvate + NH3 + NADH
-
-
-
-
r
L-Phe + H2O + NAD+
phenylpyruvate + NH3 + NADH
-
-
-
-
r
L-Phe + H2O + NAD+
phenylpyruvate + NH3 + NADH
-
the equilibrium favors L-Phe formation
-
-
r
L-Phe + H2O + NAD+
phenylpyruvate + NH3 + NADH
-
-
-
-
r
L-Phe + H2O + NAD+
phenylpyruvate + NH3 + NADH
-
the equilibrium favors L-Phe formation
-
-
r
L-Phe + H2O + NAD+
phenylpyruvate + NH3 + NADH
-
-
-
-
r
L-Phe + H2O + NAD+
phenylpyruvate + NH3 + NADH
-
-
-
-
r
L-phenylalanine + H2O + 3-acetylpyridine-NAD+
phenylpyruvate + NH3 + acetylpyridine-NADH
-
at 241% of the activity with NAD+
-
?
L-phenylalanine + H2O + 3-acetylpyridine-NAD+
phenylpyruvate + NH3 + acetylpyridine-NADH
-
at 241% of the activity with NAD+
-
?
L-phenylalanine + H2O + 3-acetylpyridine-NAD+
phenylpyruvate + NH3 + acetylpyridine-NADH
-
350% of the activity with NAD+
-
-
?
L-phenylalanine + H2O + 3-pyridinealdehyde-NAD+
phenylpyruvate + NH3 + 3-pyridinealdehyde-NADH
-
at 9.2% of the activity with NAD+
-
?
L-phenylalanine + H2O + 3-pyridinealdehyde-NAD+
phenylpyruvate + NH3 + 3-pyridinealdehyde-NADH
-
55% of the activity with NAD+
-
-
?
L-phenylalanine + H2O + deamino-NAD+
phenylpyruvate + NH3 + deamino-NADH
-
at 86% of the activity with NAD+
-
?
L-phenylalanine + H2O + deamino-NAD+
phenylpyruvate + NH3 + deamino-NADH
-
at 86% of the activity with NAD+
-
?
L-phenylalanine + H2O + NAD+
phenylpyruvate + NH3 + NADH
-
-
-
-
r
L-phenylalanine + H2O + NAD+
phenylpyruvate + NH3 + NADH
-
-
-
-
r
L-phenylalanine + H2O + NAD+
phenylpyruvate + NH3 + NADH + H+
-
-
-
-
?
L-phenylalanine + H2O + NAD+
phenylpyruvate + NH3 + NADH + H+
-
-
-
?
L-phenylalanine + H2O + NAD+
phenylpyruvate + NH3 + NADH + H+
-
-
-
?
L-phenylalanine + H2O + NAD+
phenylpyruvate + NH3 + NADH + H+
-
-
-
?
L-phenylalanine + H2O + NAD+
phenylpyruvate + NH3 + NADH + H+
Halalkalibacterium halodurans
-
-
-
?
L-phenylalanine + H2O + NAD+
phenylpyruvate + NH3 + NADH + H+
Halalkalibacterium halodurans DSM 18197
-
-
-
?
L-phenylalanine + H2O + NAD+
phenylpyruvate + NH3 + NADH + H+
-
-
-
-
?
L-phenylalanine + H2O + NAD+
phenylpyruvate + NH3 + NADH + H+
-
-
-
-
r
L-phenylalanine + H2O + NAD+
phenylpyruvate + NH3 + NADH + H+
-
-
-
?
L-phenylalanine + H2O + NAD+
phenylpyruvate + NH3 + NADH + H+
-
-
-
-
r
L-phenylalanine + H2O + NAD+
phenylpyruvate + NH3 + NADH + H+
-
-
-
-
r
L-phenylalanine + H2O + NAD+
phenylpyruvate + NH3 + NADH + H+
-
-
-
-
r
L-phenylalanine + H2O + NAD+
phenylpyruvate + NH3 + NADH + H+
-
-
-
?
L-phenylalanine + H2O + NADP+
phenylpyruvate + NH3 + NADPH
-
at 6.6% of the activity with NAD+
-
?
L-phenylalanine + H2O + NADP+
phenylpyruvate + NH3 + NADPH
-
at 6.6% of the activity with NAD+
-
?
L-phenylalanine + H2O + thionicotinamide-NAD+
phenylpyruvate + NH3 + thionicotinamide-NADH
-
at 101% of the activity with NAD+
-
?
L-phenylalanine + H2O + thionicotinamide-NAD+
phenylpyruvate + NH3 + thionicotinamide-NADH
-
at 101% of the activity with NAD+
-
?
L-phenylalanine methyl ester + H2O + NAD+
phenylpyruvic acid methyl ester + NH3 + NADH
-
38% of the activity with L-Phe
-
-
?
L-phenylalanine methyl ester + H2O + NAD+
phenylpyruvic acid methyl ester + NH3 + NADH
-
-
-
-
?
L-Trp + H2O + NAD+
indole-3-pyruvate + NH3 + NADH
-
4% of the activity with L-Phe
-
-
?
L-Trp + H2O + NAD+
indole-3-pyruvate + NH3 + NADH
-
7.5% of the activity with L-Phe
-
-
?
L-Trp + H2O + NAD+
indole-3-pyruvate + NH3 + NADH
-
2% of the activity with L-Phe
-
-
?
L-Trp + H2O + NAD+
indole-3-pyruvate + NH3 + NADH
-
2% of the activity with L-Phe
-
-
?
L-Tyr + H2O + NAD+
4-hydroxyphenylpyruvate + NH3 + NADH
-
9.0% of the activity with L-Phe
-
-
?
L-Tyr + H2O + NAD+
4-hydroxyphenylpyruvate + NH3 + NADH
-
-
-
-
?
L-Tyr + H2O + NAD+
4-hydroxyphenylpyruvate + NH3 + NADH
-
-
-
-
?
L-Tyr + H2O + NAD+
4-hydroxyphenylpyruvate + NH3 + NADH
-
-
-
-
?
L-Tyr + H2O + NAD+
4-hydroxyphenylpyruvate + NH3 + NADH
-
-
-
-
?
L-Tyr + H2O + NAD+
4-hydroxyphenylpyruvate + NH3 + NADH
-
-
-
-
?
L-Tyr + H2O + NAD+
4-hydroxyphenylpyruvate + NH3 + NADH
-
-
-
-
?
L-Tyr + H2O + NAD+
4-hydroxyphenylpyruvate + NH3 + NADH
-
40% of the activity with L-Phe
-
-
?
L-tyrosine + H2O + NAD+
(4-hydroxyphenyl)pyruvate + NH3 + NADH
-
-
-
-
r
L-tyrosine + H2O + NAD+
(4-hydroxyphenyl)pyruvate + NH3 + NADH
-
-
-
-
r
L-tyrosine + H2O + NAD+
(4-hydroxyphenyl)pyruvate + NH3 + NADH
-
74% of activity with L-phenylalanine
-
-
r
L-Val + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
-
4.0% of the activity with L-Phe
-
-
?
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
-
-
-
-
?
L-valine + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
-
-
-
-
r
L-valine + H2O + NAD+
3-methyl-2-oxobutanoate + NH3 + NADH
-
1.8% of activity with L-phenylalanine
-
-
r
m-fluoro-DL-phenylalanine + H2O + NAD+
3-(3-fluorophenyl)-2-oxopropionate + NADH + NH3
-
11% of the activity with L-Phe
-
-
?
m-fluoro-DL-phenylalanine + H2O + NAD+
3-(3-fluorophenyl)-2-oxopropionate + NADH + NH3
-
7.7% of the activity with L-Phe
-
-
?
m-fluoro-DL-phenylalanine + H2O + NAD+
3-(3-fluorophenyl)-2-oxopropionate + NADH + NH3
-
as effective as L-Phe
-
-
?
o-fluoro-DL-phenylalanine + H2O + NAD+
3-(2-fluorophenyl)-2-oxopropionate + NADH + NH3
-
2% of the activity with L-Phe
-
-
?
o-fluoro-DL-phenylalanine + H2O + NAD+
3-(2-fluorophenyl)-2-oxopropionate + NADH + NH3
-
65% of the activity with L-Phe
-
-
?
p-fluoro-DL-phenylalanine + H2O + NAD+
(4-fluorophenyl)-2-oxopropionate + NADH + NH3
-
34% of the activity with L-Phe
-
-
?
p-fluoro-DL-phenylalanine + H2O + NAD+
(4-fluorophenyl)-2-oxopropionate + NADH + NH3
-
8.3% of the activity with L-Phe
-
-
?
p-fluoro-DL-phenylalanine + H2O + NAD+
(4-fluorophenyl)-2-oxopropionate + NADH + NH3
-
118% of the activity with L-Phe
-
-
?
phenylpyruvate + NH3 + NADH + H+
L-phenylalanine + H2O + NAD+
Halalkalibacterium halodurans
-
-
-
?
phenylpyruvate + NH3 + NADH + H+
L-phenylalanine + H2O + NAD+
Halalkalibacterium halodurans DSM 18197
-
-
-
?
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V144D
mutantion significantly reduces kcat value and also decreases Km value for phenylalanine relative to that of wild-type
V144L
mutation considerably increases specific activity toward phenylalanine and decreases toward L-tyrosine. ThePhe/Tyr specificity constant in V144L increases more than 4fold
V144N
mutation reduces the specific activity toward phenylalanine and increases toward tyrosine
D126N
-
mutant without enzymatic activity
D209G
-
mutant named 1stA7, active with DL-propargylglycine
D209G/Q18H/I336F
-
mutant named 1stA7/1stB6, active with DL-propargylglycine
E313G
-
mutant named H7H10, active with DL-propargylglycine
F110Y/G124C/G293A
-
mutant named H14A12, active with DL-propargylglycine
G124A/E313G
-
mutant named 25B12, active with DL-propargylglycine
G124A/E313N
-
mutant named 20E1, active with DL-propargylglycine
K224Q/L283F
-
mutant named 2ndB10, active with DL-propargylglycine
K224Q/L283F/E313G
-
mutant named 2ndB10/H7H10, active with DL-propargylglycine
N145I
-
19% of wild-type kcat with phenylalanine
Q18H/I336F
-
mutant named 1stB6, active with DL-propargylglycine
Q18H/I336F/E313G
-
mutant named 1stB6/H7H10, active with DL-propargylglycine
V135I/I308N/Q363H
-
mutant named H21D1, active with DL-propargylglycine
V33A/A206D/L283F
-
mutant named 2ndC2., active with DL-propargylglycine
K66Q/S149G/N262C
the mutant shows activity with phenylacetone and 4-phenyl-2-butanone
F124M/V125S/H126I/A127I/A128Y/R129Q
-
the catalytic efficiencies of the mutant enzyme with aliphatic amino acids and aliphatic keto acids as substrates are 0.5% to 2% of that of the wild-type enzyme. The efficiencies for L-Phe and phenylpyruvate decreases to 0.0008% and 0.035% of that of the wild-type enzyme, respectively. Enzyme exists as monomeric or dimeric form, compared to wild-type enzyme which exists as hexameric enzyme form. Thermostability is lowered by mutation
K173A
-
37°C, t1/2 of the mutant enzyme is 60 min, compared to 48 min for the wild type enzyme, without addition of substrate or cofactor
K69A
-
37°C, t1/2 of the mutant enzyme is 50 min, compared to 48 min for the wild type enzyme, without addition of substrate or cofactor. Km-value for L-Phe is 1400fold higher compared to wild type enzyme, Km-value for phenylpyruvate is 128fold higher compared to wild type enzyme. Turnover number for deamination is 686fold lower than that of wild-type enzyme, turnover-number for amination is 43fold lower than that of wild-type enzyme
K69A/K81A
-
37°C, t1/2 of the mutant enzyme is 450 min, compared to 48 min for the wild type enzyme, without addition of substrate or cofactor. Km-value for L-Phe is 200fold higher compared to wild type enzyme, Km-value for phenylpyruvate is 108fold higher compared to wild type enzyme. Turnover number for deamination is 110fold lower than that of wild-type enzyme, turnover-number for amination is 61fold lower than that of wild-type enzyme
K81A
-
37°C, t1/2 of the mutant enzyme is 38 min, compared to 48 min for the wild type enzyme, without addition of substrate or cofactor. Turnover number for deamination is 440fold lower than that of wild-type enzyme, turnover-number for amination is 42fold lower than that of wild-type enzyme
K89A
-
37°C, t1/2 of the mutant enzyme is 75 min, compared to 48 min for the wild type enzyme, without addition of substrate or cofactor
K90A
-
37°C, t1/2 of the mutant enzyme is 80 min, compared to 48 min for the wild type enzyme, without addition of substrate or cofactor
R272M/E331Q/E196N
mutant with improved capability of catalyzing 2-(3-hydroxy-1-adamantyl)-2-oxoethanoic acid to the corresponding non-natural amino acid (S)-3-hydroxyadamantylglycine which is the key intermediate of saxagliptin
G124A
-
mutant enzyme has lower activity towards L-Phe and enhanced activity towards almost all aliphatic amino acid substrates compared to the wild-type
G124A
-
12% of wild-type kcat with L-phenylalanine
G124A
-
mutant named 9F5, active with DL-propargylglycine
G124A/L307V
-
mutant enzyme has lower activity towards L-Phe and enhanced activity towards almost all aliphatic amino acid substrates compared to the wild-type
G124A/L307V
-
7.5% of wild-type kcat with L-phenylalanine
L307V
-
mutant enzyme has lower activity towards L-Phe and enhanced activity towards almost all aliphatic amino acid substrates compared to the wild-type
L307V
-
26% of wild-type kcat with L-phenylalanine
L307V
-
shows enhanced pH stability compared to the wild type enzyme
N145A
-
50% of wild-type kcat with phenylalanine
N145A
-
reduced activity with phenylpyruvate, improved activity with non-natural 2-oxo acid substrates
N145A
-
the immobilised biocatalyst is remarkably robust, even in the presence of high concentrations of polar or non-polar organic solvents such as acetone, methanol, n-hexane, toluene and methylene chloride
N145A
-
4-trifluoromethyl-phenylpyruvate is the preferred substrate, the reaction velocity at elevated substrate concentration (5 mM) is almost 10 times higher compared to the wild type enzyme
N145A
-
shows enhanced pH stability compared to the wild type enzyme
N145L
-
12.5% of wild-type kcat with phenylalanine
N145L
-
22% of wild-type activity with phenylpyruvate, improved activity with non-natural 2-oxo acid substrates
N145L
-
4-methoxy-phenylpyruvate is the preferred substrate
N145V
-
25% of wild-type kcat with phenylalanine
N145V
-
reduced activity with phenylpyruvate, improved activity with non-natural 2-oxo acid substrates
N145V
-
4-fluoro-phenylpyruvate is the preferred substrate
additional information
-
covalent immobilization of phenylalanine dehydrogenase onto commercially available enzyme carrier Eupergit CM for the synthesis of unnatural amino acid (S)-2-amino-4-phenylbutyric acid, method optimization and evaluation, overview. The immobilized enzyme shows increased thermostability, activity, broadened pH optimum, and remarkable improvement in operability and storage stability compared to the native enzyme. Immobilized PheDH is successfully applied for the synthesis of (S)-2-amino-4-phenylbutyric acid, achieving enantiomeric excess of more than 99% and yield of more than 80%; comparable to synthesis using the free PheDH
additional information
-
covalent immobilization of phenylalanine dehydrogenase onto commercially available enzyme carrier Eupergit CM for the synthesis of unnatural amino acid (S)-2-amino-4-phenylbutyric acid, method optimization and evaluation, overview. The immobilized enzyme shows increased thermostability, activity, broadened pH optimum, and remarkable improvement in operability and storage stability compared to the native enzyme. Immobilized PheDH is successfully applied for the synthesis of (S)-2-amino-4-phenylbutyric acid, achieving enantiomeric excess of more than 99% and yield of more than 80%; comparable to synthesis using the free PheDH
-
additional information
-
the enzyme is modified initially with 2-amino-4,6-dichloro-s-triazine, and immobilized by hexamethylenediamine and glutaraldehyde. The highest activity of immobilized PheDH is determined as 95.75 U/g support with 56% retained activity. The optimum pH value of immobilized L-PheDH was shifted from pH 10.4 to pH 11.0. pH and thermal stability of the immobilized L-PheDH are improved compared to the native enzyme
additional information
-
construction of a chimeric enzyme consisting of the N-terminal domain of Thermoactinomyces intermedius phenylalanine dehydrogenase, containing the substrate-binding region and the C-terminal domain of leucine dehydrogenase from Bacillus stearothermophilus containing the NAD+-binding region. The chimeric enzyme has a specific activity of 6% of that of the parental phenylalanine dehydrogenase and shows a broad substrate specificity in the oxidative deamination, like phenylalanine dehydrogenase. However, it acts much more effectively than phenylalanine dehydrogenase on Ile and Val
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Okazaki, N.; Hibino, Y.; Asano, Y.; Ohmori, M.; Numao, N.; Kondo, K.
Cloning and nucleotide sequencing of phenylalanine dehydrogenase gene of Bacillus sphaericus
Gene
63
337-341
1988
Lysinibacillus sphaericus, Lysinibacillus sphaericus SCRC-79a
brenda
Asano, Y.; Nakazawa, A.
Crystallization of phenylalanine dehydrogenase from Sporosarcina urea
Agric. Biol. Chem.
49
3631-3632
1985
Sporosarcina ureae
-
brenda
Asano, Y.; Nakazawa, A.; Endo, K.
Novel phenylalanine dehydrogenases from Sporosarcina ureae and Bacillus sphaericus. Purification and characterization
J. Biol. Chem.
262
10346-10354
1987
Lysinibacillus sphaericus, Sporosarcina ureae
brenda
De Boer, L.; Van Rijssel, M.; Euverink, G.J.; Dijkhuizen, L.
Purification, characterization and regulation of a monomeric L-phenylalanine dehydrogenase from the facultative methylotroph Nocardia sp. 239
Arch. Microbiol.
153
12-18
1989
Nocardia sp., Nocardia sp. 239
-
brenda
Misono, H.; Yonezawa, J.; Nagata, S.; Nagasaki, S.
Purification and characterization of a dimeric phenylalanine dehydrogenase from Rhodococcus maris K-18
J. Bacteriol.
171
30-36
1989
Dietzia maris, Dietzia maris K-18
brenda
Asano, Y.; Endo, K.; Nakazawa, A.; Hibino, Y.; Okazaki, N.; Ohmori, M.; Numao, N.; Kondo, K.
Bacillus phenylalanine dehydrogenase produced in Escherichia coli - Its purification and application to L-phenylalanine synthesis
Agric. Biol. Chem.
51
2621-2623
1987
Lysinibacillus sphaericus, Pediococcus acidilactici
-
brenda
Asano, Y.; Nakazawa, A.; Endo, K.; Hibino, Y.; Ohmori, M.; Numao, N.; Kondo, K.
Phenylalanine dehydrogenase of Bacillus badius. Purification, characterization and gene cloning [published erratum appears in Eur J Biochem 1988 Jan 1;170(3):667]
Eur. J. Biochem.
168
153-159
1987
Bacillus badius
brenda
Hummel, W.; Weiss, N.; Kula, M.R.
Isolation and characterization of a bacterium possessing L-phenylalanine dehydrogenase activity
Arch. Microbiol.
137
47-52
1984
Brevibacterium sp.
-
brenda
Hummel, W.; Schuette, H.; Schmidt, E.; Wandrey, C.; Kula, M.R.
Isolation of L-phenylalanine dehydrogenase from Rhodococcus sp. M4 and its application for the production of L-phenylalanine
Appl. Microbiol. Biotechnol.
26
409-416
1987
Rhodococcus sp., Rhodococcus sp. M4
-
brenda
Hummel, W.; Schuette, H.; Kula, M.R.
Enzymatic determination of L-phenylalanine and phenylpyruvate with L-phenylalanine dehydrogenase
Anal. Biochem.
170
397-401
1988
Brevibacterium sp.
brenda
Campagna, R.; Bueckmann, A.F.
Comparison of the production of intracellular L-phenylalanine dehydrogenase by Rhodococcus species M4 and Sporosarcina urea at 50 liter scale
Appl. Microbiol. Biotechnol.
26
417-421
1987
Rhodococcus sp., Sporosarcina ureae, Rhodococcus sp. M4
-
brenda
Wendel, U.; Hummel, W.; Langenbeck, U.
Monitoring of phenylketonuria: a colorimetric method for the determination of plasma phenylalanine using L-phenylalanine dehydrogenase
Anal. Biochem.
180
91-94
1989
Rhodococcus sp., Rhodococcus sp. M4
brenda
Hummel, W.; Schuette, H.; Schmidt, E.; Kula, M.R.
Neue Mglichkeiten zur enzymatischen Herstellung von L-Phenylalanin
GBF Monogr. Ser. Volume date 1988
11
207-210
1989
Rhodococcus sp.
-
brenda
Cooper, A.J.L.; Leung, L.K.H.; Asano, Y.
Enzymatic cycling assay for phenylpyruvate
Anal. Biochem.
183
210-214
1989
Bacillus badius, Sporosarcina ureae
brenda
Asano, Y.; Nakazawa, A.
High yield synthesis of L-amino acids by phenylalanine dehydrogenase from Sporosarcina urea
Agric. Biol. Chem.
51
2035-2036
1987
Sporosarcina ureae
-
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
Thermoactinomyces intermedius
brenda
Kataoka, K.; Tanizawa, K.; Fukui, T.; Ueno, H.; Yoshimura, T.; Esaki, N.; Soda, K.
Identification of active site lysyl residues of phenylalanine dehydrogenase by chemical modification with methyl acetyl phosphate combined with site-directed mutagenesis
J. Biochem.
116
1370-1376
1994
Thermoactinomyces intermedius
brenda
Kataoka, K.; Takada, H.; Yoshimura, T.; Furuyoshi, S.; Esaki, N.; Ohshima, T.; Soda, K.
Site-directed mutagenesis of a hexapeptide segment involved in substrate recognition of phenylalanine dehydrogenase from Thermoactinomyces intermedius
J. Biochem.
114
69-75
1993
Thermoactinomyces intermedius
brenda
Asano, Y.; Tanetani, M.
Thermostable phenylalanine dehydrogenase from a mesophilic Microbacterium sp. strain DM 86-1
Arch. Microbiol.
169
220-224
1998
Microbacterium sp., Microbacterium sp. DM 86-1
brenda
Brunhuber, N.M.W.; Thoden, J.B.; Blanchard, J.S.; Vanhooke, J.L.
Rhodococcus L-Phenylalanine Dehydrogenase: Kinetics, Mechanism, and Structural Basis for Catalytic Specificity
Biochemistry
39
9174-9187
2000
Rhodococcus sp.
brenda
Vanhooke, J.L.; Thoden, J.B.; Brunhuber, N.M.W.; Blanchard, J.S.; Holden, H.M.
Phenylalanine dehydrogenase from Rhodococcus sp. M4: High-resolution x-ray analyses of inhibitory ternary complexes reveal key features in the oxidative deamination mechanism
Biochemistry
38
2326-2339
1999
Rhodococcus sp.
brenda
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Bacillus badius (Q59224), Bacillus badius
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Thermoactinomyces intermedius (P22823)
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Sporosarcina sp.
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