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(S)-2-aminoadipate 6-semialdehyde
(S)-2,3,4,5-tetrahydropiperidine-2-carboxylate + H2O
1-phenylbutan-1-one + NADH + H+ + NH3
(1R)-1-phenylbutan-1-amine + NAD+ + H2O
mutant F173A, 10 mM, 87% conversion, product in R-configuration, 99.8% ee
-
-
?
1-phenylethan-1-one + NADH + H+ + NH3
(1R)-1-phenylethan-1-amine + NAD+ + H2O
mutant F173A, 10 mM, 99% conversion, product in R-configuration, 99.9% ee
-
-
?
1-phenylpentan-1-one + NADH + H+ + NH3
1-phenylpentan-1-amine + NAD+ + H2O
mutant F173A, 10 mM, 36% conversion
-
-
?
1-phenylpropan-1-one + NADH + H+ + NH3
(1R)-1-phenylpropan-1-amine + NAD+ + H2O
mutant F173A, 10 mM, 98% conversion, product in R-configuration, 99.9% ee
-
-
?
2,3-dihydro-4H-1-benzopyran-4-one + NADH + H+ + NH3
(4R)-3,4-dihydro-2H-1-benzopyran-4-amine + NAD+ + H2O
mutant F173A, 10 mM, 82% conversion, product in R-configuration, 99.4% ee
-
-
?
3,4-dihydronaphthalen-1(2H)-one + NADH + H+ + NH3
(1R)-1,2,3,4-tetrahydronaphthalen-1-amine + NAD+ + H2O
mutant F173A, 10 mM, 79% conversion, product in R-configuration, 99% ee
-
-
?
4-methylpentan-2-one + NADH + H+ + NH3
(2R)-4-methylpentan-2-amine + NAD+ + H2O
mutant F173A, 10 mM, 76% conversion, product in R-configuration, 97% ee
-
-
?
6-oxoheptanoic acid + NADH + H+ + NH3
(6S)-6-aminoheptanoic acid + NAD+ + H2O
mutant F173A, 10 mM, 99% conversion, product in S-configuration, 99% ee
-
-
?
6-oxohexanoic acid + NADH + H+ + NH3
L-lysine + NAD+ + H2O
mutant F173A, 10 mM, 99% conversion
-
-
?
cyclohexanone + NADH + H+ + NH3
cyclohexanamine + NAD+ + H2O
mutant F173A, 10 mM, 86% conversion
-
-
?
hexan-2-one + NADH + H+ + NH3
(2R)-hexan-2-amine + NAD+ + H2O
mutant F173A, 10 mM, 87% conversion, product in R-configuration, 99% ee
-
-
?
L-lysine + 3-acetylpyridine-NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + 3-acetylpyridine-NADH
L-lysine + deamino-NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + deamino-NADH
L-lysine + NAD(P)+ + H2O
(S)-2-aminoadipate 6-semialdehyde + NAD(P)H + H+ + NH3
L-lysine + NAD+ + H2O
(S)-2-amino-6-oxohexanoate + NADH + H+ + NH3
L-lysine + NAD+ + H2O
2-aminoadipate-6-semialdehyde + NADH + H+ + NH3
-
cyclizes nonenzymatically to DELTA1-piperidine-6-carboxylate
-
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
L-lysine + NADP+
2-aminoadipate-6-semialdehyde + NADPH
22% of activity with NAD+
cyclizes nonenzymatically to DELTA1-piperidine-6-carboxylate
-
?
L-lysine + nicotinamide guanine dinucleotide + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + nicotinamide guanine dinucleotide
-
-
-
?
pentan-2-one + NADH + H+ + NH3
(2R)-pentan-2-amine + NAD+ + H2O
mutant F173A, 10 mM, 86% conversion, product in R-configuration, 89% ee
-
-
?
S-(beta-aminoethyl)-L-cysteine + NAD+
?
additional information
?
-
(S)-2-aminoadipate 6-semialdehyde
(S)-2,3,4,5-tetrahydropiperidine-2-carboxylate + H2O
-
i.e. DELTA1-piperidein-6-carboxylate, spontaneous nonenzymatical reaction, spontaneous reaction
-
?
(S)-2-aminoadipate 6-semialdehyde
(S)-2,3,4,5-tetrahydropiperidine-2-carboxylate + H2O
-
-
spontaneous reaction
-
?
(S)-2-aminoadipate 6-semialdehyde
(S)-2,3,4,5-tetrahydropiperidine-2-carboxylate + H2O
-
i.e. DELTA1-piperidein-6-carboxylate, spontaneous nonenzymatical reaction, spontaneous reaction
-
?
L-lysine + 3-acetylpyridine-NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + 3-acetylpyridine-NADH
-
-
-
?
L-lysine + 3-acetylpyridine-NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + 3-acetylpyridine-NADH
-
-
-
-
?
L-lysine + deamino-NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + deamino-NADH
-
-
-
?
L-lysine + deamino-NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + deamino-NADH
-
-
-
-
?
L-lysine + NAD(P)+ + H2O
(S)-2-aminoadipate 6-semialdehyde + NAD(P)H + H+ + NH3
-
-
-
?
L-lysine + NAD(P)+ + H2O
(S)-2-aminoadipate 6-semialdehyde + NAD(P)H + H+ + NH3
-
-
-
?
L-lysine + NAD+ + H2O
(S)-2-amino-6-oxohexanoate + NADH + H+ + NH3
-
-
-
-
?
L-lysine + NAD+ + H2O
(S)-2-amino-6-oxohexanoate + NADH + H+ + NH3
-
-
-
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
-
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
reaction A-stereospecific
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
reaction A-stereospecific
product is spontaneosly converted into delta1-piperideine-6-carboxylate
ir
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
no activity with D-lysine
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
function in lysine catabolism
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
function in lysine catabolism
product is spontaneosly converted into delta1-piperideine-6-carboxylate
ir
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
involved in biosynthesis of piperidine nucleus of alkaloids
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
S-(beta-aminoethyl)-L-cysteine + NAD+
?
-
3% of the activity with L-lysine
-
-
?
S-(beta-aminoethyl)-L-cysteine + NAD+
?
11% of activity with L-lysine
-
-
?
additional information
?
-
the alpha-carboxyl group is crucial for productive substrate binding and amination. No substrates: hexanal, heptanal, 2-heptanone, 2-octanone, acetophenone and alpha-chromanone
-
-
-
additional information
?
-
active site structure, overview
-
-
?
additional information
?
-
-
active site structure, overview
-
-
?
additional information
?
-
the enzyme catalyzes the reductive deamination of the epsilon-amino group and acts as a type of NAD+-dependent amine dehydrogenase producing DELTA1-piperideine-6-carboxylate
-
-
?
additional information
?
-
-
the enzyme catalyzes the reductive deamination of the epsilon-amino group and acts as a type of NAD+-dependent amine dehydrogenase producing DELTA1-piperideine-6-carboxylate
-
-
?
additional information
?
-
active site structure, overview
-
-
?
additional information
?
-
the enzyme catalyzes the reductive deamination of the epsilon-amino group and acts as a type of NAD+-dependent amine dehydrogenase producing DELTA1-piperideine-6-carboxylate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
(S)-2-aminoadipate 6-semialdehyde
(S)-2,3,4,5-tetrahydropiperidine-2-carboxylate + H2O
L-lysine + NAD(P)+ + H2O
(S)-2-aminoadipate 6-semialdehyde + NAD(P)H + H+ + NH3
L-lysine + NAD+ + H2O
(S)-2-amino-6-oxohexanoate + NADH + H+ + NH3
L-lysine + NAD+ + H2O
2-aminoadipate-6-semialdehyde + NADH + H+ + NH3
-
cyclizes nonenzymatically to DELTA1-piperidine-6-carboxylate
-
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
additional information
?
-
(S)-2-aminoadipate 6-semialdehyde
(S)-2,3,4,5-tetrahydropiperidine-2-carboxylate + H2O
-
i.e. DELTA1-piperidein-6-carboxylate, spontaneous nonenzymatical reaction
-
?
(S)-2-aminoadipate 6-semialdehyde
(S)-2,3,4,5-tetrahydropiperidine-2-carboxylate + H2O
-
i.e. DELTA1-piperidein-6-carboxylate, spontaneous nonenzymatical reaction
-
?
L-lysine + NAD(P)+ + H2O
(S)-2-aminoadipate 6-semialdehyde + NAD(P)H + H+ + NH3
-
-
-
?
L-lysine + NAD(P)+ + H2O
(S)-2-aminoadipate 6-semialdehyde + NAD(P)H + H+ + NH3
-
-
-
?
L-lysine + NAD+ + H2O
(S)-2-amino-6-oxohexanoate + NADH + H+ + NH3
-
-
-
-
?
L-lysine + NAD+ + H2O
(S)-2-amino-6-oxohexanoate + NADH + H+ + NH3
-
-
-
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
function in lysine catabolism
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
function in lysine catabolism
product is spontaneosly converted into delta1-piperideine-6-carboxylate
ir
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
involved in biosynthesis of piperidine nucleus of alkaloids
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
additional information
?
-
the enzyme catalyzes the reductive deamination of the epsilon-amino group and acts as a type of NAD+-dependent amine dehydrogenase producing DELTA1-piperideine-6-carboxylate
-
-
?
additional information
?
-
-
the enzyme catalyzes the reductive deamination of the epsilon-amino group and acts as a type of NAD+-dependent amine dehydrogenase producing DELTA1-piperideine-6-carboxylate
-
-
?
additional information
?
-
the enzyme catalyzes the reductive deamination of the epsilon-amino group and acts as a type of NAD+-dependent amine dehydrogenase producing DELTA1-piperideine-6-carboxylate
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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?
x * 42239, deduced from nucleotide sequence
hexamer
6 * 40000 Da, gel filtration, enzyme elutes as a hexamer when a high concentration of L-lysine (10 mM) is supplemented to both the enzyme and the elution buffer
homodimer
2 * 40000 Da, gel filtration
tetramer
-
gel filtration and centrifugation in presence of L-lysine
dimer
-
2 * 39000, gel filtration, SDS-PAGE
dimer
-
after preincubation with NAD+ without L-lysine
dimer
2 * 42600, recombinant enzyme, SDS-PAGE, 2 * 42089, amino acid sequence
dimer
-
2 * 42600, recombinant enzyme, SDS-PAGE, 2 * 42089, amino acid sequence
-
additional information
each monomer consists of a Rossmann fold domain and a C-terminal catalytic domain, and the fold of the catalytic domain showed similarity to that of saccharopine reductase, three-dimensional structure of the enzyme, structure comparisons, overview. Subunit A active site contains a sulfate ion not seen in subunit B. Consequently, subunit A adopts a closed conformation, whereas subunit B adopts an open one. In each subunit, one NAD molecule was bound to the active site in an anti-conformation, indicating that the enzyme makes use of pro-R-specific hydride transfer between the two hydrides at C-4 of NADH with type A specificity
additional information
-
each monomer consists of a Rossmann fold domain and a C-terminal catalytic domain, and the fold of the catalytic domain showed similarity to that of saccharopine reductase, three-dimensional structure of the enzyme, structure comparisons, overview. Subunit A active site contains a sulfate ion not seen in subunit B. Consequently, subunit A adopts a closed conformation, whereas subunit B adopts an open one. In each subunit, one NAD molecule was bound to the active site in an anti-conformation, indicating that the enzyme makes use of pro-R-specific hydride transfer between the two hydrides at C-4 of NADH with type A specificity
additional information
-
each monomer consists of a Rossmann fold domain and a C-terminal catalytic domain, and the fold of the catalytic domain showed similarity to that of saccharopine reductase, three-dimensional structure of the enzyme, structure comparisons, overview. Subunit A active site contains a sulfate ion not seen in subunit B. Consequently, subunit A adopts a closed conformation, whereas subunit B adopts an open one. In each subunit, one NAD molecule was bound to the active site in an anti-conformation, indicating that the enzyme makes use of pro-R-specific hydride transfer between the two hydrides at C-4 of NADH with type A specificity
-
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Misono, H.; Nagasaki, S.
Occurrence of L-lysine epsilon-dehydrogenase in Agrobacterium tumefaciens
J. Bacteriol.
150
398-401
1982
Agrobacterium tumefaciens
brenda
Misono, H.; Nagasaki, S.
Distribution and physiological function of L-lysine epsilon-dehydrogenase
Agric. Biol. Chem.
47
631-633
1983
Agrobacterium tumefaciens, Alcaligenes faecalis, Sinomonas atrocyanea, Lysinibacillus sphaericus, Corynebacterium ammoniagenes, Corynebacterium pseudodiphtheriticum, Hafnia alvei, Klebsiella pneumoniae, Micrococcus sp., Morganella morganii, no activity in Bos taurus, no activity in yeast, Pseudomonas fragi
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brenda
Misono, H.; Uehigashi, H.; Morimoto, E.; Nagasaki, S.
Purification and properties of L-lysine epsilon-deydrogenase from Agrobacterium tumefaciens
Agric. Biol. Chem.
49
2253-2255
1985
Agrobacterium tumefaciens
brenda
Esbolsev, E.O.; Klyschev, L.K.; Frantsev, A.P.
The enzymatic properties of biosythesis of piperidine nucleus of alkaloids from lysine
F. E. C. S. (Int. Conf. Chem. Biotechnol. Biol. Act. Nat. Prod. , 3rd. , Meeting Date 1985) VCH Weinheim
5
60-64
1987
Anabasis aphylla
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brenda
Hashimoto, H.; Misono, H.; Nagata, S.; Nagasaki, S.
Stereospecificity of hydrogen transfer of the coenzyme catalyzed by L-lysine epsilon-dehydrogenase
Agric. Biol. Chem.
53
1175-1176
1989
Agrobacterium tumefaciens
-
brenda
Misono, H.; Hashimoto, H.; Uehigashi, H.; Nagata, S.; Nagasaki, S.
Properties of L-lysine epsilon-dehydrogenase from Agrobacterium tumefaciens
J. Biochem.
105
1002-1008
1989
Agrobacterium tumefaciens
brenda
Hashimoto, H.; Misono, H.; Nagata, S.; Nagasaki, S.
Activation of L-lysine epsilon-dehydrogenase from Agrobacterium tumefaciens by several amino acids and monocarboxylates
J. Biochem.
106
76-80
1989
Agrobacterium tumefaciens
brenda
Hashimoto, H.; Misono, H.; Nagata, S.; Nagasaki, S.
Selective determination of L-lysine with L-lysine epsilon dehydrogenase
Agric. Biol. Chem.
54
291-294
1990
Agrobacterium tumefaciens
brenda
Misono, H.; Yoshimura, T.; Nagasaki, S.; Soda, K.
Stereospecific abstraction of epsilon-pro-R-hydrogen of L-lysine by L-lysine epsilon-dehydrogenase from Agrobacterium tumefaciens
J. Biochem.
107
169-172
1990
Agrobacterium tumefaciens
brenda
Heydari, M.; Ohshima, T.; Nunoura-Kominato, N.; Sakuraba, H.
Highly stable L-lysine 6-dehydrogenase from the thermophile Geobacillus stearothermophilus isolated from a Japanese hot spring: characterization, gene cloning and sequencing, and expression
Appl. Environ. Microbiol.
70
937-942
2004
Geobacillus stearothermophilus (Q9AJC6), Geobacillus stearothermophilus
brenda
Ruldeekulthamrong, P.; Maeda, S.; Kato, S.; Shinji, N.; Sittipraneed, S.; Packdibamrung, K.; Misono, H.
Molecular characterization of lysine 6-dehydrogenase from Achromobacter denitrificans
BMB Rep.
41
790-795
2008
Achromobacter denitrificans (Q3S559), Achromobacter denitrificans
brenda
Yoneda, K.; Fukuda, J.; Sakuraba, H.; Ohshima, T.
First crystal structure of L-lysine 6-dehydrogenase as an NAD-dependent amine dehydrogenase
J. Biol. Chem.
285
8444-8453
2010
Pyrococcus horikoshii (O59312), Pyrococcus horikoshii, Pyrococcus horikoshii ATCC 700860 (O59312)
brenda
Perez-Garcia, F.; Peters-Wendisch, P.; Wendisch, V.F.
Engineering Corynebacterium glutamicum for fast production of L-lysine and L-pipecolic acid
Appl. Microbiol. Biotechnol.
100
8075-8090
2016
Ruegeria pomeroyi
brenda
Perez-Garcia, F.; Max Risse, J.; Friehs, K.; Wendisch, V.F.
Fermentative production of L-pipecolic acid from glucose and alternative carbon sources
Biotechnol. J.
12
7-7
2017
Ruegeria pomeroyi (Q5LX24), Ruegeria pomeroyi
brenda
Tseliou, V.; Knaus, T.; Masman, M.F.; Corrado, M.L.; Mutti, F.G.
Generation of amine dehydrogenases with increased catalytic performance and substrate scope from epsilon-deaminating L-Lysine dehydrogenase
Nat. Commun.
10
3717
2019
Geobacillus stearothermophilus (Q9AJC6)
brenda