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Information on EC 1.4.1.18 - lysine 6-dehydrogenase
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1.4.1.18 lysine 6-dehydrogenaseIUBMB Comments
The enzyme is highly specific for L-lysine as substrate, although S-(2-aminoethyl)-L-cysteine can act as a substrate, but more slowly. While the enzyme from Agrobacterium tumefaciens can use only NAD+, that from the thermophilic bacterium Geobacillus stearothermophilus can also use NADP+, but more slowly [1,4].
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Word Map
- 1.4.1.18
-
deamination
- tumefaciens
-
agrobacterium
- saccharopine
- glutamicum
-
nad-dependent
-
pyrroline
-
silicibacter
- pomeroyi
- tetramer
-
alkaloid
- albicans
-
l-pipecolic
-
non-proteinogenic
-
5-carboxylate
-
corynebacterium
- analysis
The expected taxonomic range for this enzyme is: Bacteria, Archaea, Eukaryota
Synonyms
L-lysine 6-dehydrogenase, L-lysine 6-dehydrogenase (deaminating), L-lysine epsilon-dehydrogenase, Lys 6-DH, LysDH, lysine 6-dehydrogenase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
L-lysine 6-dehydrogenase
L-lysine 6-dehydrogenase (deaminating)
LysDH
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-lysine + NAD+ + H2O = (S)-2-amino-6-oxohexanoate + NADH + H+ + NH3
-
-
-
-
L-lysine + NAD+ + H2O = (S)-2-amino-6-oxohexanoate + NADH + H+ + NH3
reaction mechanism, overview
L-lysine + NAD+ + H2O = (S)-2-amino-6-oxohexanoate + NADH + H+ + NH3
reaction mechanism, overview
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
L-lysine:NAD+ 6-oxidoreductase (deaminating)
The enzyme is highly specific for L-lysine as substrate, although S-(2-aminoethyl)-L-cysteine can act as a substrate, but more slowly. While the enzyme from Agrobacterium tumefaciens can use only NAD+, that from the thermophilic bacterium Geobacillus stearothermophilus can also use NADP+, but more slowly [1,4].
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CAS REGISTRY NUMBER
COMMENTARY
89400-30-6
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-lysine + 3-acetylpyridine-NAD+ + H2O
alpha-aminoadipate delta-semialdehyde + NH3 + 3-acetylpyridine-NADH
L-lysine + NAD+ + H2O
2-aminoadipate-6-semialdehyde + NADH + H+ + NH3
-
cyclizes nonenzymatically to DELTA1-piperidine-6-carboxylate
-
?
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
-
-
-
?
(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
?
-
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
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-lysine + NAD+ + H2O
2-aminoadipate-6-semialdehyde + NADH + H+ + NH3
-
cyclizes nonenzymatically to DELTA1-piperidine-6-carboxylate
-
?
(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
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
NAD+
preferred cofactor, binding structure, overview. 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
both NAD+ and NADP+ are able to serve as the coenzyme for Pyrococcus horikoshii LysDH, although the reaction rate with NADP+ is only 7.8% of that with NAD+, when L-lysine is the substrate
-
additional information
-
both NAD+ and NADP+ are able to serve as the coenzyme for Pyrococcus horikoshii LysDH, although the reaction rate with NADP+ is only 7.8% of that with NAD+, when L-lysine is the substrate
-
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
6-amino-n-caproate
inhibition 20% by 10 mM 6-amino-n-caproate
DTNB
-
almost complete inhibition in presence of NAD+, 40% inhibition in presence of L-lysine
N-ethylmaleimide
-
complete inhibition at 1 mM after 10 min incubation
p-chloromercuribenzoate
-
complete inhibition at 0.01 mM after 10 min incubation, reversible with 2-mercaptoethanol or dithiothreitol
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Dehydration
Fermentative production of L-pipecolic acid from glucose and alternative carbon sources.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10
9.7
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7 - 10.8
approx. 35% of maximal activity at pH 7.0, approx. 50% of maximal activity at pH 10.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50 - 95
maximum activity at about 95°C and an extraordinary drop off in activity with reduction in temperature, the activity at 50°C is only about 1/170th of that at 95°C
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Aerobacter aerogenes ICR 0220 and IFO 12059, traces of activity with strain IFO 3319
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Show AA Sequence and Transmembrane Helices (250 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
42089
2 * 42600, recombinant enzyme, SDS-PAGE, 2 * 42089, amino acid sequence
42600
2 * 42600, recombinant enzyme, SDS-PAGE, 2 * 42089, amino acid sequence
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
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
tetramer
-
gel filtration and centrifugation in presence of L-lysine
additional information
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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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme complexed with NAD+ and a sulfate ion, sitting drop vapor diffusion method, 0.001 ml of 10 mg/ml protein in 100 mM citrate, pH 5.8, 2.1 M ammonium sulfate, and 1 mM NAD+, is mixed with 0.001 ml of reservoir solution, 20°C, X-ray diffraction structure determination and analysis at 2.44 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 12
the purified recombinant enzyme is stable over a wide range of pH values, losing no activity when incubated at pH values between 5.0 and 12 for 30 min at 50°C, most stable at pH 10.0
712491
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
100
purified recombinant enzyme, half-life is 180 min, the enzyme is highly thermostable and retaining full activity even after incubation for 50 min at 100°C at pH 7.5
30
at 30°C enzyme activity is kept for 3 days and 70% of the activity remains after 7 days
50
65
approx. 25% loss of activity after 10 min at pH 7.2 in the absence of 5 mM lysine, no loss of activity in the presence of 5 mM lysine
50
enzyme is stable up to 50°C when heated for 10 min in KP buffer (pH 7.4)
50
-
stable for 10 min in presence of L-lysine, unstable above 50°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme is purified approximately 100fold to homogeneity with a 15% yield
native LysDH, SuperQ-Toyopearl, Red-Sepharose, Gigapite, Cellulofine, recombinant LysDH, Red-Sepharose
refolded recombinant His-tagged wild-type and mutant LysDHs from Escherichia coli strain Rosettagami (DE3) by gel filtration and nickel affinity chromatography
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression of His-tagged wild-type and mutant LysDHs in Escherichia coli strain Rosettagami (DE3)
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
His-tagged wild-type and mutant LysDHs after recombinant expression in Escherichia coli inclusion bodies are suspended in 20 mM Tris-HCl, pH 7.5, containing 5 mM 2-mercaptoethanol and 4% Triton X-100, and disrupted by sonication, followed by solubilization in 50 mM Tris-HCl, pH 7.5, containing 5 mM 2-mercaptoethanol, 6 M guanidine HCl, 0.2 M NaCl, and 1 mM EDTA. Refolding in buffer containing 0.1 M Tris-HCl, pH 7.5, 5 mM 2-mercaptoethanol, 0.4 M arginine, 2 mM EDTA, and 0.1 mM phenylmethylsulfonyl fluoride and incubation for 36 h at 4°C. Refolded LysDH is heated at 80°C for 10 min and clarified by centrifugation
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
highly specific determination of L-lysine concentration in serum
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
-
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
-
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
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