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Enzyme Nomenclature
Information on EC 1.4.1.18 - lysine 6-dehydrogenase
for references in articles please use BRENDA:EC1.4.1.18
Word Map on EC 1.4.1.18
- 1.4.1.18
-
deamination
- tumefaciens
-
agrobacterium
- albicans
-
non-proteinogenic
-
corynebacterium
-
5-carboxylate
-
pyrroline
-
silicibacter
-
nad-dependent
- glutamicum
-
by-product
- pomeroyi
-
l-pipecolic
- analysis
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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EC NUMBER 
COMMENTARY 
1.4.1.18
-
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RECOMMENDED NAME
GeneOntology No.
lysine 6-dehydrogenase
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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
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Aerobacter aerogenes ICR 0220 and IFO 12059, traces of activity with strain IFO 3319
-
-
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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 + 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
-
-
-
?
(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+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
reaction A-stereospecific
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
reaction A-stereospecific
product is spontaneosly converted into delta1-piperideine-6-carboxylate
ir
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
no activity with D-lysine
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
function in lysine catabolism
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
function in lysine catabolism
product is spontaneosly converted into delta1-piperideine-6-carboxylate
ir
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
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+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
(S)-2-amino-6-oxohexanoate + NADH + H+ + NH3
-
-
-
-
?
L-lysine + NAD+ + H2O
(S)-2-amino-6-oxohexanoate + NADH + H+ + NH3
-
-
-
?
S-(beta-aminoethyl)-L-cysteine + NAD+
?
-
3% of the activity with L-lysine
-
-
-
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 SUBSTRATES
NATURAL PRODUCTS
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
Q9AJC6
-
cyclizes nonenzymatically to DELTA1-piperidine-6-carboxylate
-
?
(S)-2-aminoadipate 6-semialdehyde
(S)-2,3,4,5-tetrahydropiperidine-2-carboxylate + H2O
O59312
-
i.e. DELTA1-piperidein-6-carboxylate, spontaneous nonenzymatical reaction
-
?
(S)-2-aminoadipate 6-semialdehyde
(S)-2,3,4,5-tetrahydropiperidine-2-carboxylate + H2O
O59312
-
i.e. DELTA1-piperidein-6-carboxylate, spontaneous nonenzymatical reaction
-
?
L-lysine + NAD(P)+ + H2O
(S)-2-aminoadipate 6-semialdehyde + NAD(P)H + H+ + NH3
O59312
-
-
-
?
L-lysine + NAD(P)+ + H2O
(S)-2-aminoadipate 6-semialdehyde + NAD(P)H + H+ + NH3
O59312
-
-
-
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
function in lysine catabolism
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
function in lysine catabolism
product is spontaneosly converted into delta1-piperideine-6-carboxylate
ir
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
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+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+
alpha-aminoadipate delta-semialdehyde + NH3 + NADH
-
-
product is spontaneosly converted into delta1-piperideine-6-carboxylate
?
L-lysine + NAD+ + H2O
(S)-2-amino-6-oxohexanoate + NADH + H+ + NH3
-
-
-
-
?
L-lysine + NAD+ + H2O
(S)-2-amino-6-oxohexanoate + NADH + H+ + NH3
Q5LX24
-
-
-
?
additional information
?
-
O59312
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
?
-
O59312
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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INHIBITORS
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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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
9.7
10
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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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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
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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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SUBUNITS
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
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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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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
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
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
50
enzyme is stable up to 50°C when heated for 10 min in KP buffer (pH 7.4)
50
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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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
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highly specific determination of L-lysine concentration in serum
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LINKS TO OTHER DATABASES (specific for EC-Number 1.4.1.18)
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