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Information on EC 1.4.1.15 - lysine dehydrogenase
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1.4.1.15 lysine dehydrogenaseSpecify your search results
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
L-lysine epsilon dehydrogenase, LysDH, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-lysine + NAD+ = 1,2-didehydropiperidine-2-carboxylate + NH3 + NADH + H+
the pro-R hydrogen at the prochiral C-6 carbon of L-lysine is specifically abstracted and transferred to the pro-R position at C-4 of NAD+
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L-lysine + NAD+ = 1,2-didehydropiperidine-2-carboxylate + NH3 + NADH + H+
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Deamination
-
-
-
-
oxidation
-
-
-
-
redox reaction
-
-
-
-
reduction
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
L-lysine:NAD+ oxidoreductase (deaminating, cyclizing)
-
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CAS REGISTRY NUMBER
COMMENTARY
68073-29-0
-
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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-glutamate + 3-acetylpyridine-NAD+
L-glutamine + 2-oxoglutarate + 3-acetylpyridine-NADH + H+
-
-
-
-
r
L-glutamate + deamino-NAD+
L-glutamine + 2-oxoglutarate + deamino-NADH + H+
-
-
-
-
r
L-lysine + NAD+
1,2-didehydropiperidine-2-carboxylate + NH3 + NADH
-
-
-
?
L-lysine + NAD+
1,2-didehydropiperidine-2-carboxylate + NH3 + NADH + H+
-
-
-
-
r
additional information
?
-
-
LysDH directly converts L-lysine to alpha-aminoadipic-delta-semialdehyde
-
-
?
4-hydroxylysine + NADP+
alpha-amino-gamma-hydroxyadipate-semialdehyde + NADPH
-
-
-
?
4-hydroxylysine + NADP+
alpha-amino-gamma-hydroxyadipate-semialdehyde + NADPH
-
-
-
?
5-hydroxylysine + NADP+
alpha-amino-delta-hydroxyadipate-semialdehyde + NADPH
-
-
-
?
5-hydroxylysine + NADP+
alpha-amino-delta-hydroxyadipate-semialdehyde + NADPH
-
-
-
?
L-lysine + NAD+ + H2O
1,2-didehydropiperidine-6-carboxylate + NH3 + NADH
-
-
-
?
L-lysine + NAD+ + H2O
1,2-didehydropiperidine-6-carboxylate + NH3 + NADH
-
-
-
?
L-lysine + NAD+ + H2O
1,2-didehydropiperidine-6-carboxylate + NH3 + NADH
-
-
-
?
L-lysine + NAD+ + H2O
1,2-didehydropiperidine-6-carboxylate + NH3 + NADH
-
epsilon amino group is oxidatively deaminated to alpha-aminoadipate delta-semialdehyde, which is spontaneously converted into 1,2-didehydropiperidine-6-carboxylate
-
?
L-lysine + NAD+ + H2O
1,2-didehydropiperidine-6-carboxylate + NH3 + NADH
-
epsilon amino group is oxidatively deaminated to alpha-aminoadipate delta-semialdehyde, which is spontaneously converted into 1,2-didehydropiperidine-6-carboxylate, first step of lysine degradation
-
?
L-lysine + NAD+ + H2O
1,2-didehydropiperidine-6-carboxylate + NH3 + NADH
-
-
-
?
L-lysine + NAD+ + H2O
1,2-didehydropiperidine-6-carboxylate + NH3 + NADH
-
-
-
?
L-lysine + NAD+ + H2O
1,2-didehydropiperidine-6-carboxylate + NH3 + NADH
-
-
-
?
L-lysine + NAD+ + H2O
1,2-didehydropiperidine-6-carboxylate + NH3 + NADH
-
-
-
?
L-lysine + NAD+ + H2O
1,2-didehydropiperidine-6-carboxylate + NH3 + NADH
-
-
-
?
L-lysine + NAD+ + H2O
1,2-didehydropiperidine-6-carboxylate + NH3 + NADH
-
-
-
?
L-lysine + NAD+ + H2O
1,2-didehydropiperidine-6-carboxylate + NH3 + NADH
-
-
-
?
L-lysine + NAD+ + H2O
1,2-didehydropiperidine-6-carboxylate + NH3 + NADH
-
-
-
?
L-lysine + NAD+ + H2O
1,2-didehydropiperidine-6-carboxylate + NH3 + NADH
-
-
-
?
L-lysine + NAD+ + H2O
1,2-didehydropiperidine-6-carboxylate + NH3 + NADH
-
-
-
?
L-lysine + NAD+ + H2O
1,2-didehydropiperidine-6-carboxylate + NH3 + NADH
-
-
-
?
L-lysine + NAD+ + H2O
1,2-didehydropiperidine-6-carboxylate + NH3 + NADH
-
-
-
?
L-lysine + NAD+ + H2O
1,2-didehydropiperidine-6-carboxylate + NH3 + NADH
-
-
-
?
L-lysine + NAD+ + H2O
1,2-didehydropiperidine-6-carboxylate + NH3 + NADH
-
-
-
?
L-lysine + NAD+ + H2O
1,2-didehydropiperidine-6-carboxylate + NH3 + NADH
-
-
-
?
L-lysine + NAD+ + H2O
1,2-didehydropiperidine-6-carboxylate + NH3 + NADH
-
-
-
?
L-lysine + NAD+ + H2O
1,2-didehydropiperidine-6-carboxylate + NH3 + NADH
-
-
-
?
L-lysine + NAD+ + H2O
1,2-didehydropiperidine-6-carboxylate + NH3 + NADH
-
-
-
?
L-lysine + NAD+ + H2O
1,2-didehydropiperidine-6-carboxylate + NH3 + NADH
-
-
-
?
L-lysine + NAD+ + H2O
1,2-didehydropiperidine-6-carboxylate + NH3 + NADH
-
-
-
?
L-lysine + NAD+ + H2O
1,2-didehydropiperidine-6-carboxylate + NH3 + NADH
-
-
-
?
L-lysine + NAD+ + H2O
1,2-didehydropiperidine-6-carboxylate + NH3 + NADH
-
-
-
?
S-(2-aminoethyl)-L-cysteine + NADP+ + H2O
S-(2-oxoethyl)-L-cysteine + NADPH + NH3
-
-
-
?
S-(2-aminoethyl)-L-cysteine + NADP+ + H2O
S-(2-oxoethyl)-L-cysteine + NADPH + NH3
-
-
-
?
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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+
1,2-didehydropiperidine-2-carboxylate + NH3 + NADH
-
-
-
?
L-lysine + NAD+
1,2-didehydropiperidine-2-carboxylate + NH3 + NADH + H+
-
-
-
-
r
L-lysine + NAD+ + H2O
1,2-didehydropiperidine-6-carboxylate + NH3 + NADH
-
epsilon amino group is oxidatively deaminated to alpha-aminoadipate delta-semialdehyde, which is spontaneously converted into 1,2-didehydropiperidine-6-carboxylate, first step of lysine degradation
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5,5-dithiobis(2-nitrobenzoate)
-
0.5 mM, 70% inhibition, 40% inhibition after preincubation with 10 mM L-lysine, 98.5% inhibition after preincubation with 1 mM NAD+
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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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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
11.96 micromol/min*l homogenate, in the presence of cysteine
additional information
-
6.24 micromol/min*l homogenate, in the absence of cysteine
additional information
-
2.70 micromol/min*l homogenate, 3 months old baby girl with congenital lysine intolerance, in the presence of cysteine
additional information
-
0.874 micromol/min*l homogenate, 3 months old baby girl with congenital lysine intolerance, in the absence of cysteine
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
9
-
oxidative deamination of S-(beta-aminoethyl)-cysteine, 5- and 4-hydroxylysine
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strains ICR 1600 and IFO 3058, enzyme is induced by lysin
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
genomic organization and functional role of lysine catabolic pathways among prokaryotes, overview
physiological function
-
the enzyme is part of the lysine-to alpha-aminoadipic-delta-semialdehyde-pathway, that has a broad evolutionary importance in osmotic stress resistance
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 50
-
in the absence of lysine, approx. 50% activity after 10 min at 40°C
30 - 60
-
in the presence of 5 mM L-lysine, approx. 50% activity after 10 min at 55°C
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
gene lysdh is not upregulated under salt stress, in contrast to several other enzymes from the lysine-to-alpha-aminoadipic-delta-semialdehyde pathways, but is upregulated by addition of exogenous lysine
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
-
amperometric biosensor for L-lysine based on immobilized enzyme
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Buergi, W.; Richterich, R.; Colombo, J.P.
L-Lysine dehydrogenase deficiency in a patient with congenital lysine intolerance
Nature
211
854-855
1966
Homo sapiens
brenda
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
Klebsiella aerogenes, Agrobacterium tumefaciens, Alcaligenes faecalis, Sinomonas atrocyanea, Lysinibacillus sphaericus, Corynebacterium ammoniagenes, Corynebacterium pseudodiphtheriticum, Hafnia alvei, Micrococcus flavus, Kocuria rosea, Morganella morganii, no activity in Achromobacter superficialis, no activity in Aerobacter aerogenes, no activity in Arthrobacter tumescens, no activity in Bacillus cereus, no activity in Bacillus licheniformis, no activity in Bacillus megaterium, no activity in Bacillus subtilis, no activity in Bos taurus, no activity in Brevibacterium divaricatum, no activity in Candida albicans, no activity in Yarrowia lipolytica, no activity in Candida tropicalis, no activity in Corynebacterium glutamicum, no activity in Cryptococcus albidus, no activity in Escherichia coli, no activity in Endomycopsis burtonii, no activity in Erwinia aroideae, no activity in Flavobacterium lutescens, no activity in Hansenula anomala, no activity in Hansenula beijerinckii, no activity in Hansenula bimundalis, no activity in Hansenula canadensis, no activity in Debaryomyces hansenii, no activity in Hansenula holstii, no activity in Hansenula mrakii, no activity in Cyberlindnera petersonii, no activity in Hansenula saturnus, no activity in Kluyveromyces lactis, no activity in Oosporidium margaritiferum, no activity in Pseudomonas aeruginosa, no activity in Pichia polymorpha, no activity in Proteus vulgaris, no activity in Pseudomonas aureofaciens, no activity in Pseudomonas dacunhae, no activity in Pseudomonas fluorescens, no activity in Pseudomonas marginalis, no activity in Pseudomonas ovalis, no activity in Rhodotorula glutinis, no activity in Rhodotorula lactosa, no activity in Rhodotorula marina, no activity in Rhodotorula minuta, no activity in Rhodotorula rubra, no activity in Cystobasidium minutum, no activity in Sarcina subflava, no activity in Serratia marcescens, no activity in Staphylococcus aureus, no activity in Candida melibiosi, no activity in Torulopsis candida, no activity in Trichosporon cutaneum, Pseudomonas fragi, no activity in Rhodotorula lactosa IFO 1006, Corynebacterium ammoniagenes IFO 12071, no activity in Bacillus megaterium ICR 1340, no activity in Rhodotorula minuta IFO 0387, Pseudomonas fragi IFO 3458, no activity in Cryptococcus albidus IFO 0410, no activity in Pichia polymorpha IFO 0195, no activity in Erwinia aroideae IFO 3830, no activity in Arthrobacter tumescens IFO 12960, no activity in Hansenula saturnus IFO 0125, Micrococcus flavus ICR 1820, no activity in Cystobasidium minutum IFO 0412, no activity in Pseudomonas dacunhae ICR 3180, Kocuria rosea IFO 3764, no activity in Hansenula beijerinckii IFO 0981, no activity in Flavobacterium lutescens IFO 3014, no activity in Yarrowia lipolytica IFO 1209, no activity in Pseudomonas aeruginosa IFO 3080, Lysinibacillus sphaericus IFO 3525, no activity in Cyberlindnera petersonii IFO 1372, no activity in Proteus vulgaris IFO 3167, no activity in Rhodotorula glutinis IFO 0898, no activity in Bacillus licheniformis IFO 12200, no activity in Serratia marcescens IFO 3046, no activity in Sarcina subflava IFO 11992, no activity in Oosporidium margaritiferum IFO 1208, no activity in Bacillus cereus IFO 3001, no activity in Aerobacter aerogenes IFO 3320, no activity in Candida tropicalis IFO 1401, no activity in Brevibacterium divaricatum ICR 4100, no activity in Hansenula anomala 118, no activity in Pseudomonas aureofaciens IFO 3521, no activity in Hansenula holstii IFO 0980, no activity in Candida melibiosi IFO 0454, no activity in Pseudomonas fluorescens IFO 3081, no activity in Hansenula canadensis IFO 0937, no activity in Pseudomonas ovalis IFO 3738, Sinomonas atrocyanea IFO 12670, no activity in Hansenula mrakii IFO 0895, Alcaligenes faecalis IFO 3160, no activity in Pseudomonas marginalis IFO 3925, Corynebacterium pseudodiphtheriticum ICR 2210, no activity in Debaryomyces hansenii IFO 0794, no activity in Hansenula bimundalis IFO 1366, no activity in Rhodotorula marina IFO 0879, no activity in Kluyveromyces lactis IFO 1090, Morganella morganii IFO 3848, no activity in Achromobacter superficialis ICR 0890, no activity in Staphylococcus aureus IFO 3060, no activity in Bacillus subtilis IFO 3037
-
brenda
Misono, H.
NAD+-dependent lysine dehydrogenase from a plant-pathogenic bacterium, Agrobacterium tumefaciens
Vitamins (Kyoto)
65
1-12
1991
Agrobacterium tumefaciens
-
brenda
Hammer, T.; Bode, R.
Enzymic production of alpha-aminoadipate-delta-semialdehyde and related compounds by lysine epsilon-dehydrogenase from Candida albicans
Zentralbl. Mikrobiol.
147
65-70
1992
Candida albicans, Candida albicans SBUG 182
brenda
Dempsey, E.; Wang, J.; Wollenberger, U.; Ozsoz, M.; Smyth, M.R.
A lysine dehydrogenase-based electrode for biosensing of L-lysine
Biosens. Bioelectron.
7
323-327
1992
Agrobacterium tumefaciens
brenda
Umair, S.; Bland, R.J.; Simpson, H.V.
Lysine catabolism in Haemonchus contortus and Teladorsagia circumcincta
Exp. Parasitol.
131
101-106
2012
no activity in Haemonchus contortus, no activity in Teladorsagia circumcincta
brenda
Neshich, I.A.; Kiyota, E.; Arruda, P.
Genome-wide analysis of lysine catabolism in bacteria reveals new connections with osmotic stress resistance
ISME J.
7
240-2410
2013
Ruegeria pomeroyi
brenda
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