4.1.1.18: lysine decarboxylase
This is an abbreviated version!
For detailed information about lysine decarboxylase, go to the full flat file.
Word Map on EC 4.1.1.18
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4.1.1.18
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ornithine
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urease
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aeromonas
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dihydrolase
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decarboxylases
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voges-proskauer
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dna-dna
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esculin
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non-motile
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cadba
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salicin
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1,5-diaminopentane
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d-mannitol
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melibiose
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dulcitol
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ruminantium
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adonitol
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selenomonas
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sobria
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enteroinvasive
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d-sorbitol
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carbenicillin
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cephalothin
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corrodens
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simmons
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alvei
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macconkey
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quinolizidine
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hafnia
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eikenella
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huperzia
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d-arabitol
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4.1.1.17
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synthesis
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medicine
- 4.1.1.18
- ornithine
- urease
- aeromonas
-
dihydrolase
- decarboxylases
-
voges-proskauer
-
dna-dna
- esculin
-
non-motile
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cadba
- salicin
- 1,5-diaminopentane
- d-mannitol
- melibiose
- dulcitol
- ruminantium
- adonitol
-
selenomonas
- sobria
-
enteroinvasive
- d-sorbitol
- carbenicillin
- cephalothin
- corrodens
-
simmons
- alvei
-
macconkey
-
quinolizidine
-
hafnia
- eikenella
- huperzia
- d-arabitol
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4.1.1.17
- synthesis
- medicine
Reaction
Synonyms
AsLdc, CadA, constitutive LDCc, constitutive lysine decarboxylase, DesA, EcLDCc, ECORLD, gtLDC, inducible lysine decarboxylase, L-Lys-OD, L-lysine decarboxylase, LDC, ldcC, LdcI, LdcI/CadA, LysA, lysine decarboxylase, MaLDC, multimeric lysine decarboxylase, SrLDC, VSAL_I2491
ECTree
4.1.1.18 lysine decarboxylaseAdvanced search results
results (
results (Substrates Products
Substrates Products on EC 4.1.1.18 - lysine decarboxylase
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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
delta-Hydroxylysine
1,5-Diamino-2-hydroxypentane + CO2
Bacterium cadaveris
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at 35% of the activity with L-Lys
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-
?
delta-Hydroxylysine
1,5-Diamino-2-hydroxypentane + CO2
-
25% of the activity with L-Lys
-
-
?
delta-Hydroxylysine
1,5-Diamino-2-hydroxypentane + CO2
Escherichia coli B / ATCC 11303
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25% of the activity with L-Lys
-
-
?
delta-Hydroxylysine
1,5-Diamino-2-hydroxypentane + CO2
-
17% of the activity with L-Lys
-
-
?
delta-Hydroxylysine
1,5-Diamino-2-hydroxypentane + CO2
-
17% of the activity with L-Lys
-
-
?
L-2,4-diaminobutanoate
1,3-diaminopropane + CO2
-
-
-
?
L-Lys
?
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enzyme activity is positively correlated with the chlorophyll content during leaf regreening. The enzyme is an integrated part of the alkaloid specific biosynthetic sequence
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
-
?
L-Lys
Cadaverine + CO2
constitutive enzyme is involved in synthesis of cadaverine, which is an essential constituent of the peptidoglycan for normal cell growth
-
-
?
L-Lys
Cadaverine + CO2
-
the ratio of activity with L-Orn to activity with L-Lys is 0.69 in wild type enzyme, 1.0 in mutant enzyme A44V/G45T/V46P, 4.0 in mutant enzyme M50V/A52C/P54D/T55S, 0.64 in mutant enzyme M50V, 1.2 in mutant enzyme A52C, 1.8 in mutant enzyme P54D, 0.66 in mutant enzyme T55S, 1.9 in mutant enzyme M50V/A52C, 1.8 in mutant enzyme P54D/T55S, 2.6 in mutant enzyme A52C/P54D, 2.4 in mutant enzyme M50V/A52C/P54D and 2.7 in mutant enzyme A52C/P54D/T55S
-
-
?
L-Lys
Cadaverine + CO2
the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 0.83 for the wild-type enzyme
-
-
?
L-lysine
1,5-diaminopentane + CO2
best substrate
-
-
?
L-lysine
cadaverine + CO2
100% conversion by the recombinant enzyme at pH 7.5
-
-
?
L-lysine
cadaverine + CO2
-
enzyme is a bifunctional L-lysine oxidase/decarboxylase, the decarboxylation reaction takes place 150 times faster than the oxidation reaction
-
-
?
L-lysine
cadaverine + CO2
-
enzyme is a bifunctional L-lysine oxidase/decarboxylase, the decarboxylation reaction takes place 150 times faster than the oxidation reaction
-
-
?
L-lysine
cadaverine + CO2
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CadA protects Escherichia coli starved of phosphate against fermentation acids in the host gut, the tolerance of the starved cells to fermentation acids is markedly increased as a result of the activity of the inducible CadBA lysine-dependent acid resistance system, independent of expression of the RpoS regulon, overview
-
-
?
L-lysine
cadaverine + CO2
optimal at 0.25 M lysine
-
-
?
L-lysine
cadaverine + CO2
Klebsiella aerogenes ATCC 13048 / DSM 30053 / JCM 1235 / KCTC 2190 / NBRC 13534 / NCIMB 10102 / NCTC 10006
-
-
-
?
L-lysine
cadaverine + CO2
Klebsiella aerogenes ATCC 13048 / DSM 30053 / JCM 1235 / KCTC 2190 / NBRC 13534 / NCIMB 10102 / NCTC 10006
optimal at 0.25 M lysine
-
-
?
L-lysine
cadaverine + CO2
Klebsiella oxytoca ATCC 8724 / DSM 4798 / JCM 20051 / NBRC 3318 / NRRL B-199 / KCTC 1686
-
-
-
?
L-Orn
Putrescine + CO2
-
the ratio of activity with L-Orn to activity with L-Lys is 0.69 in wild type enzyme, 1.0 in mutant enzyme A44V/G45T/V46P, 4.o in mutant enzyme M50V/A52C/P54D/T55S, 0.64 in mutant enzyme M50V, 1.2 in mutant enzyme A52C, 1.8 in mutant enzyme P54D, 0.66 in mutant enzyme T55S, 1.9 in mutant enzyme M50V/A52C, 1.8 in mutant enzyme P54D/T55S, 2.6 in mutant enzyme A52C/P54D, 2.4 in mutant enzyme M50V/A52C/P54D and 2.7 in mutant enzyme A52C/P54D/T55S
-
-
?
S-Aminoethyl-L-Cys
1-Amino-2-(S-aminoethyl)mercaptoethane + CO2
Bacterium cadaveris
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at 49% of the activity with L-Lys
-
-
?
S-Aminoethyl-L-Cys
1-Amino-2-(S-aminoethyl)mercaptoethane + CO2
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15% of the activity with L-Lys
-
-
?
S-Aminoethyl-L-Cys
1-Amino-2-(S-aminoethyl)mercaptoethane + CO2
Escherichia coli B / ATCC 11303
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15% of the activity with L-Lys
-
-
?
S-Aminoethyl-L-Cys
1-Amino-2-(S-aminoethyl)mercaptoethane + CO2
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23% of the activity with L-Lys
-
-
?
S-Aminoethyl-L-Cys
1-Amino-2-(S-aminoethyl)mercaptoethane + CO2
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23% of the activity with L-Lys
-
-
?
additional information
?
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when used for whole-cell biotransformation of L-lysine to cadaverine at pH 7.5, 37°C, recombinant AsLdc in Escherichia coli cells completes the transformation within 7 h
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-
?
additional information
?
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evaluation of a simple assay method, a colorimetric assay with pH indicator, applied for monitoring and quantifying the liquid-based enzyme reaction in biotransformation of decarboxylase in a high-throughput way, modification of a pH indicator-based assay on solid agar medium
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-
?
additional information
?
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optimization of direct lysine decarboxylase biotransformation of lysine to cadaverine for cadaverine production with whole-cell biocatalysts at high lysine concentration. Consumption of 91% lysine and conversion of about 80% lysine to cadaverine at 0.025 mM pyridoxal 5'-phosphate and 1.75 M lysine in 500 mM sodium acetate buffer, pH 6.0
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-
?
additional information
?
-
-
optimization of direct lysine decarboxylase biotransformation of lysine to cadaverine for cadaverine production with whole-cell biocatalysts at high lysine concentration. Consumption of 91% lysine and conversion of about 80% lysine to cadaverine at 0.025 mM pyridoxal 5'-phosphate and 1.75 M lysine in 500 mM sodium acetate buffer, pH 6.0
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-
?
additional information
?
-
the cofactor pyridoxal 5'-phosphate-dependent decarboxylation of the amino acid into a polyamine is catalysed in a multistep reaction that consumes a cytoplasmic proton and produces a CO2 molecule passively diffusing out of the cell, while the polyamine is excreted by the antiporter in exchange for a new amino acid substrate
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-
?
additional information
?
-
the cofactor pyridoxal 5'-phosphate-dependent decarboxylation of the amino acid into a polyamine is catalysed in a multistep reaction that consumes a cytoplasmic proton and produces a CO2 molecule passively diffusing out of the cell, while the polyamine is excreted by the antiporter in exchange for a new amino acid substrate
-
-
?
additional information
?
-
-
the cofactor pyridoxal 5'-phosphate-dependent decarboxylation of the amino acid into a polyamine is catalysed in a multistep reaction that consumes a cytoplasmic proton and produces a CO2 molecule passively diffusing out of the cell, while the polyamine is excreted by the antiporter in exchange for a new amino acid substrate
-
-
?
additional information
?
-
evaluation of a simple assay method, a colorimetric assay with pH indicator, applied for monitoring and quantifying the liquid-based enzyme reaction in biotransformation of decarboxylase in a high-throughput way, modification of a pH indicator-based assay on solid agar medium
-
-
?
additional information
?
-
Escherichia coli K-12 / MG1655
optimization of direct lysine decarboxylase biotransformation of lysine to cadaverine for cadaverine production with whole-cell biocatalysts at high lysine concentration. Consumption of 91% lysine and conversion of about 80% lysine to cadaverine at 0.025 mM pyridoxal 5'-phosphate and 1.75 M lysine in 500 mM sodium acetate buffer, pH 6.0
-
-
?
additional information
?
-
Escherichia coli K-12 / MG1655
evaluation of a simple assay method, a colorimetric assay with pH indicator, applied for monitoring and quantifying the liquid-based enzyme reaction in biotransformation of decarboxylase in a high-throughput way, modification of a pH indicator-based assay on solid agar medium
-
-
?
additional information
?
-
whole-cell bioconversion by Klebsiella pneumoniae lysine decaarboxylase LdcC is markedly lower than that of Klebsiella pneumoniae lysine decarboxylase CadA in Klebsiella pneumoniae cells and in transformed Escherichia coli cells
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-
?
additional information
?
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whole-cell bioconversion by Klebsiella pneumoniae lysine decaarboxylase LdcC is markedly lower than that of Klebsiella pneumoniae lysine decarboxylase CadA in Klebsiella pneumoniae cells and in transformed Escherichia coli cells
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-
?
additional information
?
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enzyme CadA is very substrate specific and shows only very low activity with ornithine and no activity with arginine and diaminopimelate
-
-
?
additional information
?
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enzyme CadA is very substrate specific and shows only very low activity with ornithine and no activity with arginine and diaminopimelate
-
-
?
additional information
?
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enzyme LdcC is very substrate specific and shows only very low activity with ornithine and no activity with arginine and diaminopimelate
-
-
?
additional information
?
-
enzyme LdcC is very substrate specific and shows only very low activity with ornithine and no activity with arginine and diaminopimelate
-
-
?
additional information
?
-
evaluation of a simple assay method, a colorimetric assay with pH indicator, applied for monitoring and quantifying the liquid-based enzyme reaction in biotransformation of decarboxylase in a high-throughput way, modification of a pH indicator-based assay on solid agar medium
-
-
?
additional information
?
-
Klebsiella aerogenes ATCC 13048 / DSM 30053 / JCM 1235 / KCTC 2190 / NBRC 13534 / NCIMB 10102 / NCTC 10006
evaluation of a simple assay method, a colorimetric assay with pH indicator, applied for monitoring and quantifying the liquid-based enzyme reaction in biotransformation of decarboxylase in a high-throughput way, modification of a pH indicator-based assay on solid agar medium
-
-
?
additional information
?
-
Klebsiella aerogenes ATCC 13048 / DSM 30053 / JCM 1235 / KCTC 2190 / NBRC 13534 / NCIMB 10102 / NCTC 10006
whole-cell bioconversion by Klebsiella pneumoniae lysine decaarboxylase LdcC is markedly lower than that of Klebsiella pneumoniae lysine decarboxylase CadA in Klebsiella pneumoniae cells and in transformed Escherichia coli cells
-
-
?
additional information
?
-
Klebsiella aerogenes ATCC 13048 / DSM 30053 / JCM 1235 / KCTC 2190 / NBRC 13534 / NCIMB 10102 / NCTC 10006
enzyme LdcC is very substrate specific and shows only very low activity with ornithine and no activity with arginine and diaminopimelate
-
-
?
additional information
?
-
-
no substrates: lysine, 2,4-diaminobutanoate, arginine
-
-
?
additional information
?
-
Ligilactobacillus saerimneri 30a ATCC 33222
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no substrates: lysine, 2,4-diaminobutanoate, arginine
-
-
?
additional information
?
-
substrate and product binding structure and binding mode, overview. A shallow substrate-binding hole is formed at the interface between the sheet domains of two monomers. The epsilon-amino group of the cadaverine product seems to be stabilized by hydroxyl groups of residues Tyr290 and Ser356. Hydrophobic residues such as Tyr298 and Phe360 provide hydrophobicity for the stabilization of five methylene groups of cadaverine. Asp299 also aids the stabilization of hydrophobic parts of cadaverine. Residues Asp324 and Tyr352 are located in the vicinity of the epsilon-amino group of cadaverine
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-
?
additional information
?
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-
substrate and product binding structure and binding mode, overview. A shallow substrate-binding hole is formed at the interface between the sheet domains of two monomers. The epsilon-amino group of the cadaverine product seems to be stabilized by hydroxyl groups of residues Tyr290 and Ser356. Hydrophobic residues such as Tyr298 and Phe360 provide hydrophobicity for the stabilization of five methylene groups of cadaverine. Asp299 also aids the stabilization of hydrophobic parts of cadaverine. Residues Asp324 and Tyr352 are located in the vicinity of the epsilon-amino group of cadaverine
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-
?
