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
-
4.1.1.18
-
ornithine
-
urease
-
aeromonas
-
dihydrolase
-
decarboxylases
-
voges-proskauer
-
dna-dna
-
esculin
-
non-motile
-
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
-
4.1.1.17
-
synthesis
-
medicine
- 4.1.1.18
- ornithine
- urease
- aeromonas
-
dihydrolase
- decarboxylases
-
voges-proskauer
-
dna-dna
- esculin
-
non-motile
-
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
-
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 (Engineering
Engineering on EC 4.1.1.18 - lysine decarboxylase
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
top
PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
F14C/K44C
site-directed mutagenesis, mutant B1, the disulfide bond mutation in the decameric interface of wild-type CadA improves its structural stability, and as a result, enhances the pH and thermal stabilities along with organic solvent tolerance, but reduces the catalytic efficiency, compared to the wild-type
F14C/K44C/L7M/N8G
site-directed mutagenesis, the disulfide bond mutation in the decameric interface of wild-type CadA improves its structural stability, and as a result, enhances the pH and thermal stabilities along with organic solvent tolerance compared to the wild-type, addition of mutations L7M and N8G to mutant B1 slightly increases the catalytic efficiency compared to mutant B1 but remains still lower than wild-type
L89R
the mutant elutes at the expected position for an LdcI dimer (about 150000 Da), the mutant shows about 5fold lower level of activity than wild type and this activity is not inhibited by ppGpp
R206S
the ppGpp-binding site mutant shows wild type oligomerisation profile, the mutant is insensitive to the addition of ppGpp and has activity comparable to wild type LdcI in the absence of ppGpp
R97A
the ppGpp-binding site mutant shows wild type oligomerisation profile, the mutant is insensitive to the addition of ppGpp and has activity comparable to wild type LdcI in the absence of ppGpp
T88D
site-directed mutagenesis, the mutant shows decreased thermostability compared to the wild-type enzyme
T88F
site-directed mutagenesis, the mutant shows increased thermostability compared to the wild-type enzyme
T88N
site-directed mutagenesis, the mutant is expressed in inclusion bodies and shows no clear activity
T88P
site-directed mutagenesis, the mutant is expressed in inclusion bodies and shows no clear activity
T88Q
site-directed mutagenesis, the mutant is expressed in inclusion bodies and shows no clear activity
T88S
site-directed mutagenesis, the mutant shows higher thermostability with a 2.9fold increase in the half-life at 70°C (from 11 min to 32 min) and increased melting temperature (from 76°C to 78°C). The specific activity and pH stability of T88S at pH 8.0 are increased to 164 U/mg and 78% compared to 58 U/mg and 57% for the wild-type enzyme. The productivity of cadaverine with T88S is 40 g/l/h in contrast to 28 g/l/h with wild-type enzyme. The mutant is a promising biocatalyst for industrial production of cadaverine. No additional hydrogen bond is formed when T88 is substituted by D, F, or S, and the improved stability may be attributed to the favorable atom and torsion angle potentials
F14C/K44C
Escherichia coli K-12 / B
-
site-directed mutagenesis, mutant B1, the disulfide bond mutation in the decameric interface of wild-type CadA improves its structural stability, and as a result, enhances the pH and thermal stabilities along with organic solvent tolerance, but reduces the catalytic efficiency, compared to the wild-type
-
F14C/K44C/L7M/N8G
Escherichia coli K-12 / B
-
site-directed mutagenesis, the disulfide bond mutation in the decameric interface of wild-type CadA improves its structural stability, and as a result, enhances the pH and thermal stabilities along with organic solvent tolerance compared to the wild-type, addition of mutations L7M and N8G to mutant B1 slightly increases the catalytic efficiency compared to mutant B1 but remains still lower than wild-type
-
E583G
-
site-directed mutagenesis, the mutant shows 1.32fold increased LDC activity and 1.48fold improved productivity of cadaverine compared to wild-type enzyme
V147F/E583G
-
site-directed mutagenesis, the mutant shows 1.62fold increased LDC activity compared to wild-type enzyme
E583G
Hafnia alvei AS1.1009
-
site-directed mutagenesis, the mutant shows 1.32fold increased LDC activity and 1.48fold improved productivity of cadaverine compared to wild-type enzyme
-
V147F/E583G
Hafnia alvei AS1.1009
-
site-directed mutagenesis, the mutant shows 1.62fold increased LDC activity compared to wild-type enzyme
-
A225C/T302C
site-directed mutagenesis, due to high flexibility at the pyridoxal 5'-phosphate (PLP) binding site, use of the enzyme for cadaverine production requires continuous supplement of large amounts of PLP. In order to develop an LDC enzyme from Selenomonas ruminantium (SrLDC) with an enhanced affinity for PLP, an internal disulfide bond between Ala225 and Thr302 residues is introduced with a desire to retain the PLP binding site in a closed conformation. The SrLDCA225C/T302C mutant shows bound PLP, and exhibits 3fold enhanced PLP affinity compared with the wild-type SrLDC. The mutant also exhibits a dramatically enhanced LDC activity and cadaverine conversion particularly under no or low PLP concentrations. Introduction of the disulfide bond renders mutant SrLDC more resistant to high pH and temperature. The formation of the introduced disulfide bond and the maintenance of the PLP binding site in the closed conformation are confirmed by determination of the crystal structure of the mutant. Mutant structure determination and analysis, overview. The mutant shows increased affinity for pyridoxal 5'-phosphate and increased activity compared to wild-type
A44V/G45T/V46P
A44V/G45T/V46P/P54D
the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 3.8, compared to 0.83 for the wild-type enzyme
A44V/G45T/V46P/P54D/S322A
the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 58, compared to 0.83 for the wild-type enzyme
A44V/G45T/V46P/P54D/S322T/I326L
the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 13, compared to 0.83 for the wild-type enzyme
A52C
A52C/P54D
A52C/P54D/T55S
-
the ratio of activity with L-Orn to activity with L-Lys is 2.7, compared to 0.69 for the wild-type enzyme
G319W
the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 3.9, compared to 0.83 for the wild-type enzyme
K2C/G227C
site-directed mutagenesis, the mutant shows reduced affinity for pyridoxal 5'-phosphate and reduced activity compared to wild-type
M50V
-
the ratio of activity with L-Orn to activity with L-Lys is 0.64, compared to 0.69 for the wild-type enzyme
M50V/A52C
-
the ratio of activity with L-Orn to activity with L-Lys is 1.9, compared to 0.69 for the wild-type enzyme
M50V/A52C/P54D
-
the ratio of activity with L-Orn to activity with L-Lys is 2.4, compared to 0.69 for the wild-type enzyme
M50V/A52C/P54D/T55S
P54D
P54D/T55S
-
the ratio of activity with L-Orn to activity with L-Lys is 1.8, compared to 0.69 for the wild-type enzyme
S322A
the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 24, compared to 0.83 for the wild-type enzyme
S322T/I326L
the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 13, compared to 0.83 for the wild-type enzyme
T55S
-
the ratio of activity with L-Orn to activity with L-Lys is 0.66, compared to 0.69 for the wild-type enzyme
additional information
A44V/G45T/V46P
-
the ratio of activity with L-Orn to activity with L-Lys is 1.0, compared to 0.69 for the wild-type enzyme
A44V/G45T/V46P
the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 2.0, compared to 0.83 for the wild-type enzyme
A52C
-
the ratio of activity with L-Orn to activity with L-Lys is 1.2, compared to 0.69 for the wild-type enzyme
A52C
the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 1.0, compared to 0.83 for the wild-type enzyme
A52C/P54D
-
the ratio of activity with L-Orn to activity with L-Lys is 2.6, compared to 0.69 for the wild-type enzyme
A52C/P54D
the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 1.6, compared to 0.83 for the wild-type enzyme
M50V/A52C/P54D/T55S
-
the ratio of activity with L-Orn to activity with L-Lys is 4.0, compared to 0.69 for the wild-type enzyme
M50V/A52C/P54D/T55S
the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 1.5, compared to 0.83 for the wild-type enzyme
P54D
-
the ratio of activity with L-Orn to activity with L-Lys is 1.8, compared to 0.69 for the wild-type enzyme
P54D
the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 2.2, compared to 0.83 for the wild-type enzyme
additional information
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, method optimiztaion and comprisons, overview
additional information
cadaverine is a major source of many industrial polyamides such as nylon and chelating agents. Cadaverine is produced by the microbial fermentation of glucose to lysine, which is then decarboxylated by lysine decarboxylase CadA. But utilizing CadA for cadaverine production causes enzyme instability. In order to stabilize the CadA homodecamer structure for in vitro decarboxylation reaction, four disulfide bond mutants in the multimeric interfacial region are designed, CadA plasmid library/mutant screening
additional information
development of an innovative immobilisation approach using catalytically active recombinant constitutive L-lysine decarboxylase (EcLDCc) in inclusion bodies, CatIBs, overview. EcLDCc-CatIBs can compete with the whole cell biocatalyst in production of cadaverine
additional information
-
development of an innovative immobilisation approach using catalytically active recombinant constitutive L-lysine decarboxylase (EcLDCc) in inclusion bodies, CatIBs, overview. EcLDCc-CatIBs can compete with the whole cell biocatalyst in production of cadaverine
additional information
engineering the decameric interface for potential for industrial applications
additional information
-
engineering the decameric interface for potential for industrial applications
additional information
immobilization of the recombinant enzyme CadA, preparation of a cross-linked enzyme aggregate (CLEA) of Escherichia coli CadA and bioconversion of lysine using CadACLEA. The thermostability of CadACLEA is significantly higher than that of CadAfree. The optimum temperatures of CadAfree and CadACLEA are 60°C and 55°C, respectively. The thermostability of CadACLEA is significantly higher than that of CadAfree. The optimum pH of both enzymes is 6.0. CadAfree cannot be recovered after use, whereas CadACLEA is rapidly recovered and the residual activity is 53% after the 10th recycle
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
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
additional information
recombinant Escherichia coli-overexpressing CadA produces cadaverine from crude L-lysine solution. Constitutive lysine decarboxylase EcLdcC retains a higher cadaverine yield after being reused 10 times at acidic and alkaline pH values than that of a recombinant Escherichia coli strain overexpressing the inducible lysine carboxylase CadA, the conventional cadaverine producer. Although the soluble expression level of LdcC in Escherichia coli is less than that of CadA, LdcC is active over a broader pH range (pH 5-9) and exhibits less substrate inhibition than CadA, indicating that LdcC is a more suitable biocatalyst than CadA for the direct synthesis of cadaverine from highly concentrated lysine
additional information
recombinant Escherichia coli-overexpressing CadA produces cadaverine from crude L-lysine solution. Constitutive lysine decarboxylase EcLdcC retains a higher cadaverine yield after being reused 10 times at acidic and alkaline pH values than that of a recombinant Escherichia coli strain overexpressing the inducible lysine carboxylase CadA, the conventional cadaverine producer. Although the soluble expression level of LdcC in Escherichia coli is less than that of CadA, LdcC is active over a broader pH range (pH 5-9) and exhibits less substrate inhibition than CadA, indicating that LdcC is a more suitable biocatalyst than CadA for the direct synthesis of cadaverine from highly concentrated lysine
additional information
-
recombinant Escherichia coli-overexpressing CadA produces cadaverine from crude L-lysine solution. Constitutive lysine decarboxylase EcLdcC retains a higher cadaverine yield after being reused 10 times at acidic and alkaline pH values than that of a recombinant Escherichia coli strain overexpressing the inducible lysine carboxylase CadA, the conventional cadaverine producer. Although the soluble expression level of LdcC in Escherichia coli is less than that of CadA, LdcC is active over a broader pH range (pH 5-9) and exhibits less substrate inhibition than CadA, indicating that LdcC is a more suitable biocatalyst than CadA for the direct synthesis of cadaverine from highly concentrated lysine
additional information
recombinant Escherichia coli-overexpressing LdcC (EcLdcC) produces cadaverine from crude L-lysine solution. EcLdcC retains a higher cadaverine yield after being reused 10 times at acidic and alkaline pH values than that of a recombinant Escherichia coli strain overexpressing an inducible lysine carboxylase (CadA), a conventional cadaverine producer. Although the soluble expression level of LdcC in Escherichia coli is less than that of CadA, LdcC is active over a broader pH range (pH 5-9) and exhibits less substrate inhibition than CadA, indicating that LdcC is a more suitable biocatalyst than CadA for the direct synthesis of cadaverine from highly concentrated lysine. Optimization of the EcLdcC-catalyzed whole-cell biotransformation, overview
additional information
recombinant Escherichia coli-overexpressing LdcC (EcLdcC) produces cadaverine from crude L-lysine solution. EcLdcC retains a higher cadaverine yield after being reused 10 times at acidic and alkaline pH values than that of a recombinant Escherichia coli strain overexpressing an inducible lysine carboxylase (CadA), a conventional cadaverine producer. Although the soluble expression level of LdcC in Escherichia coli is less than that of CadA, LdcC is active over a broader pH range (pH 5-9) and exhibits less substrate inhibition than CadA, indicating that LdcC is a more suitable biocatalyst than CadA for the direct synthesis of cadaverine from highly concentrated lysine. Optimization of the EcLdcC-catalyzed whole-cell biotransformation, overview
additional information
-
recombinant Escherichia coli-overexpressing LdcC (EcLdcC) produces cadaverine from crude L-lysine solution. EcLdcC retains a higher cadaverine yield after being reused 10 times at acidic and alkaline pH values than that of a recombinant Escherichia coli strain overexpressing an inducible lysine carboxylase (CadA), a conventional cadaverine producer. Although the soluble expression level of LdcC in Escherichia coli is less than that of CadA, LdcC is active over a broader pH range (pH 5-9) and exhibits less substrate inhibition than CadA, indicating that LdcC is a more suitable biocatalyst than CadA for the direct synthesis of cadaverine from highly concentrated lysine. Optimization of the EcLdcC-catalyzed whole-cell biotransformation, overview
additional information
Escherichia coli K-12 / B
-
cadaverine is a major source of many industrial polyamides such as nylon and chelating agents. Cadaverine is produced by the microbial fermentation of glucose to lysine, which is then decarboxylated by lysine decarboxylase CadA. But utilizing CadA for cadaverine production causes enzyme instability. In order to stabilize the CadA homodecamer structure for in vitro decarboxylation reaction, four disulfide bond mutants in the multimeric interfacial region are designed, CadA plasmid library/mutant screening
-
additional information
Escherichia coli K-12 / MG1655
-
recombinant Escherichia coli-overexpressing CadA produces cadaverine from crude L-lysine solution. Constitutive lysine decarboxylase EcLdcC retains a higher cadaverine yield after being reused 10 times at acidic and alkaline pH values than that of a recombinant Escherichia coli strain overexpressing the inducible lysine carboxylase CadA, the conventional cadaverine producer. Although the soluble expression level of LdcC in Escherichia coli is less than that of CadA, LdcC is active over a broader pH range (pH 5-9) and exhibits less substrate inhibition than CadA, indicating that LdcC is a more suitable biocatalyst than CadA for the direct synthesis of cadaverine from highly concentrated lysine
-
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
-
recombinant Escherichia coli-overexpressing LdcC (EcLdcC) produces cadaverine from crude L-lysine solution. EcLdcC retains a higher cadaverine yield after being reused 10 times at acidic and alkaline pH values than that of a recombinant Escherichia coli strain overexpressing an inducible lysine carboxylase (CadA), a conventional cadaverine producer. Although the soluble expression level of LdcC in Escherichia coli is less than that of CadA, LdcC is active over a broader pH range (pH 5-9) and exhibits less substrate inhibition than CadA, indicating that LdcC is a more suitable biocatalyst than CadA for the direct synthesis of cadaverine from highly concentrated lysine. Optimization of the EcLdcC-catalyzed whole-cell biotransformation, overview
-
additional information
-
directed evolution of LDC and high-throughput mutant screening, mutant library construction using DNA shuffling or error-prone PCR (optimum concentrations of Mn2+ and Mg2+ are 5 and 0.2 mM, respectively). Three nucleotide mutations, A438G, G439T, and A1748G correspond to amino acid changes V147F and E583G
additional information
Hafnia alvei AS1.1009
-
directed evolution of LDC and high-throughput mutant screening, mutant library construction using DNA shuffling or error-prone PCR (optimum concentrations of Mn2+ and Mg2+ are 5 and 0.2 mM, respectively). Three nucleotide mutations, A438G, G439T, and A1748G correspond to amino acid changes V147F and E583G
-
additional information
whole-cell bioconversion by Klebsiella pneumoniae lysine decarboxylase LdcC is markedly lower than that of Klebsiella pneumoniae lysine decaarboxylase CadA in Klebsiella pneumoniae cells and in transformed Escherichia coli cells
additional information
whole-cell bioconversion by Klebsiella pneumoniae lysine decarboxylase LdcC is markedly lower than that of Klebsiella pneumoniae lysine decaarboxylase CadA in Klebsiella pneumoniae cells and in transformed Escherichia coli cells
additional information
whole-cell bioconversion by Klebsiella pneumoniae lysine decarboxylase LdcC is markedly lower than that of Klebsiella pneumoniae lysine decarboxylase CadA in Klebsiella pneumoniae cells and in transformed Escherichia coli cells
additional information
whole-cell bioconversion by Klebsiella pneumoniae lysine decarboxylase 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
-
whole-cell bioconversion by Klebsiella pneumoniae lysine decarboxylase LdcC is markedly lower than that of Klebsiella pneumoniae lysine decarboxylase CadA in Klebsiella pneumoniae cells and in transformed Escherichia coli cells
-
additional information
-
biotransformation of cadaverine using a lysine decarboxylase from Klebsiella oxytoca expressed in Escherichia coli. Codon optimization of the gene encoding the enzyme is carried on for the heterologous expression in Escherichia coli, which leads to a system that converts more than 24% lysine-HCl to cadaverine compared to the same system expressing CadA, overview. The final optimized system converts lysine-HCl to cadaverine at a conversion rate of 0.133%/min/g
additional information
-
identification of mutant Ldc-co with increased lysine decarboxylase ability. Codon optimization of the gene encoding the enzyme is carried on for the heterologous expression in Escherichia coli. Identification of mutant lysine decarboxylase enzymes with enhanced cadaverine-production ability. Together, these modifications increase cadaverine production in the system by 50%, and the system has a yield of 80% from lysine-HCl, the system to produce cadaverine using the lysine decarboxylase from Klebsiella oxytoca performs at a level that is competitive with the traditional systems using the Escherichia coli lysine decarboxylases in both lab-scale and batch fermentation conditions. Generation of several mutant strains and evaluation, overview
additional information
Klebsiella oxytoca DSM 6673
-
biotransformation of cadaverine using a lysine decarboxylase from Klebsiella oxytoca expressed in Escherichia coli. Codon optimization of the gene encoding the enzyme is carried on for the heterologous expression in Escherichia coli, which leads to a system that converts more than 24% lysine-HCl to cadaverine compared to the same system expressing CadA, overview. The final optimized system converts lysine-HCl to cadaverine at a conversion rate of 0.133%/min/g
-
additional information
Klebsiella oxytoca DSM 6673
-
identification of mutant Ldc-co with increased lysine decarboxylase ability. Codon optimization of the gene encoding the enzyme is carried on for the heterologous expression in Escherichia coli. Identification of mutant lysine decarboxylase enzymes with enhanced cadaverine-production ability. Together, these modifications increase cadaverine production in the system by 50%, and the system has a yield of 80% from lysine-HCl, the system to produce cadaverine using the lysine decarboxylase from Klebsiella oxytoca performs at a level that is competitive with the traditional systems using the Escherichia coli lysine decarboxylases in both lab-scale and batch fermentation conditions. Generation of several mutant strains and evaluation, overview
-
additional information
disulfide bond-mediated spatial reconstitution can be a platform technology for development of enzymes with enhanced pyridoxal 5'-phosphate affinity
additional information
-
disulfide bond-mediated spatial reconstitution can be a platform technology for development of enzymes with enhanced pyridoxal 5'-phosphate affinity
additional information
construction of a cadA gene-inactivated strain from wild-type strain V02-64, serotype O3:K, by a plasmid integrated in its chromosome, single crossing over, acid resistance of the mutant strain at pH 4.0 in phosphate buffer is weaker than in the parental strain
additional information
-
construction of a cadA gene-inactivated strain from wild-type strain V02-64, serotype O3:K, by a plasmid integrated in its chromosome, single crossing over, acid resistance of the mutant strain at pH 4.0 in phosphate buffer is weaker than in the parental strain
additional information
-
a lack of cadaverine caused by mutation in cadA results in low tolerance to oxidative stress compared to the wild type, cadaverine, which neutralizes the external medium, also appears to scavenge superoxide radicals, since increasing cellular cadaverine by elevating the gene dosage of cadBA significantly diminished the induction of Mn-containing superoxide dismutase under methyl viologen-induced oxidative stress, overview
