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delta-Hydroxylysine
1,5-Diamino-2-hydroxypentane + CO2
L-2,4-diaminobutanoate
1,3-diaminopropane + CO2
L-lysine
1,5-diaminopentane + CO2
L-lysine
cadaverine + CO2
L-ornithine
1,4-diaminobutane + CO2
S-Aminoethyl-L-Cys
1-Amino-2-(S-aminoethyl)mercaptoethane + CO2
additional information
?
-
delta-Hydroxylysine
1,5-Diamino-2-hydroxypentane + CO2
Bacterium cadaveris
-
at 35% of the activity with L-Lys
-
-
?
delta-Hydroxylysine
1,5-Diamino-2-hydroxypentane + CO2
-
25% of the activity with L-Lys
-
-
?
delta-Hydroxylysine
1,5-Diamino-2-hydroxypentane + CO2
-
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-2,4-diaminobutanoate
1,3-diaminopropane + CO2
-
-
-
?
L-Lys
?
-
inducible enzyme
-
-
?
L-Lys
?
-
inducible enzyme
-
-
?
L-Lys
?
-
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
?
-
the enzyme is produced constitutively
-
-
?
L-Lys
?
-
inducible enzyme
-
-
?
L-Lys
?
-
inducible enzyme
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
Bacterium cadaveris
-
-
-
?
L-Lys
Cadaverine + CO2
Bacterium cadaveris
-
-
-
?
L-Lys
Cadaverine + CO2
Bacterium cadaveris
-
-
-
?
L-Lys
Cadaverine + CO2
Bacterium cadaveris
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
Cytisus beanii
-
-
-
?
L-Lys
Cadaverine + CO2
Cytisus canariensis
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
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-Lys
Cadaverine + CO2
Senecio fuchsii
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
Valeriana excelsa subsp. sambucifolia
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
?
L-lysine
1,5-diaminopentane + CO2
best substrate
-
-
?
L-lysine
1,5-diaminopentane + CO2
best substrate
-
-
?
L-lysine
cadaverine + CO2
-
-
-
?
L-lysine
cadaverine + CO2
100% conversion by the recombinant enzyme at pH 7.5
-
-
?
L-lysine
cadaverine + CO2
Bacterium cadaveris
-
-
-
-
?
L-lysine
cadaverine + CO2
Bacterium cadaveris
-
-
cadaverine is 1,5-pentanediamine
-
?
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
-
-
-
-
?
L-lysine
cadaverine + CO2
-
-
-
-
?
L-lysine
cadaverine + CO2
-
-
-
?
L-lysine
cadaverine + CO2
-
-
-
?
L-lysine
cadaverine + CO2
-
-
-
?
L-lysine
cadaverine + CO2
-
-
-
-
?
L-lysine
cadaverine + CO2
-
-
-
?
L-lysine
cadaverine + CO2
-
-
-
?
L-lysine
cadaverine + CO2
-
-
-
-
?
L-lysine
cadaverine + CO2
-
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
-
-
-
?
L-lysine
cadaverine + CO2
-
-
-
?
L-lysine
cadaverine + CO2
-
-
-
?
L-lysine
cadaverine + CO2
-
-
-
?
L-lysine
cadaverine + CO2
-
-
-
-
?
L-lysine
cadaverine + CO2
-
-
-
-
?
L-lysine
cadaverine + CO2
-
-
-
-
?
L-lysine
cadaverine + CO2
-
-
-
?
L-lysine
cadaverine + CO2
-
-
-
?
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
-
-
-
-
?
L-lysine
cadaverine + CO2
-
-
-
?
L-lysine
cadaverine + CO2
-
-
-
?
L-lysine
cadaverine + CO2
-
-
-
-
?
L-lysine
cadaverine + CO2
-
-
-
-
?
L-lysine
cadaverine + CO2
-
-
-
-
?
L-lysine
cadaverine + CO2
-
-
-
?
L-lysine
cadaverine + CO2
-
-
-
?
L-lysine
cadaverine + CO2
-
-
-
-
?
L-lysine
cadaverine + CO2
-
-
-
-
?
L-lysine
cadaverine + CO2
-
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
?
L-Orn
Putrescine + CO2
-
-
-
-
?
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
-
-
?
L-ornithine
1,4-diaminobutane + CO2
-
-
-
?
L-ornithine
1,4-diaminobutane + CO2
-
-
-
?
S-Aminoethyl-L-Cys
1-Amino-2-(S-aminoethyl)mercaptoethane + CO2
Bacterium cadaveris
-
at 49% of the activity with L-Lys
-
-
?
S-Aminoethyl-L-Cys
1-Amino-2-(S-aminoethyl)mercaptoethane + CO2
-
15% of the activity with L-Lys
-
-
?
S-Aminoethyl-L-Cys
1-Amino-2-(S-aminoethyl)mercaptoethane + CO2
-
15% of the activity with L-Lys
-
-
?
S-Aminoethyl-L-Cys
1-Amino-2-(S-aminoethyl)mercaptoethane + CO2
-
23% of the activity with L-Lys
-
-
?
S-Aminoethyl-L-Cys
1-Amino-2-(S-aminoethyl)mercaptoethane + CO2
-
23% of the activity with L-Lys
-
-
?
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
-
-
?
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
?
-
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
?
-
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
?
-
-
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
?
-
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
?
-
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
-
-
?
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
-
-
?
additional information
?
-
enzyme CadA is very substrate specific and shows only very low activity with ornithine and no activity with arginine and diaminopimelate
-
-
?
additional information
?
-
enzyme CadA 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
?
-
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
?
-
-
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
-
-
?
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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F102C/T544C
site-directed mutagenesis, mutant A2
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
P233C/L628C
site-directed mutagenesis, mutant C1
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
V91C/G445C
site-directed mutagenesis, mutant A1
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
-
P233C/L628C
-
site-directed mutagenesis, mutant C1
-
V91C/G445C
-
site-directed mutagenesis, mutant A1
-
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
-
site-directed mutagenesis, the mutant shows increased LDC activity
V147F/E583G
-
site-directed mutagenesis, the mutant shows 1.62fold increased LDC activity compared to wild-type enzyme
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
-
site-directed mutagenesis, the mutant shows increased LDC activity
-
V147F/E583G
-
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/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/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
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
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
-
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
-
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
-
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 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
-
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
-
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
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
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Beier, H.; Fecker, L.F.; Berlin, J.
Lysine decarboxylase from Hafnia alvei: purification, molecular data and preparation of polyclonal antibodies
Z. Naturforsch. C
42
1307-1312
1987
Hafnia alvei
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Lysine decarboxylase activity and alkaloid production in Heimia salicifolia cultures
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1986
Heimia salicifolia
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Cloning and characterization of a lysine decarboxylase gene from Hafnia alvei
Mol. Gen. Genet.
203
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1986
Hafnia alvei
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Lysine decarboxylase assay by the pH-stat method
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Escherichia coli
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Inhibition of growth of Mycoplasma dispar by DL-alpha-difluoromethyllsine, a selective irreversible inhibitor of lysine decarboxylase, and reversal by cadaverine (1,5-diaminopentane)
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Mycoplasma dispar
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Lysine decarboxylase in plants and its integration in quinolizidine alkaloid biosynthesis
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22
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1983
Anchusa italica, Arum maculatum, Asarum maculatum, Astragalus cicer, Astragalus glycyphyllos, Atropa belladonna, Baptisia australis, Vicia faba, Calla palustris, Oxybasis rubra, Conium maculatum, Cytisus beanii, Cytisus canariensis, Cytisus scoparius, Dictamnus albus, Galega officinalis, Genista anglica, Genista hispanica, Genista lydia, Genista pilosa, Genista sagittalis, Genista tinctoria, Glycine max, Glycyrrhiza echinata, Laburnum alpinum, Laburnum anagyroides, Levisticum officinale, Medicago sativa, Lupinus albus, Lupinus luteus, Lupinus polyphyllus, Malva sylvestris, Melilotus albus, Mentha suaveolens, Menyanthes trifoliata, Nicotiana tabacum, Phaseolus vulgaris, Pisum sativum, Robinia pseudoacacia, Ruta graveolens, Sanguisorba officinalis, Saponaria officinalis, Sedum acre, Senecio fuchsii, Styphnolobium japonicum, Sophora tetraptera, Spinacia oleracea, Symphytum officinale, Trollius europaeus, Valeriana excelsa subsp. sambucifolia
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Lysine decarboxylase (Escherichia coli B)
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Escherichia coli, Escherichia coli B / ATCC 11303
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Purification and properties of Selenomonas ruminantium lysine decarboxylase
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Selenomonas ruminantium
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Lupinus polyphyllus
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Chemical properties of Escherichia coli lysine decarboxylase including a segment of its pyridoxal 5 -phosphate binding site
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Escherichia coli
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Purification and physical properties of inducible Escherichia coli lysine decarboxylase
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Escherichia coli, Escherichia coli B / ATCC 11303
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L-Lysine decarboxylase (Bacterium cadaveris)
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Crystalline lysine decarboxylase
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Studies of enzyme-mediated reactions. Part 14. Stereochemical course of the formation of cadaverine by decarboxylation of (2S)-lysine with lysine decarboxylase (E.C. 4.1.1.18) from Bacillus cadaveris
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1982
Bacterium cadaveris
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Purification and characterization of monomeric lysine decarboxylase from soybean (Glycine max) axes
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Purification and some properties of inducible lysine decarboxylase from Vibrio parahaemolyticus
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Mus musculus, no activity in Rattus norvegicus
brenda
Takatsuka, Y.; Onoda, M.; Sugiyama, T.; Muramoto, K.; Tomita, T.; Kamio, Y.
Novel characteristics of Selenomonas ruminantium lysine decarboxylase capable of decarboxylating both L-lysine and L-ornithine
Biosci. Biotechnol. Biochem.
63
1063-1069
1999
Selenomonas ruminantium (O50657), Selenomonas ruminantium
brenda
Takatsuka, Y.; Tomita, T.; Kamio, Y.
Identification of the amino acid residues conferring substrate specificity upon Selenomonas ruminantium lysine decarboxylase
Biosci. Biotechnol. Biochem.
63
1843-1846
1999
Selenomonas ruminantium
brenda
Takatsuka, Y.; Yamaguchi, Y.; Ono, M.; Kamio, Y.
Gene cloning and molecular characterization of lysine decarboxylase from Selenomonas ruminantium delineate its evolutionary relationship to ornithine decarboxylases from eukaryotes
J. Bacteriol.
182
6732-6741
2000
Selenomonas ruminantium (O50657), Selenomonas ruminantium
brenda
Levine, M.; Progulske-Fox, A.; Denslow, N.D.; Farmerie, W.G.; Smith, D.M.; Swearingen, W.T.; Miller, F.C.; Liang, Z.; Roe, B.A.; Pan, H.Q.
Identification of lysine decarboxylase as a mammalian cell growth inhibitor in Eikenella corrodens: possible role in periodontal disease
Microb. Pathog.
30
179-192
2001
Eikenella corrodens
brenda
Snider, J.; Gutsche, I.; Lin, M.; Baby, S.; Cox, B.; Butland, G.; Greenblatt, J.; Emili, A.; Houry, W.A.
Formation of a distinctive complex between the inducible bacterial lysine decarboxylase and a novel AAA+ ATPase
J. Biol. Chem.
281
1532-1546
2006
Escherichia coli
brenda
Kukimoto-Niino, M.; Murayama, K.; Kato-Murayama, M.; Idaka, M.; Bessho, Y.; Tatsuguchi, A.; Ushikoshi-Nakayama, R.; Terada, T.; Kuramitsu, S.; Shirouzu, M.; Yokoyama, S.
Crystal structures of possible lysine decarboxylases from Thermus thermophilus HB8
Protein Sci.
13
3038-3042
2004
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
brenda
Tanaka, Y.; Kimura, B.; Takahashi, H.; Watanabe, T.; Obata, H.; Kai, A.; Morozumi, S.; Fujii, T.
Lysine decarboxylase of Vibrio parahaemolyticus: kinetics of transcription and role in acid resistance
J. Appl. Microbiol.
104
1283-1293
2007
Vibrio parahaemolyticus (Q87KT6), Vibrio parahaemolyticus
brenda
Kim, J.S.; Choi, S.H.; Lee, J.K.
Lysine decarboxylase expression by Vibrio vulnificus is induced by SoxR in response to superoxide stress
J. Bacteriol.
188
8586-8592
2006
Vibrio vulnificus
brenda
Moreau, P.L.
The lysine decarboxylase CadA protects Escherichia coli starved of phosphate against fermentation acids
J. Bacteriol.
189
2249-2261
2007
Escherichia coli
brenda
Alexopoulos, E.; Kanjee, U.; Snider, J.; Houry, W.A.; Pai, E.F.
Crystallization and preliminary X-ray analysis of the inducible lysine decarboxylase from Escherichia coli
Acta Crystallogr. Sect. F
64
700-706
2008
Escherichia coli (P0A9H3), Escherichia coli
brenda
Ohe, M.; Scoccianti, V.; Bagni, N.; Tassoni, A.; Matsuzaki, S.
Putative occurrence of lysine decarboxylase isoforms in soybean (Glycine max) seedlings
Amino Acids
36
65-70
2009
Glycine max
brenda
Tateno, T.; Okada, Y.; Tsuchidate, T.; Tanaka, T.; Fukuda, H.; Kondo, A.
Direct production of cadaverine from soluble starch using Corynebacterium glutamicum coexpressing alpha-amylase and lysine decarboxylase
Appl. Microbiol. Biotechnol.
82
115-121
2009
Escherichia coli
brenda
Lafay, B.; Ruimy, R.; de Traubenberg, C.R.; Breittmayer, V.; Gauthier, M.J.; Christen, R.
Roseobacter algicola sp. nov., a new marine bacterium isolated from the phycosphere of the toxin-producing dinoflagellate Prorocentrum lima
Int. J. Syst. Bacteriol.
45
290-296
1995
no activity in Marinovum algicola, no activity in Marinovum algicola ATCC 51442
brenda
Ruiz-Ponte, C.; Cilia, V.; Lambert, C.; Nicolas, J.L.
Roseobacter gallaeciensis sp. nov., a new marine bacterium isolated from rearings and collectors of the scallop Pecten maximus
Int. J. Syst. Bacteriol.
48 Pt 2
537-542
1998
no activity in Phaeobacter gallaeciensis BS107
brenda
Lau, S.C.; Tsoi, M.M.; Li, X.; Plakhotnikova, I.; Wu, M.; Wong, P.K.; Qian, P.Y.
Loktanella hongkongensis sp. nov., a novel member of the alpha-Proteobacteria originating from marine biofilms in Hong Kong waters
Int. J. Syst. Evol. Microbiol.
54
2281-2284
2004
no activity in Loktanella hongkongensis
brenda
Lee, O.O.; Tsoi, M.M.; Li, X.; Wong, P.K.; Qian, P.Y.
Thalassococcus halodurans gen. nov., sp. nov., a novel halotolerant member of the Roseobacter clade isolated from the marine sponge Halichondria panicea at Friday Harbor, USA
Int. J. Syst. Evol. Microbiol.
57
1919-1924
2007
no activity in Thalassobius mediterraneus, no activity in Thalassobius mediterraneus XSM19, no activity in Thalassococcus halodurans, no activity in Thalassococcus halodurans UST050418-052, Shimia aestuarii, Shimia aestuarii JC2049
brenda
Alvarez-Ordonez, A.; Fernandez, A.; Bernardo, A.; Lopez, M.
Arginine and lysine decarboxylases and the acid tolerance response of Salmonella typhimurium
Int. J. Food Microbiol.
136
278-282
2010
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium CECT 443
brenda
Sempruch, C.; Leszczynski, B.; Wojcicka, A.; Makosz, M.; Matok, H.; Chrzanowski, G.
Changes in activity of lysine decarboxylase in winter triticale in response to grain aphid feeding
Acta Biol. Hung.
61
512-515
2010
Secale cereale x Triticum aestivum
brenda
Kanjee, U.; Gutsche, I.; Alexopoulos, E.; Zhao, B.; El Bakkouri, M.; Thibault, G.; Liu, K.; Ramachandran, S.; Snider, J.; Pai, E.F.; Houry, W.A.
Linkage between the bacterial acid stress and stringent responses: the structure of the inducible lysine decarboxylase
EMBO J.
30
931-944
2011
Escherichia coli (P0A9H3), Escherichia coli
brenda
Teng, Y.; Scott, E.; Van Zeeland, A.; Sanders, J.
The use of L-lysine decarboxylase as a means to separate amino acids by electrodialysis
Green Chem.
13
624-630
2011
Bacterium cadaveris
-
brenda
El Bakkouri, M.; Gutsche, I.; Kanjee, U.; Zhao, B.; Yu, M.; Goret, G.; Schoehn, G.; Burmeister, W.P.; Houry, W.A.
Structure of RavA MoxR AAA+ protein reveals the design principles of a molecular cage modulating the inducible lysine decarboxylase activity
Proc. Natl. Acad. Sci. USA
107
22499-22504
2010
Escherichia coli
brenda
Romano, A.; Trip, H.; Lolkema, J.S.; Lucas, P.M.
Three-component lysine/ornithine decarboxylation system in Lactobacillus saerimneri 30a
J. Bacteriol.
195
1249-1254
2013
Ligilactobacillus saerimneri 30a, Ligilactobacillus saerimneri 30a ATCC 33222
brenda
Sugawara, A.; Matsui, D.; Takahashi, N.; Yamada, M.; Asano, Y.; Isobe, K.
Characterization of a pyridoxal-5'-phosphate-dependent L-lysine decarboxylase/oxidase from Burkholderia sp. AIU 395
J. Biosci. Bioeng.
118
496-501
2014
Burkholderia sp., Burkholderia sp. AIU 395
brenda
Lohinai, Z.; Keremi, B.; Szoko, E.; Tabi, T.; Szabo, C.; Tulassay, Z.; Levine, M.
Bacterial lysine decarboxylase influences human dental biofilm lysine content, biofilm accumulation, and subclinical gingival inflammation
J. Periodontol.
83
1048-1056
2012
Eikenella corrodens (Q9Z4R7), Eikenella corrodens
brenda
Burrell, M.; Hanfrey, C.C.; Kinch, L.N.; Elliott, K.A.; Michael, A.J.
Evolution of a novel lysine decarboxylase in siderophore biosynthesis
Mol. Microbiol.
86
485-499
2012
Streptomyces coelicolor (Q9L072), Streptomyces coelicolor, Streptomyces coelicolor ATCC BAA-471 (Q9L072)
brenda
Shin, J.; Joo, J.C.; Lee, E.; Hyun, S.M.; Kim, H.J.; Park, S.J.; Yang, Y.H.; Park, K.
Characterization of a whole-cell biotransformation using a constitutive lysine decarboxylase from Escherichia coli for the high-level production of cadaverine from industrial grade L-lysine
Appl. Biochem. Biotechnol.
185
909-924
2018
Escherichia coli (P0A9H3), Escherichia coli (P52095), Escherichia coli, Escherichia coli K-12 / MG1655 (P0A9H3), Escherichia coli K-12 / MG1655 (P52095)
brenda
Wang, S.; Wan, B.; Zhang, L.; Yang, Y.; Guo, L.H.
In vitro inhibition of lysine decarboxylase activity by organophosphate esters
Biochem. Pharmacol.
92
506-516
2014
Bacterium cadaveris
brenda
Li, N.; Chou, H.; Yu, L.; Xu, Y.
Cadaverine production by heterologous expression of Klebsiella oxytoca lysine decarboxylase
Biotechnol. Bioprocess Eng.
19
965-972
2014
Klebsiella oxytoca, Klebsiella oxytoca DSM 6673
-
brenda
Wang, C.; Zhang, K.; Zhongjun, C.; Cai, H.; Honggui, W.; Ouyang, P.
Directed evolution and mutagenesis of lysine decarboxylase from Hafnia alvei AS1.1009 to improve its activity toward efficient cadaverine production
Biotechnol. Bioprocess Eng.
20
439-446
2015
Hafnia alvei, Hafnia alvei AS1.1009
-
brenda
Hong, E.Y.; Lee, S.G.; Park, B.J.; Lee, J.M.; Yun, H.; Kim, B.G.
Simultaneously enhancing the stability and catalytic activity of multimeric lysine decarboxylase CadA by engineering interface regions for enzymatic production of cadaverine at high concentration of lysine
Biotechnol. J.
12
1700278
2017
Escherichia coli (P0A9H3), Escherichia coli K-12 / B (P0A9H3)
brenda
Kou, F.; Zhao, J.; Liu, J.; Sun, C.; Guo, Y.; Tan, Z.; Cheng, F.; Li, Z.; Zheng, P.; Sun, J.
Enhancement of the thermal and alkaline pH stability of Escherichia coli lysine decarboxylase for efficient cadaverine production
Biotechnol. Lett.
40
719-727
2018
Escherichia coli (P0A9H3), Escherichia coli
brenda
Kmiec, K.; Sempruch, C.; Chrzanowski, G.; Czerniewicz, P.
The effect of Tetraneura ulmi L. galling process on the activity of amino acid decarboxylases and the content of biogenic amines in Siberian elm tissues
Bull. Entomol. Res.
108
69-76
2018
Ulmus pumila
brenda
Li, N.; Yu, L.; Xu, Y.
Heterologous expression and characterization of Klebsiella oxytoca lysine decarboxylase
Chin. J. Biotechnol.
32
527-531
2016
Klebsiella oxytoca (A0A0H3H393), Klebsiella oxytoca, Klebsiella oxytoca ATCC 8724 / DSM 4798 / JCM 20051 / NBRC 3318 / NRRL B-199 / KCTC 1686 (A0A0H3H393)
brenda
Li, N.; Chou, H.; Xu, Y.
Improved cadaverine production from mutant Klebsiella oxytoca lysine decarboxylase
Eng. Life Sci.
16
299-305
2016
Klebsiella oxytoca, Klebsiella oxytoca DSM 6673
-
brenda
Kim, H.J.; Kim, Y.H.; Shin, J.H.; Bhatia, S.K.; Sathiyanarayanan, G.; Seo, H.M.; Choi, K.Y.; Yang, Y.H.; Park, K.
Optimization of direct lysine decarboxylase biotransformation for cadaverine production with whole-cell biocatalysts at high lysine concentration
J. Microbiol. Biotechnol.
25
1108-1113
2015
Escherichia coli (P0A9H3), Escherichia coli, Escherichia coli K-12 / MG1655 (P0A9H3)
brenda
Kim, Y.H.; Sathiyanarayanan, G.; Kim, H.J.; Bhatia, S.K.; Seo, H.M.; Kim, J.H.; Song, H.S.; Kim, Y.G.; Park, K.; Yang, Y.H.
A Liquid-based colorimetric assay of lysine decarboxylase and its application to enzymatic assay
J. Microbiol. Biotechnol.
25
2110-2115
2015
Burkholderia thailandensis, Klebsiella aerogenes (A0A0H3FP92), Escherichia coli (P52095), Escherichia coli K-12 / MG1655 (P52095), Klebsiella aerogenes ATCC 13048 / DSM 30053 / JCM 1235 / KCTC 2190 / NBRC 13534 / NCIMB 10102 / NCTC 10006 (A0A0H3FP92)
brenda
Kim, J.H.; Kim, H.J.; Kim, Y.H.; Jeon, J.M.; Song, H.S.; Kim, J.; No, S.Y.; Shin, J.H.; Choi, K.Y.; Park, K.M.; Yang, Y.H.
Functional study of lysine decarboxylases from Klebsiella pneumoniae in Escherichia coli and application of whole cell bioconversion for cadaverine production
J. Microbiol. Biotechnol.
26
1586-1592
2016
Klebsiella aerogenes (A0A094XEM2), Klebsiella aerogenes (A0A0H3FP92), Klebsiella aerogenes ATCC 13048 / DSM 30053 / JCM 1235 / KCTC 2190 / NBRC 13534 / NCIMB 10102 / NCTC 10006 (A0A0H3FP92)
brenda
Park, S.H.; Soetyono, F.; Kim, H.K.
Cadaverine production by using cross-linked enzyme aggregate of Escherichia coli lysine decarboxylase
J. Microbiol. Biotechnol.
27
289-296
2017
Escherichia coli (P0A9H3)
brenda
Kou, F.; Zhao, J.; Liu, J.; Shen, J.; Ye, Q.; Zheng, P.; Li, Z.; Sun, J.; Ma, Y.
Characterization of a new lysine decarboxylase from Aliivibrio salmonicida for cadaverine production at alkaline pH
J. Mol. Catal. B
133
S88-S94
2016
Aliivibrio salmonicida (B6EKJ5)
-
brenda
Jeong, S.; Yeon, Y.; Choi, E.; Byun, S.; Cho, D.; Kim, I.; Kim, Y.
Alkaliphilic lysine decarboxylases for effective synthesis of cadaverine from L-lysine
Korean J. Chem. Engin.
33
1530-1533
2016
Geobacillus thermodenitrificans
-
brenda
Sagong, H.Y.; Son, H.F.; Kim, S.; Kim, Y.H.; Kim, I.K.; Kim, K.J.
Crystal structure and pyridoxal 5-phosphate binding property of lysine decarboxylase from Selenomonas ruminantium
PLoS ONE
11
e0166667
2016
Selenomonas ruminantium (O50657), Selenomonas ruminantium
brenda
Sagong, H.Y.; Kim, K.J.
Lysine decarboxylase with an enhanced affinity for pyridoxal 5-phosphate by disulfide bond-mediated spatial reconstitution
PLoS ONE
12
e0170163
2017
Selenomonas ruminantium (O50657), Selenomonas ruminantium
brenda
Wang, D.; Zhao, L.; Jiang, J.; Liu, J.; Wang, D.; Yu, X.; Wei, Y.; Ouyang, Z.
Cloning, expression, and functional analysis of lysine decarboxylase in mulberry (Morus alba L.)
Protein Expr. Purif.
151
30-37
2018
Morus alba (A0A2Z4EVE5), Morus alba
brenda
Kandiah, E.; Carriel, D.; Perard, J.; Malet, H.; Bacia, M.; Liu, K.; Chan, S.W.; Houry, W.A.; Ollagnier de Choudens, S.; Elsen, S.; Gutsche, I.
Structural insights into the Escherichia coli lysine decarboxylases and molecular determinants of interaction with the AAA+ ATPase RavA
Sci. Rep.
6
24601
2016
Escherichia coli (P0A9H3), Escherichia coli (P52095), Escherichia coli
brenda
Kloss, R.; Limberg, M.H.; Mackfeld, U.; Hahn, D.; Gruenberger, A.; Jaeger, V.D.; Krauss, U.; Oldiges, M.; Pohl, M.
Catalytically active inclusion bodies of L-lysine decarboxylase from E. coli for 1,5-diaminopentane production
Sci. Rep.
8
5856
2018
Escherichia coli (P52095), Escherichia coli
brenda