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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
-
-
-
?
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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7
delta-hydroxylysine
-
-
1.3
L-2,4-diaminobutanoate
pH 7.5, 30°C
3.4 - 4.5
S-aminoethyl-L-Cys
additional information
additional information
-
0.37
L-Lys

Bacterium cadaveris
-
-
1.5
L-Lys
pH 6.0, 30°C, wild-type enzyme
1.9
L-Lys
pH 6.0, 30°C, mutant enzyme A52C
2.4
L-Lys
pH 6.0, 30°C, mutant enzyme A52C/P54D
3
L-Lys
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P
3.6
L-Lys
pH 6.0, 30°C, mutant enzyme M50V/A52C/P54D/T55S
4
L-Lys
pH 6.0, 30°C, mutant enzyme G319W
5.7
L-Lys
pH 6.0, 30°C, mutant enzyme P54D
6.7
L-Lys
pH 6.0, 30°C, mutant enzyme S322A
8
L-Lys
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D
17
L-Lys
pH 6.0, 30°C, mutant enzyme S322T/I326L
22
L-Lys
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D/S322T/I326L
270
L-Lys
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D/S322A
0.0192
L-lysine

recombinant His-tagged enzyme, pH 8.0, 37°C
0.058
L-lysine
pH 7.5, 30°C
0.42
L-lysine
at pH 6.5, between 4°C and 10°C
0.84
L-lysine
-
pH 7, 30°C
0.92
L-lysine
recombinant enzyme, pH 7.5, 37°C
1.22
L-lysine
pH 5.6, 45°C, recombinant His6-tagged wild-type enzyme
1.33
L-lysine
pH 5.6, 45°C, recombinant His6-tagged mutant F14C/K44C
1.47
L-lysine
pH 5.6, 45°C, recombinant His6-tagged mutant F14C/K44C/L7M/N8G
3.23
L-lysine
-
pH 6.0, 37°C, recombinant mutant E583G
4.93
L-lysine
-
pH 6.0, 37°C, recombinant wild-type enzyme
7.7
L-lysine
pH 6.0, 37°C, recombinant enzyme
12.7
L-lysine
-
pH 5.5, 37°C
0.96
L-Orn

pH 6.0, 30°C, wild type enzyme
0.98
L-Orn
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P
1.2
L-Orn
pH 6.0, 30°C, mutant enzyme S322A
1.3
L-Orn
pH 6.0, 30°C, mutant enzyme A52C
1.3
L-Orn
pH 6.0, 30°C, mutant enzyme G319W
1.5
L-Orn
pH 6.0, 30°C, mutant enzyme S322T/I326L
1.6
L-Orn
pH 6.0, 30°C, mutant enzyme A52C/P54D
2.1
L-Orn
pH 6.0, 30°C, mutant enzyme P54D
3.1
L-Orn
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D
3.3
L-Orn
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D/S322T/I326L
4
L-Orn
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D/S322A
4.5
L-Orn
pH 6.0, 30°C, mutant enzyme M50V/A52C/P54D/T55S
3.4
S-aminoethyl-L-Cys

-
-
4.5
S-aminoethyl-L-Cys
Bacterium cadaveris
-
-
additional information
additional information

Michaelis-Menten kinetics
-
additional information
additional information
kinetic analysis of wild-type and mutant enzymes
-
additional information
additional information
-
kinetic analysis of wild-type and mutant enzymes
-
additional information
additional information
-
kinetic analysis of wild-type and mutant enzymes, overview
-
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metabolism
-
changes in the contents of plant biogenic amines (putrescine, cadaverine, spermidine, tryptamine, spermine and histamine) and key enzymes of their biosynthesis, i.e. lysine decarboxylase (LDC), tyrosine decarboxylase, and ornithine decarboxylase (ODC) in galls and other parts of Siberian elm (Ulmus pumila) leaves during the galling process caused by the aphid Tetraneura ulmi first instar larvae, overview
evolution

certain enterobacteria exert evolutionary pressure on the lysine decarboxylase towards the macromolecular cage-like assembly with AAA+ ATPase RavA, implying that this complex may have an important function under particular stress conditions. The C-terminal beta-sheet of a lysine decarboxylase is a highly conserved signature allowing to distinguish between LdcI and LdcC. RavA is binding to LdcI, but is not capable of binding to LdcC, LDC sequence comparisons and phylogenetic analysis
evolution
Selenomonas ruminantium SrLDC shows much lower pyridoxal 5'-phosphate affinity than other pyridoxal 5'-phosphate-dependent enzymes. The highly flexible active site contributes to the low affinity for pyridoxal 5'-phosphate in SrLDC
evolution
the L-lysine decarboxylase (LDC) genes from Escherichia coli include genes cadA and ldcC encoding the acid-inducible enzyme CadA and the constitutive LDCc, respectively
physiological function

inducible lysine decarboxylase, LdcI/CadA, together with the inner-membrane lysine-cadaverine antiporter, CadB, provide cells with protection against mild acidic conditions (about pH 5.0)
physiological function
enzyme is involved in NRPS-independent siderophore biosynthesis
physiological function
-
Lactobacillus saerimneri 30a contains a three-component decarboxylation system consisting of ornithine decarboxylase, lysine decarboxylase and a transporter catalyzing both lysine/cadaverine and ornithine/putrescine exchange
physiological function
lysine decarboxylase (LDC) is an important enzyme for maintenance of pH homeostasis and the biosynthesis of cadaverine. Most of bacteria utilize acid stress-induced lysine decarboxylase in the response to the environmental acid stress
physiological function
lysine decarboxylase MaLDC is involved in the biosynthesis of DNJ alkaloids. 1-Deoxynojirimycin (DNJ) is the main bioactive compound of Morus alba and has pharmacological effects in humans, including blood sugar level regulation and antiviral activity. The enzyme expression is correlated with DNJ content in leaves
physiological function
the inducible lysine decarboxylase LdcI (or CadA) is an important enterobacterial acid stress response enzyme whereas constitutive lysine decarboxylase LdcC is its close paralogue, thought to play mainly a metabolic role. Escherichia coli AAA+ ATPase RavA, involved in multiple stress response pathways, tightly interacts with enzyme LdcI. A unique macromolecular cage is formed by two decamers (two double pentameric rings) of the Escherichia coli LdcI and five hexamers of the AAA+ ATPase RavA (UniProt ID P31473) counteracting acid stress under starvation. LdcI is bound to the LARA domain of RavA
physiological function
-
Lactobacillus saerimneri 30a contains a three-component decarboxylation system consisting of ornithine decarboxylase, lysine decarboxylase and a transporter catalyzing both lysine/cadaverine and ornithine/putrescine exchange
-
physiological function
-
enzyme is involved in NRPS-independent siderophore biosynthesis
-
additional information

-
compared to the activity of lysine/ornithine decarboxylase from Selenomonas ruminantium and from Vibrio vulnificus, the cadaverine producing activity of enzyme gtLDC is severalfold reduced
additional information
construction of a pseudoatomic model of the LdcI-RavA cage based on its cryo-electron microscopy map and yo-electron microscopy 3D reconstructions of the Escherichia coli LdcI and LdcC at optimal pH, overview. RavA is not capable of binding to LdcC. Conformational rearrangements in the enzyme LdcI active site, overview
additional information
construction of a pseudoatomic model of the LdcI-RavA cage based on its cryo-electron microscopy map and yo-electron microscopy 3D reconstructions of the Escherichia coli LdcI and LdcC at optimal pH, overview. RavA is not capable of binding to LdcC. Conformational rearrangements in the enzyme LdcI active site, overview
additional information
-
construction of a pseudoatomic model of the LdcI-RavA cage based on its cryo-electron microscopy map and yo-electron microscopy 3D reconstructions of the Escherichia coli LdcI and LdcC at optimal pH, overview. RavA is not capable of binding to LdcC. Conformational rearrangements in the enzyme LdcI active site, overview
additional information
due to the flexible pyridoxal 5'-phosphate binding site, the protein undergoes an open/closed conformational change at the PLP binding site depending on the pyridoxal 5'-phosphate binding. Especially, two loops located in the vicinity of the pyridoxal 5'-phosphate binding site, the pyridoxal 5'-phosphate stabilization loop (PS-loop) and the regulatory loop (R-loop), undergo a significant structural movement depending on the pyridoxal 5'-phosphate binding
additional information
-
due to the flexible pyridoxal 5'-phosphate binding site, the protein undergoes an open/closed conformational change at the PLP binding site depending on the pyridoxal 5'-phosphate binding. Especially, two loops located in the vicinity of the pyridoxal 5'-phosphate binding site, the pyridoxal 5'-phosphate stabilization loop (PS-loop) and the regulatory loop (R-loop), undergo a significant structural movement depending on the pyridoxal 5'-phosphate binding
additional information
Escherichia coli AAA+ ATPase RavA is not capable of binding to LdcC
additional information
Escherichia coli AAA+ ATPase RavA is not capable of binding to LdcC
additional information
-
Escherichia coli AAA+ ATPase RavA is not capable of binding to LdcC
additional information
optimization of the EcLdcC-catalyzed whole-cell biotransformation, overview
additional information
optimization of the EcLdcC-catalyzed whole-cell biotransformation, overview
additional information
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optimization of the EcLdcC-catalyzed whole-cell biotransformation, overview
additional information
structure of enzyme SrLDC in complex with pyridoxal 5'-phosphate and cadaverine and binding mode of cofactor and substrate, overview
additional information
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structure of enzyme SrLDC in complex with pyridoxal 5'-phosphate and cadaverine and binding mode of cofactor and substrate, overview
additional information
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the LDC monomer has a C-terminal domain (residues 564-715), that has a predominantly alpha-helical outer surface and an inner surface that consists of two sets of beta-sheets, and is very important. The C-terminal domain forms part of the entry channel into the active site of the enzyme. The amino acid change E583G changes a residue located in this channel with improving effects on enzyme activity
additional information
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optimization of the EcLdcC-catalyzed whole-cell biotransformation, overview
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additional information
-
the LDC monomer has a C-terminal domain (residues 564-715), that has a predominantly alpha-helical outer surface and an inner surface that consists of two sets of beta-sheets, and is very important. The C-terminal domain forms part of the entry channel into the active site of the enzyme. The amino acid change E583G changes a residue located in this channel with improving effects on enzyme activity
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monomer
-
1 * 95000, SDS-PAGE
?

-
x * 80000, equilibrium ultracentrifugation in 6 M guanidine-HCl, SDS-PAGE. Association of the dimeric form to the decamer is concomitant with the increase in ionic strength
?
-
x * 80000, SDS-PAGE, high-speed sedimentation equilibrium in presence of 6 M guanidine HCl. Subunits associate or dissociate reversibly as a function of pH and ionic strength. The native decameric form is formed by the cyclic association of five dimers. Its overall appearance is that of two stacked pentameric rings. Higher aggregates result from the linear stacking of decamers to form rodlike particles of indefinite length
?
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x * 80000, equilibrium ultracentrifugation in 6 M guanidine-HCl, SDS-PAGE. Association of the dimeric form to the decamer is concomitant with the increase in ionic strength
-
?
-
x * 80000, SDS-PAGE, high-speed sedimentation equilibrium in presence of 6 M guanidine HCl. Subunits associate or dissociate reversibly as a function of pH and ionic strength. The native decameric form is formed by the cyclic association of five dimers. Its overall appearance is that of two stacked pentameric rings. Higher aggregates result from the linear stacking of decamers to form rodlike particles of indefinite length
-
?
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x * 54800, recombinant His6-tagged enzyme, SDS-PAGE
?
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? * 80000, SDS-PAGE, under native conditions aggregation of up to 10 subunits
?
x * 80000, recombinant enzyme
?
-
x * 80000, recombinant enzyme
-
?
-
x * 85000, SDS-PAGE
-
?
x * 24000, recombinant His-tagged enzyme, SDS-PAGE
decamer

-
decamer
-
10 * 80000, SDS-PAGE
decamer
x-ray crystallography
decamer
the protein is an oligomer of five dimers that associate to form a decamer, X-ray crystallography
decamer
10 * 81000, recombinant His-tagged wild-type and mutant T88S, SDS-PAGE
dimer

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dimer
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2 * 76500, SDS-PAGE
dimer
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2 * 76500, SDS-PAGE
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dimer
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2 * 44000, SDS-PAGE
dimer
2 * 42000, SDS-PAGE
heptamer

-
7 * 79000, SDS-PAGE
heptamer
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7 * 79000, SDS-PAGE
-
hexamer

-
isozyme TT1465, crystallization data
hexamer
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isozyme TT1465, crystallization data
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homodecamer

-
homodecamer
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10 * 81000, X-ray crystallography
homodecamer
a pentamer of homodimers, 10 * 82000, recombinant His6-tagged wild-type enzyme, SDS-PAGE
homodecamer
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a pentamer of homodimers, 10 * 82000, recombinant His6-tagged wild-type enzyme, SDS-PAGE
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homodimer

2 * 44000, recombinant His-tagged enzyme, SDS-PAGE
homodimer
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2 * 44000, recombinant His-tagged enzyme, SDS-PAGE
tetramer

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isozyme TT1887, crystallization data
tetramer
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isozyme TT1887, crystallization data
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additional information

a mixture of dimers (about 158 kDa) and decamers (about 780 kDa) is present for the enzyme at pH 7.5. Decamers are dominant for AsLdc, dependent on the pH: the highest proportion of decamer for AsLdc (78%) is observed at pH 7.5, while it is reduced to 30% and 57% at pH 5.0 and pH 8.5, respectively
additional information
-
enzyme interacts strongly with regulatory ATPase variant A, RavA, forming a cage-like structure consisting of two enzyme decamers linked by up to five RavA oligomers. Enzyme activity is not affected by binding to RavA, but complex formation results in stimulation of RavA ATPase activity
additional information
three-dimensional structure analysis of enzyme CadA, overview
additional information
-
three-dimensional structure analysis of enzyme CadA, overview
additional information
SrLDC functions as a dimer and each monomer consists of two distinct domains, a pyridoxal 5'-phosphate-binding-barrel domain and a sheet domain. A shallow substrate-binding hole is formed at the interface between the sheet domains of two monomers
additional information
-
SrLDC functions as a dimer and each monomer consists of two distinct domains, a pyridoxal 5'-phosphate-binding-barrel domain and a sheet domain. A shallow substrate-binding hole is formed at the interface between the sheet domains of two monomers
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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
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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
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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
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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
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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
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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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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
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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
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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
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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
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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
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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
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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
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Klebsiella aerogenes ATCC 13048 / DSM 30053 / JCM 1235 / KCTC 2190 / NBRC 13534 / NCIMB 10102 / NCTC 10006
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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
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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
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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
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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
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additional information
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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
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disulfide bond-mediated spatial reconstitution can be a platform technology for development of enzymes with enhanced pyridoxal 5'-phosphate affinity
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disulfide bond-mediated spatial reconstitution can be a platform technology for development of enzymes with enhanced pyridoxal 5'-phosphate affinity
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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
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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
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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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