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Information on EC 4.1.1.18 - lysine decarboxylase
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4.1.1.18 lysine decarboxylaseIUBMB Comments
A pyridoxal-phosphate protein. Also acts on 5-hydroxy-L-lysine.
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Word Map
- 4.1.1.18
- ornithine
- urease
-
dihydrolase
- aeromonas
- decarboxylases
-
voges-proskauer
-
dna-dna
- esculin
-
non-motile
- salicin
-
cadba
- 1,5-diaminopentane
- d-mannitol
- melibiose
- adonitol
- dulcitol
- carbenicillin
- ruminantium
- sobria
-
enteroinvasive
-
selenomonas
- cephalothin
- d-sorbitol
-
quinolizidine
- corrodens
- alvei
-
4.1.1.17
-
simmons
- huperzia
-
macconkey
- synthesis
- d-arabitol
-
hafnia
- eikenella
- medicine
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
AsLdc, CadA, constitutive LDCc, constitutive lysine decarboxylase, DesA, EcLDCc, ECORLD, gtLDC, inducible lysine decarboxylase, L-Lys-OD, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
CadA
constitutive lysine decarboxylase
DesA
inducible lysine decarboxylase
L-Lys-OD
L-lysine decarboxylase
LDC
ldcC
LdcI/CadA
LysA
lysine decarboxylase
multimeric lysine decarboxylase
LDC
-
-
-
-
ldcC
Klebsiella aerogenes ATCC 13048 / DSM 30053 / JCM 1235 / KCTC 2190 / NBRC 13534 / NCIMB 10102 / NCTC 10006
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
L-lysine = cadaverine + CO2
reaction proceeds with retention of configuration at C-2, stereochemistry
Bacterium cadaveris
-
L-lysine = cadaverine + CO2
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
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SYSTEMATIC NAME
IUBMB Comments
L-lysine carboxy-lyase (cadaverine-forming)
A pyridoxal-phosphate protein. Also acts on 5-hydroxy-L-lysine.
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CAS REGISTRY NUMBER
COMMENTARY
9024-76-4
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
delta-Hydroxylysine
1,5-Diamino-2-hydroxypentane + CO2
Bacterium cadaveris
-
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
Escherichia coli B / ATCC 11303
-
25% of the activity with L-Lys
-
-
?
delta-Hydroxylysine
1,5-Diamino-2-hydroxypentane + CO2
-
17% of the activity with L-Lys
-
-
?
delta-Hydroxylysine
1,5-Diamino-2-hydroxypentane + CO2
-
17% of the activity with L-Lys
-
-
?
L-2,4-diaminobutanoate
1,3-diaminopropane + CO2
-
-
-
?
L-Lys
?
-
enzyme activity is positively correlated with the chlorophyll content during leaf regreening. The enzyme is an integrated part of the alkaloid specific biosynthetic sequence
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
-
?
L-Lys
Cadaverine + CO2
-
-
-
-
?
L-Lys
Cadaverine + CO2
constitutive enzyme is involved in synthesis of cadaverine, which is an essential constituent of the peptidoglycan for normal cell growth
-
-
?
L-Lys
Cadaverine + CO2
-
the ratio of activity with L-Orn to activity with L-Lys is 0.69 in wild type enzyme, 1.0 in mutant enzyme A44V/G45T/V46P, 4.0 in mutant enzyme M50V/A52C/P54D/T55S, 0.64 in mutant enzyme M50V, 1.2 in mutant enzyme A52C, 1.8 in mutant enzyme P54D, 0.66 in mutant enzyme T55S, 1.9 in mutant enzyme M50V/A52C, 1.8 in mutant enzyme P54D/T55S, 2.6 in mutant enzyme A52C/P54D, 2.4 in mutant enzyme M50V/A52C/P54D and 2.7 in mutant enzyme A52C/P54D/T55S
-
-
?
L-Lys
Cadaverine + CO2
the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 0.83 for the wild-type enzyme
-
-
?
L-lysine
1,5-diaminopentane + CO2
best substrate
-
-
?
L-lysine
cadaverine + CO2
100% conversion by the recombinant enzyme at pH 7.5
-
-
?
L-lysine
cadaverine + CO2
-
enzyme is a bifunctional L-lysine oxidase/decarboxylase, the decarboxylation reaction takes place 150 times faster than the oxidation reaction
-
-
?
L-lysine
cadaverine + CO2
-
enzyme is a bifunctional L-lysine oxidase/decarboxylase, the decarboxylation reaction takes place 150 times faster than the oxidation reaction
-
-
?
L-lysine
cadaverine + CO2
-
CadA protects Escherichia coli starved of phosphate against fermentation acids in the host gut, the tolerance of the starved cells to fermentation acids is markedly increased as a result of the activity of the inducible CadBA lysine-dependent acid resistance system, independent of expression of the RpoS regulon, overview
-
-
?
L-lysine
cadaverine + CO2
optimal at 0.25 M lysine
-
-
?
L-lysine
cadaverine + CO2
Klebsiella aerogenes ATCC 13048 / DSM 30053 / JCM 1235 / KCTC 2190 / NBRC 13534 / NCIMB 10102 / NCTC 10006
-
-
-
?
L-lysine
cadaverine + CO2
Klebsiella aerogenes ATCC 13048 / DSM 30053 / JCM 1235 / KCTC 2190 / NBRC 13534 / NCIMB 10102 / NCTC 10006
optimal at 0.25 M lysine
-
-
?
L-lysine
cadaverine + CO2
Klebsiella oxytoca ATCC 8724 / DSM 4798 / JCM 20051 / NBRC 3318 / NRRL B-199 / KCTC 1686
-
-
-
?
L-Orn
Putrescine + CO2
-
the ratio of activity with L-Orn to activity with L-Lys is 0.69 in wild type enzyme, 1.0 in mutant enzyme A44V/G45T/V46P, 4.o in mutant enzyme M50V/A52C/P54D/T55S, 0.64 in mutant enzyme M50V, 1.2 in mutant enzyme A52C, 1.8 in mutant enzyme P54D, 0.66 in mutant enzyme T55S, 1.9 in mutant enzyme M50V/A52C, 1.8 in mutant enzyme P54D/T55S, 2.6 in mutant enzyme A52C/P54D, 2.4 in mutant enzyme M50V/A52C/P54D and 2.7 in mutant enzyme A52C/P54D/T55S
-
-
?
S-Aminoethyl-L-Cys
1-Amino-2-(S-aminoethyl)mercaptoethane + CO2
Bacterium cadaveris
-
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
Escherichia coli B / ATCC 11303
-
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
?
-
Escherichia coli K-12 / MG1655
optimization of direct lysine decarboxylase biotransformation of lysine to cadaverine for cadaverine production with whole-cell biocatalysts at high lysine concentration. Consumption of 91% lysine and conversion of about 80% lysine to cadaverine at 0.025 mM pyridoxal 5'-phosphate and 1.75 M lysine in 500 mM sodium acetate buffer, pH 6.0
-
-
?
additional information
?
-
Escherichia coli K-12 / MG1655
evaluation of a simple assay method, a colorimetric assay with pH indicator, applied for monitoring and quantifying the liquid-based enzyme reaction in biotransformation of decarboxylase in a high-throughput way, modification of a pH indicator-based assay on solid agar medium
-
-
?
additional information
?
-
whole-cell bioconversion by Klebsiella pneumoniae lysine decaarboxylase LdcC is markedly lower than that of Klebsiella pneumoniae lysine decarboxylase CadA in Klebsiella pneumoniae cells and in transformed Escherichia coli cells
-
-
?
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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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-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
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-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
Klebsiella aerogenes ATCC 13048 / DSM 30053 / JCM 1235 / KCTC 2190 / NBRC 13534 / NCIMB 10102 / NCTC 10006
-
-
-
?
L-lysine
cadaverine + CO2
Klebsiella oxytoca ATCC 8724 / DSM 4798 / JCM 20051 / NBRC 3318 / NRRL B-199 / KCTC 1686
-
-
-
?
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
?
-
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
?
-
Escherichia coli K-12 / MG1655
optimization of direct lysine decarboxylase biotransformation of lysine to cadaverine for cadaverine production with whole-cell biocatalysts at high lysine concentration. Consumption of 91% lysine and conversion of about 80% lysine to cadaverine at 0.025 mM pyridoxal 5'-phosphate and 1.75 M lysine in 500 mM sodium acetate buffer, pH 6.0
-
-
?
additional information
?
-
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
?
-
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
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
-
contains 1 mol of pyridoxal 5'-phosphate per mol of subunit
pyridoxal 5'-phosphate
Bacterium cadaveris
-
contains 10 mol of pyridoxal 5'-phosphate per mol of enzyme
pyridoxal 5'-phosphate
-
enzyme solution exhibits absorption maxima at 279 and 415 nm, and the ratio of absorbance value at 415 nm to that at 279 nm i 0.158
pyridoxal 5'-phosphate
dependent on, best at 0.025-0.1 mM in whole-cell assay
pyridoxal 5'-phosphate
PLP, binding structure and binding mode, overview. The highly flexible active site contributes to the low affinity for pyridoxal 5'-phosphate in SrLDC. The cofactor affinity is increased in enzyme mutant A225C/T302C due to introduction of an artificial disulfide bond
pyridoxal 5'-phosphate
PLP, binding structure and binding mode, overview. The PLP cofactor binds mainly to the pocket formed at the barrel domain, and the catalytic residue Lys51 interacts with the aldehyde group of the pyridoxal ring. The pyridine ring is stabilized by hydrogen bond between N1 of the ring and the acidic residue Glu255. The phosphate moiety of PLP is mainly stabilized by strong hydrogen bonds with the side-chains of His179, Ser182, and Tyr352, and the main chains of Gly219, Gly257, and Arg258 are also involved in the stabilization of the moiety
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
PCMB
Bacterium cadaveris
-
inhibition is eliminated by addition of 2-mercaptoethanol or glutathione, and pyridoxal 5'-phosphate
cadaverine
competitive inhibition mechanism, 90% inhibition at 10 mM
ppGpp
addition of ppGpp at low salt concentrations (25-135 mM NaCl depending on the buffer) results in a dramatic inhibition of LdcI activity of about 10fold at pH values higher than 5.0
ppGpp
-
LdcI activity is strongly inhibited by the binding of ppGpp. The RavA-LdcI interaction reduces the inhibition of LdcI activity by ppGpp in vitro as well as in vivo
additional information
Bacterium cadaveris
-
at 30°C the presence of L-Arg has little effect on the activity of the enzyme
-
additional information
Bacterium cadaveris
-
inhibitory effect of organophosphate esters (OPEs) with aromatic, alkyl or chlorinated alkyl substituents on the activity of lysine decarboxylase (LDC) is assessed quantitatively with an economic and label-free fluorescence sensor and cell assay. Molecular docking analysis of the LDC/OPE complexes reveals that different binding modes contribute to the difference in their inhibitory effect. No inhibition by tris(2-ethylhexyl) phosphate, tributoxyethyl phosphate, tri-n-butyl phosphate, tri-n-propyl phosphate, triethyl phosphate, and trimethyl phosphate. In vivo cytotoxic effect of the compounds in Rattus norvegicus PC-12 cells, overview
-
additional information
at pH values lower than 5.0, there is no effect of ppGpp, pppGpp, GDP and GTP on LdcI activity
-
additional information
-
at pH values lower than 5.0, there is no effect of ppGpp, pppGpp, GDP and GTP on LdcI activity
-
additional information
enzyme LdcC shows no or poor substrate inhibition by L-lysine
-
additional information
enzyme LdcC shows no or poor substrate inhibition by L-lysine
-
additional information
-
enzyme LdcC shows no or poor substrate inhibition by L-lysine
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
RpoS is not required either for induction of the cadBA operon or for activity of the Cad system in Escherichia coli starved of phosphate
-
additional information
the enzyme is encoded in an acid-induced operon
-
additional information
-
the enzyme is encoded in an acid-induced operon
-
additional information
-
the enzyme is upregulated by CadC in response to acid stress, and is also induced by SoxR in response to superoxide stress, SoxR binds directly to the promoter region of the cadBA operon, coding for a lysine-cadaverine antiporter, CadB, and the lysine decarboxylase CadA
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Breast Neoplasms
Cadaverine, a metabolite of the microbiome, reduces breast cancer aggressiveness through trace amino acid receptors.
Breast Neoplasms
Fecal expression of Escherichia coli lysine decarboxylase (LdcC) is downregulated in E-cadherin negative lobular breast carcinoma.
Gastroenteritis
An outbreak of acute gastroenteritis due to Aeromonas sobria in Benghazi, Libyan Arab Jamahiriya.
Gastroenteritis
[Lysine decarboxylase from E. coli serotypes isolated from' gastroenteritis in infants.]
Gingivitis
Bacterial Lysine Decarboxylase Influences Human Dental Biofilm Lysine Content, Biofilm Accumulation and Sub-Clinical Gingival Inflammation.
Gingivitis
Effects of immunization with natural and recombinant lysine decarboxylase on canine gingivitis development.
Hemolytic-Uremic Syndrome
Biochemical and molecular characterization of minor serogroups of Shiga toxin-producing Escherichia coli isolated from humans in Osaka prefecture.
Infections
Outbreak Caused by cad-Negative Shiga Toxin-Producing Escherichia coli O111, Oklahoma.
Intestinal Diseases
Resolving the Contradictory Functions of Lysine Decarboxylase and Butyrate in Periodontal and Intestinal Diseases.
Periodontal Diseases
CE-LIF determination of salivary cadaverine and lysine concentration ratio as an indicator of lysine decarboxylase enzyme activity.
Periodontal Diseases
Identification of lysine decarboxylase as a mammalian cell growth inhibitor in Eikenella corrodens: possible role in periodontal disease.
Typhoid Fever
Typhoid fever caused by a negative lysine decarboxylase Salmonella typhi strain in two patients from Distrito Federal, Brazil.
Whooping Cough
A LONELY GUY protein of Bordetella pertussis with unique features is related to oxidative stress.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
3.3
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
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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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.5
L-Lys
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D/S322A
19
L-Lys
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D/S322T/I326L
146.4
L-lysine
pH 5.6, 45°C, recombinant His6-tagged wild-type enzyme
149.3
L-lysine
pH 5.6, 45°C, recombinant His6-tagged mutant F14C/K44C
172.1
L-lysine
pH 5.6, 45°C, recombinant His6-tagged mutant F14C/K44C/L7M/N8G
3 - 6
L-Orn
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D/S322T/I326L
4.8
L-Orn
pH 6.0, 30°C, mutant enzyme A44V/G45T/V46P/P54D/S322A
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
112.3
L-lysine
pH 5.6, 45°C, recombinant His6-tagged mutant F14C/K44C
117.1
L-lysine
pH 5.6, 45°C, recombinant His6-tagged mutant F14C/K44C/L7M/N8G
120.1
L-lysine
pH 5.6, 45°C, recombinant His6-tagged wild-type enzyme
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0175
DL-alpha-Difluoromethyllysine
pH 6.0, 40°C, reaction with L-Lys
0.028
DL-alpha-Difluoromethyllysine
pH 6.0, 40°C, reaction with L-Orn
0.00525
DL-alpha-difluoromethylornithine
pH 6.0, 40°C, reaction with L-Lys
0.0082
DL-alpha-difluoromethylornithine
pH 6.0, 40°C, reaction with L-Orn
0.0002377
ppGpp
uncompetitive inhibition, at pH 6.5, between 4°C and 10°C
0.000374
ppGpp
noncompetitive inhibition, at pH 6.5, between 4°C and 10°C
0.002791
ppGpp
mixed type inhibition, at pH 6.5, between 4°C and 10°C
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
205.1
purified recombinant enzyme, pH 7.5, 37°C, substrate L-lysine
94.1
purified recombinant enzyme, pH 8.5, 37°C, substrate L-lysine
additional information
additional information
lysine decarboxylase-dependent acid-tolerance assays, overview
additional information
-
lysine decarboxylase-dependent acid-tolerance assays, overview
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 7.5
-
assay at, transcription of cadBA in a pH-dependent manner, overview
5.5
5.6
6.2 - 8
7.5
8 - 8.5
recombinant enzyme inclusion bodies, EcLDCc-CatIBs, the activity is dependent on the medium
additional information
6
recombinant immobilized enzyme CadACLEA and recombinant free enzyme CadAfree
additional information
survival of acid adapted and nonadpted strains at pH 5.5 and pH 7.5, 30°C, overview
additional information
-
survival of acid adapted and nonadpted strains at pH 5.5 and pH 7.5, 30°C, overview
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 7
-
pH 4.5: about 35% of maximal activity, pH 7.0: about 60% of maximal activity
4.5 - 8
-
pH 4.5: about 30% of maximal activity, pH 8: about 35% of maximal activity
5.5 - 8
maximal activity at pH 5.5, 30% of maximal activity at pH 8.0
6.2 - 8.8
soluble wild-type enzyme, maximal activity at pH 6.2-8.0, 30% of maximal activity at pH 8.8
7 - 8
-
pH 7.0: about 70% of maximal activity, pH 9.0: about 25% of maximal activity
7.5 - 9
recombinant enzyme inclusion bodies, EcLDCc-CatIBs, range of higher activity
8 - 9
-
enzyme gtLDC does not exhibit effective activity in alkaline pH conditions, the conversion rate of about 8% is similar at pH 8.0 and pH 9.0, no activity at pH 10.0
additional information
additional information
CadA is rapidly inactivated as the pH increases during the decarboxylation of lysine because it has an acidic optimum pH 5.0-6.0
additional information
CadA is rapidly inactivated as the pH increases during the decarboxylation of lysine because it has an acidic optimum pH 5.0-6.0
additional information
-
CadA is rapidly inactivated as the pH increases during the decarboxylation of lysine because it has an acidic optimum pH 5.0-6.0
additional information
the cadaverine conversion rate is negatively affected at above pH 9
additional information
-
the cadaverine conversion rate is negatively affected at above pH 9
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
37
50
55
60
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 50
recombinant enzyme, over 50% of maximal activity within this range, profile overview
20 - 70
activity profiles of recombinant immobilized enzyme CadACLEA and recombinant free enzyme CadAfree
20 - 80
-
20°C: about 25% of maximal activity, 80°C: about 95% of maximal activity
30 - 41
-
30°C: 38% of maximal activity, 37°C: 71% of maximal activity, 41°C: optimum
40 - 70
-
40°C: about 40% of maximal activity, 70°C: about 90% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Escherichia coli K-12 / MG1655
Klebsiella aerogenes ATCC 13048 / DSM 30053 / JCM 1235 / KCTC 2190 / NBRC 13534 / NCIMB 10102 / NCTC 10006
i.e. Enterobacter aerogenes
UniProt
brenda
Klebsiella oxytoca ATCC 8724 / DSM 4798 / JCM 20051 / NBRC 3318 / NRRL B-199 / KCTC 1686
-
UniProt
brenda
all of the detectable lysine decarboxylase activity is due to the action of ornithine decarboxylase
-
-
brenda
no activity in Rattus norvegicus
all of the detectable lysine decarboxylase activity is due to the action of ornithine decarboxylase
-
-
brenda
2 enzyme form, one is encoded by the gen cadA and the other by the gene ldc
-
-
brenda
several acid adapted and nonadapted strains, gene cadA or VP2890
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
drastic descent of enzyme activity owing to degradation of LDC at entry into the stationary phase of cell growth
brenda
additional information
-
no appreciable activity is detected in cotyledons and shoots
brenda
additional information
-
LDC activity in healthy, aphid-damaged, or healthy parts of the damaged leaves is highest at the initial phase, especially in galls. The enzyme activity drops after the initial stage. Activity profile overview
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
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
physiological function
additional information
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
-
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
-
structure of enzyme SrLDC in complex with pyridoxal 5'-phosphate and cadaverine and binding mode of cofactor and substrate, overview
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
additional information
Escherichia coli K-12 / MG1655
-
optimization of the EcLdcC-catalyzed whole-cell biotransformation, overview
-
additional information
Hafnia alvei AS1.1009
-
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
-
Show AA Sequence and Transmembrane Helices (2074 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80000
88000
80000
-
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
80000
-
? * 80000, SDS-PAGE, under native conditions aggregation of up to 10 subunits
80000
-
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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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decamer
dimer
heptamer
hexamer
homodecamer
homodimer
tetramer
additional information
?
-
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
?
Escherichia coli B / ATCC 11303
-
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
-
?
Escherichia coli B / ATCC 11303
-
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
-
?
-
? * 80000, SDS-PAGE, under native conditions aggregation of up to 10 subunits
?
Klebsiella oxytoca ATCC 8724 / DSM 4798 / JCM 20051 / NBRC 3318 / NRRL B-199 / KCTC 1686
-
x * 80000, recombinant enzyme
-
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
homodecamer
a pentamer of homodimers, 10 * 82000, recombinant His6-tagged wild-type enzyme, SDS-PAGE
homodecamer
Escherichia coli K-12 / B
-
a pentamer of homodimers, 10 * 82000, recombinant His6-tagged wild-type enzyme, SDS-PAGE
-
homodimer
2 * 44000, recombinant His-tagged enzyme, SDS-PAGE
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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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
cage-like complex of about 3.3 MDa consisting of two LdcI (81 kDa) decamers and up to five RavA (56 kDa) hexamers, hanging drop vapor diffusion method, using
-
hanging drop vapour diffusion method, with 18-28% (w/v) PEG 1000, 100 mM NaCl, 100 mM Tris-HCl pH 8.5, 15% (v/v) glycerol, 5 mM tris(2-carboxyethyl)phospine hydrochloride
purified recombinant His6-tagged enzyme, mixing 0.001 ml of 65 mg/ml protein in 40 mM Tris-HCl, pH 8.0, with 0.001 ml of reservoir solution, containing 28% w/v PEG 400, 0.1 M sodium citrate tribasic-citric acid, pH 6.0, and 0.2 M MgCl2, and equilibration against 0.5 ml of reservoir solution, 20°C, the apo-form II crystals of SrLDC are crystallized using a reservoir solution containing 1.15 M sodium citrate and 0.1 M sodium cacodylate, pH 5.0. The crystals of SrLDC complexed with PLP/cadaverine are crystallized using 50% PEG 200, 0.1 M sodium phosphate, pH 4.2, 0.2 M sodium chloride, and 5 mM PLP, followed by soaking in 10 mM L-lysine solution for 30 min, X-ray diffraction structure determination and analysis at 2.0-2.9 A resolution, molecular replacement with the structure of L/ODC from Vibrio vulnificus (VvL/ODC, PDB ID 2PLK) as search model, model building
purified SrLDCA225C/T302C mutant, hanging drop vapour diffusion method, mixing of 0.001 ml of 65 mg/ml protein in 40 mM Tris-HCl, pH 8.0, with 0.001 ml of reservoir solution containing 1.4 M ammonium sulfate, 0.1 M sodium cacodylate, pH 6.5, and 0.2 M sodium chloride, and equilibration against 0.5 ml of reservoir solution, 20°C, X-ray diffraction structure determination and analysis at 1.8 A resolution, molecular replacement using the structure of refined SrLDC as a model, model building
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
F14C/K44C
site-directed mutagenesis, mutant B1, the disulfide bond mutation in the decameric interface of wild-type CadA improves its structural stability, and as a result, enhances the pH and thermal stabilities along with organic solvent tolerance, but reduces the catalytic efficiency, compared to the wild-type
F14C/K44C/L7M/N8G
site-directed mutagenesis, the disulfide bond mutation in the decameric interface of wild-type CadA improves its structural stability, and as a result, enhances the pH and thermal stabilities along with organic solvent tolerance compared to the wild-type, addition of mutations L7M and N8G to mutant B1 slightly increases the catalytic efficiency compared to mutant B1 but remains still lower than wild-type
L89R
the mutant elutes at the expected position for an LdcI dimer (about 150000 Da), the mutant shows about 5fold lower level of activity than wild type and this activity is not inhibited by ppGpp
R206S
the ppGpp-binding site mutant shows wild type oligomerisation profile, the mutant is insensitive to the addition of ppGpp and has activity comparable to wild type LdcI in the absence of ppGpp
R97A
the ppGpp-binding site mutant shows wild type oligomerisation profile, the mutant is insensitive to the addition of ppGpp and has activity comparable to wild type LdcI in the absence of ppGpp
T88D
site-directed mutagenesis, the mutant shows decreased thermostability compared to the wild-type enzyme
T88F
site-directed mutagenesis, the mutant shows increased thermostability compared to the wild-type enzyme
T88N
site-directed mutagenesis, the mutant is expressed in inclusion bodies and shows no clear activity
T88P
site-directed mutagenesis, the mutant is expressed in inclusion bodies and shows no clear activity
T88Q
site-directed mutagenesis, the mutant is expressed in inclusion bodies and shows no clear activity
T88S
site-directed mutagenesis, the mutant shows higher thermostability with a 2.9fold increase in the half-life at 70°C (from 11 min to 32 min) and increased melting temperature (from 76°C to 78°C). The specific activity and pH stability of T88S at pH 8.0 are increased to 164 U/mg and 78% compared to 58 U/mg and 57% for the wild-type enzyme. The productivity of cadaverine with T88S is 40 g/l/h in contrast to 28 g/l/h with wild-type enzyme. The mutant is a promising biocatalyst for industrial production of cadaverine. No additional hydrogen bond is formed when T88 is substituted by D, F, or S, and the improved stability may be attributed to the favorable atom and torsion angle potentials
F14C/K44C
Escherichia coli K-12 / B
-
site-directed mutagenesis, mutant B1, the disulfide bond mutation in the decameric interface of wild-type CadA improves its structural stability, and as a result, enhances the pH and thermal stabilities along with organic solvent tolerance, but reduces the catalytic efficiency, compared to the wild-type
-
F14C/K44C/L7M/N8G
Escherichia coli K-12 / B
-
site-directed mutagenesis, the disulfide bond mutation in the decameric interface of wild-type CadA improves its structural stability, and as a result, enhances the pH and thermal stabilities along with organic solvent tolerance compared to the wild-type, addition of mutations L7M and N8G to mutant B1 slightly increases the catalytic efficiency compared to mutant B1 but remains still lower than wild-type
-
E583G
-
site-directed mutagenesis, the mutant shows 1.32fold increased LDC activity and 1.48fold improved productivity of cadaverine compared to wild-type enzyme
V147F/E583G
-
site-directed mutagenesis, the mutant shows 1.62fold increased LDC activity compared to wild-type enzyme
E583G
Hafnia alvei AS1.1009
-
site-directed mutagenesis, the mutant shows 1.32fold increased LDC activity and 1.48fold improved productivity of cadaverine compared to wild-type enzyme
-
V147F/E583G
Hafnia alvei AS1.1009
-
site-directed mutagenesis, the mutant shows 1.62fold increased LDC activity compared to wild-type enzyme
-
A225C/T302C
site-directed mutagenesis, due to high flexibility at the pyridoxal 5'-phosphate (PLP) binding site, use of the enzyme for cadaverine production requires continuous supplement of large amounts of PLP. In order to develop an LDC enzyme from Selenomonas ruminantium (SrLDC) with an enhanced affinity for PLP, an internal disulfide bond between Ala225 and Thr302 residues is introduced with a desire to retain the PLP binding site in a closed conformation. The SrLDCA225C/T302C mutant shows bound PLP, and exhibits 3fold enhanced PLP affinity compared with the wild-type SrLDC. The mutant also exhibits a dramatically enhanced LDC activity and cadaverine conversion particularly under no or low PLP concentrations. Introduction of the disulfide bond renders mutant SrLDC more resistant to high pH and temperature. The formation of the introduced disulfide bond and the maintenance of the PLP binding site in the closed conformation are confirmed by determination of the crystal structure of the mutant. Mutant structure determination and analysis, overview. The mutant shows increased affinity for pyridoxal 5'-phosphate and increased activity compared to wild-type
A44V/G45T/V46P
A44V/G45T/V46P/P54D
the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 3.8, compared to 0.83 for the wild-type enzyme
A44V/G45T/V46P/P54D/S322A
the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 58, compared to 0.83 for the wild-type enzyme
A44V/G45T/V46P/P54D/S322T/I326L
the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 13, compared to 0.83 for the wild-type enzyme
A52C
A52C/P54D
A52C/P54D/T55S
-
the ratio of activity with L-Orn to activity with L-Lys is 2.7, compared to 0.69 for the wild-type enzyme
G319W
the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 3.9, compared to 0.83 for the wild-type enzyme
K2C/G227C
site-directed mutagenesis, the mutant shows reduced affinity for pyridoxal 5'-phosphate and reduced activity compared to wild-type
M50V
-
the ratio of activity with L-Orn to activity with L-Lys is 0.64, compared to 0.69 for the wild-type enzyme
M50V/A52C
-
the ratio of activity with L-Orn to activity with L-Lys is 1.9, compared to 0.69 for the wild-type enzyme
M50V/A52C/P54D
-
the ratio of activity with L-Orn to activity with L-Lys is 2.4, compared to 0.69 for the wild-type enzyme
M50V/A52C/P54D/T55S
P54D
P54D/T55S
-
the ratio of activity with L-Orn to activity with L-Lys is 1.8, compared to 0.69 for the wild-type enzyme
S322A
the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 24, compared to 0.83 for the wild-type enzyme
S322T/I326L
the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 13, compared to 0.83 for the wild-type enzyme
T55S
-
the ratio of activity with L-Orn to activity with L-Lys is 0.66, compared to 0.69 for the wild-type enzyme
additional information
A44V/G45T/V46P
-
the ratio of activity with L-Orn to activity with L-Lys is 1.0, compared to 0.69 for the wild-type enzyme
A44V/G45T/V46P
the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 2.0, compared to 0.83 for the wild-type enzyme
A52C
-
the ratio of activity with L-Orn to activity with L-Lys is 1.2, compared to 0.69 for the wild-type enzyme
A52C
the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 1.0, compared to 0.83 for the wild-type enzyme
A52C/P54D
-
the ratio of activity with L-Orn to activity with L-Lys is 2.6, compared to 0.69 for the wild-type enzyme
A52C/P54D
the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 1.6, compared to 0.83 for the wild-type enzyme
M50V/A52C/P54D/T55S
-
the ratio of activity with L-Orn to activity with L-Lys is 4.0, compared to 0.69 for the wild-type enzyme
M50V/A52C/P54D/T55S
the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 1.5, compared to 0.83 for the wild-type enzyme
P54D
-
the ratio of activity with L-Orn to activity with L-Lys is 1.8, compared to 0.69 for the wild-type enzyme
P54D
the ratio of turnover number to Km-value obtained with L-Orn relative to that obtained with L-Lys as substrate is 2.2, compared to 0.83 for the wild-type enzyme
additional information
when used for whole-cell biotransformation of L-lysine to cadaverine at pH 7.5, 37°C, recombinant AsLdc in Escherichia coli cells completes the transformation within 7 h, method optimiztaion and comprisons, overview
additional information
cadaverine is a major source of many industrial polyamides such as nylon and chelating agents. Cadaverine is produced by the microbial fermentation of glucose to lysine, which is then decarboxylated by lysine decarboxylase CadA. But utilizing CadA for cadaverine production causes enzyme instability. In order to stabilize the CadA homodecamer structure for in vitro decarboxylation reaction, four disulfide bond mutants in the multimeric interfacial region are designed, CadA plasmid library/mutant screening
additional information
development of an innovative immobilisation approach using catalytically active recombinant constitutive L-lysine decarboxylase (EcLDCc) in inclusion bodies, CatIBs, overview. EcLDCc-CatIBs can compete with the whole cell biocatalyst in production of cadaverine
additional information
-
development of an innovative immobilisation approach using catalytically active recombinant constitutive L-lysine decarboxylase (EcLDCc) in inclusion bodies, CatIBs, overview. EcLDCc-CatIBs can compete with the whole cell biocatalyst in production of cadaverine
additional information
engineering the decameric interface for potential for industrial applications
additional information
-
engineering the decameric interface for potential for industrial applications
additional information
immobilization of the recombinant enzyme CadA, preparation of a cross-linked enzyme aggregate (CLEA) of Escherichia coli CadA and bioconversion of lysine using CadACLEA. The thermostability of CadACLEA is significantly higher than that of CadAfree. The optimum temperatures of CadAfree and CadACLEA are 60°C and 55°C, respectively. The thermostability of CadACLEA is significantly higher than that of CadAfree. The optimum pH of both enzymes is 6.0. CadAfree cannot be recovered after use, whereas CadACLEA is rapidly recovered and the residual activity is 53% after the 10th recycle
additional information
optimization of direct lysine decarboxylase biotransformation of lysine to cadaverine for cadaverine production with whole-cell biocatalysts at high lysine concentration. Consumption of 91% lysine and conversion of about 80% lysine to cadaverine at 0.025 mM pyridoxal 5'-phosphate and 1.75 M lysine in 500 mM sodium acetate buffer, pH 6.0
additional information
-
optimization of direct lysine decarboxylase biotransformation of lysine to cadaverine for cadaverine production with whole-cell biocatalysts at high lysine concentration. Consumption of 91% lysine and conversion of about 80% lysine to cadaverine at 0.025 mM pyridoxal 5'-phosphate and 1.75 M lysine in 500 mM sodium acetate buffer, pH 6.0
additional information
recombinant Escherichia coli-overexpressing CadA produces cadaverine from crude L-lysine solution. Constitutive lysine decarboxylase EcLdcC retains a higher cadaverine yield after being reused 10 times at acidic and alkaline pH values than that of a recombinant Escherichia coli strain overexpressing the inducible lysine carboxylase CadA, the conventional cadaverine producer. Although the soluble expression level of LdcC in Escherichia coli is less than that of CadA, LdcC is active over a broader pH range (pH 5-9) and exhibits less substrate inhibition than CadA, indicating that LdcC is a more suitable biocatalyst than CadA for the direct synthesis of cadaverine from highly concentrated lysine
additional information
recombinant Escherichia coli-overexpressing CadA produces cadaverine from crude L-lysine solution. Constitutive lysine decarboxylase EcLdcC retains a higher cadaverine yield after being reused 10 times at acidic and alkaline pH values than that of a recombinant Escherichia coli strain overexpressing the inducible lysine carboxylase CadA, the conventional cadaverine producer. Although the soluble expression level of LdcC in Escherichia coli is less than that of CadA, LdcC is active over a broader pH range (pH 5-9) and exhibits less substrate inhibition than CadA, indicating that LdcC is a more suitable biocatalyst than CadA for the direct synthesis of cadaverine from highly concentrated lysine
additional information
-
recombinant Escherichia coli-overexpressing CadA produces cadaverine from crude L-lysine solution. Constitutive lysine decarboxylase EcLdcC retains a higher cadaverine yield after being reused 10 times at acidic and alkaline pH values than that of a recombinant Escherichia coli strain overexpressing the inducible lysine carboxylase CadA, the conventional cadaverine producer. Although the soluble expression level of LdcC in Escherichia coli is less than that of CadA, LdcC is active over a broader pH range (pH 5-9) and exhibits less substrate inhibition than CadA, indicating that LdcC is a more suitable biocatalyst than CadA for the direct synthesis of cadaverine from highly concentrated lysine
additional information
recombinant Escherichia coli-overexpressing LdcC (EcLdcC) produces cadaverine from crude L-lysine solution. EcLdcC retains a higher cadaverine yield after being reused 10 times at acidic and alkaline pH values than that of a recombinant Escherichia coli strain overexpressing an inducible lysine carboxylase (CadA), a conventional cadaverine producer. Although the soluble expression level of LdcC in Escherichia coli is less than that of CadA, LdcC is active over a broader pH range (pH 5-9) and exhibits less substrate inhibition than CadA, indicating that LdcC is a more suitable biocatalyst than CadA for the direct synthesis of cadaverine from highly concentrated lysine. Optimization of the EcLdcC-catalyzed whole-cell biotransformation, overview
additional information
recombinant Escherichia coli-overexpressing LdcC (EcLdcC) produces cadaverine from crude L-lysine solution. EcLdcC retains a higher cadaverine yield after being reused 10 times at acidic and alkaline pH values than that of a recombinant Escherichia coli strain overexpressing an inducible lysine carboxylase (CadA), a conventional cadaverine producer. Although the soluble expression level of LdcC in Escherichia coli is less than that of CadA, LdcC is active over a broader pH range (pH 5-9) and exhibits less substrate inhibition than CadA, indicating that LdcC is a more suitable biocatalyst than CadA for the direct synthesis of cadaverine from highly concentrated lysine. Optimization of the EcLdcC-catalyzed whole-cell biotransformation, overview
additional information
-
recombinant Escherichia coli-overexpressing LdcC (EcLdcC) produces cadaverine from crude L-lysine solution. EcLdcC retains a higher cadaverine yield after being reused 10 times at acidic and alkaline pH values than that of a recombinant Escherichia coli strain overexpressing an inducible lysine carboxylase (CadA), a conventional cadaverine producer. Although the soluble expression level of LdcC in Escherichia coli is less than that of CadA, LdcC is active over a broader pH range (pH 5-9) and exhibits less substrate inhibition than CadA, indicating that LdcC is a more suitable biocatalyst than CadA for the direct synthesis of cadaverine from highly concentrated lysine. Optimization of the EcLdcC-catalyzed whole-cell biotransformation, overview
additional information
Escherichia coli K-12 / B
-
cadaverine is a major source of many industrial polyamides such as nylon and chelating agents. Cadaverine is produced by the microbial fermentation of glucose to lysine, which is then decarboxylated by lysine decarboxylase CadA. But utilizing CadA for cadaverine production causes enzyme instability. In order to stabilize the CadA homodecamer structure for in vitro decarboxylation reaction, four disulfide bond mutants in the multimeric interfacial region are designed, CadA plasmid library/mutant screening
-
additional information
Escherichia coli K-12 / MG1655
-
recombinant Escherichia coli-overexpressing CadA produces cadaverine from crude L-lysine solution. Constitutive lysine decarboxylase EcLdcC retains a higher cadaverine yield after being reused 10 times at acidic and alkaline pH values than that of a recombinant Escherichia coli strain overexpressing the inducible lysine carboxylase CadA, the conventional cadaverine producer. Although the soluble expression level of LdcC in Escherichia coli is less than that of CadA, LdcC is active over a broader pH range (pH 5-9) and exhibits less substrate inhibition than CadA, indicating that LdcC is a more suitable biocatalyst than CadA for the direct synthesis of cadaverine from highly concentrated lysine
-
additional information
Escherichia coli K-12 / MG1655
-
optimization of direct lysine decarboxylase biotransformation of lysine to cadaverine for cadaverine production with whole-cell biocatalysts at high lysine concentration. Consumption of 91% lysine and conversion of about 80% lysine to cadaverine at 0.025 mM pyridoxal 5'-phosphate and 1.75 M lysine in 500 mM sodium acetate buffer, pH 6.0
-
additional information
Escherichia coli K-12 / MG1655
-
recombinant Escherichia coli-overexpressing LdcC (EcLdcC) produces cadaverine from crude L-lysine solution. EcLdcC retains a higher cadaverine yield after being reused 10 times at acidic and alkaline pH values than that of a recombinant Escherichia coli strain overexpressing an inducible lysine carboxylase (CadA), a conventional cadaverine producer. Although the soluble expression level of LdcC in Escherichia coli is less than that of CadA, LdcC is active over a broader pH range (pH 5-9) and exhibits less substrate inhibition than CadA, indicating that LdcC is a more suitable biocatalyst than CadA for the direct synthesis of cadaverine from highly concentrated lysine. Optimization of the EcLdcC-catalyzed whole-cell biotransformation, overview
-
additional information
-
directed evolution of LDC and high-throughput mutant screening, mutant library construction using DNA shuffling or error-prone PCR (optimum concentrations of Mn2+ and Mg2+ are 5 and 0.2 mM, respectively). Three nucleotide mutations, A438G, G439T, and A1748G correspond to amino acid changes V147F and E583G
additional information
Hafnia alvei AS1.1009
-
directed evolution of LDC and high-throughput mutant screening, mutant library construction using DNA shuffling or error-prone PCR (optimum concentrations of Mn2+ and Mg2+ are 5 and 0.2 mM, respectively). Three nucleotide mutations, A438G, G439T, and A1748G correspond to amino acid changes V147F and E583G
-
additional information
whole-cell bioconversion by Klebsiella pneumoniae lysine decarboxylase LdcC is markedly lower than that of Klebsiella pneumoniae lysine decaarboxylase CadA in Klebsiella pneumoniae cells and in transformed Escherichia coli cells
additional information
whole-cell bioconversion by Klebsiella pneumoniae lysine decarboxylase LdcC is markedly lower than that of Klebsiella pneumoniae lysine decaarboxylase CadA in Klebsiella pneumoniae cells and in transformed Escherichia coli cells
additional information
whole-cell bioconversion by Klebsiella pneumoniae lysine decarboxylase LdcC is markedly lower than that of Klebsiella pneumoniae lysine decarboxylase CadA in Klebsiella pneumoniae cells and in transformed Escherichia coli cells
additional information
whole-cell bioconversion by Klebsiella pneumoniae lysine decarboxylase LdcC is markedly lower than that of Klebsiella pneumoniae lysine decarboxylase CadA in Klebsiella pneumoniae cells and in transformed Escherichia coli cells
additional information
Klebsiella aerogenes ATCC 13048 / DSM 30053 / JCM 1235 / KCTC 2190 / NBRC 13534 / NCIMB 10102 / NCTC 10006
-
whole-cell bioconversion by Klebsiella pneumoniae lysine decarboxylase LdcC is markedly lower than that of Klebsiella pneumoniae lysine decarboxylase CadA in Klebsiella pneumoniae cells and in transformed Escherichia coli cells
-
additional information
-
biotransformation of cadaverine using a lysine decarboxylase from Klebsiella oxytoca expressed in Escherichia coli. Codon optimization of the gene encoding the enzyme is carried on for the heterologous expression in Escherichia coli, which leads to a system that converts more than 24% lysine-HCl to cadaverine compared to the same system expressing CadA, overview. The final optimized system converts lysine-HCl to cadaverine at a conversion rate of 0.133%/min/g
additional information
-
identification of mutant Ldc-co with increased lysine decarboxylase ability. Codon optimization of the gene encoding the enzyme is carried on for the heterologous expression in Escherichia coli. Identification of mutant lysine decarboxylase enzymes with enhanced cadaverine-production ability. Together, these modifications increase cadaverine production in the system by 50%, and the system has a yield of 80% from lysine-HCl, the system to produce cadaverine using the lysine decarboxylase from Klebsiella oxytoca performs at a level that is competitive with the traditional systems using the Escherichia coli lysine decarboxylases in both lab-scale and batch fermentation conditions. Generation of several mutant strains and evaluation, overview
additional information
Klebsiella oxytoca DSM 6673
-
biotransformation of cadaverine using a lysine decarboxylase from Klebsiella oxytoca expressed in Escherichia coli. Codon optimization of the gene encoding the enzyme is carried on for the heterologous expression in Escherichia coli, which leads to a system that converts more than 24% lysine-HCl to cadaverine compared to the same system expressing CadA, overview. The final optimized system converts lysine-HCl to cadaverine at a conversion rate of 0.133%/min/g
-
additional information
Klebsiella oxytoca DSM 6673
-
identification of mutant Ldc-co with increased lysine decarboxylase ability. Codon optimization of the gene encoding the enzyme is carried on for the heterologous expression in Escherichia coli. Identification of mutant lysine decarboxylase enzymes with enhanced cadaverine-production ability. Together, these modifications increase cadaverine production in the system by 50%, and the system has a yield of 80% from lysine-HCl, the system to produce cadaverine using the lysine decarboxylase from Klebsiella oxytoca performs at a level that is competitive with the traditional systems using the Escherichia coli lysine decarboxylases in both lab-scale and batch fermentation conditions. Generation of several mutant strains and evaluation, overview
-
additional information
disulfide bond-mediated spatial reconstitution can be a platform technology for development of enzymes with enhanced pyridoxal 5'-phosphate affinity
additional information
-
disulfide bond-mediated spatial reconstitution can be a platform technology for development of enzymes with enhanced pyridoxal 5'-phosphate affinity
additional information
construction of a cadA gene-inactivated strain from wild-type strain V02-64, serotype O3:K, by a plasmid integrated in its chromosome, single crossing over, acid resistance of the mutant strain at pH 4.0 in phosphate buffer is weaker than in the parental strain
additional information
-
construction of a cadA gene-inactivated strain from wild-type strain V02-64, serotype O3:K, by a plasmid integrated in its chromosome, single crossing over, acid resistance of the mutant strain at pH 4.0 in phosphate buffer is weaker than in the parental strain
additional information
-
a lack of cadaverine caused by mutation in cadA results in low tolerance to oxidative stress compared to the wild type, cadaverine, which neutralizes the external medium, also appears to scavenge superoxide radicals, since increasing cellular cadaverine by elevating the gene dosage of cadBA significantly diminished the induction of Mn-containing superoxide dismutase under methyl viologen-induced oxidative stress, overview
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5
10 h at 37°C, about 80% activity remaining for the wild-type enzyme, and about 75% activity remaining for the recombinant His-tagged mutant T88S
747396
5.3
Bacterium cadaveris
-
crystalline enzyme is stable
37294
6
recombinant His-tagged wild-type enzyme, most stable at pH 6.0, over 90% activity remaining after 10 h at 37°C, about 85% activity remaining for the mutant T88S
747396
8.5
7
recombinant His-tagged mutant T88S, most stable at pH 7.0, over 90% activity remaining after 10 h at 37°C, about 60% activity remaining for the wild-type enzyme
747396
7
recombinant immobilized enzyme CadACLEA and recombinant free enzyme CadAfree, stable up to, 30 min, 37°C, inactivation above
748386
8.5
purified recombinant enzyme AsLdc, 10 h, 37°C, residual activity is 71%
748418
8.5
10 h at 37°C, about 40% activity remaining for the wild-type enzyme, and about 70% activity remaining for the recombinant His-tagged mutant T88S
747396
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
30 min, 50% loss of activity without pyridoxal-5'-phosphate
37
50
60
70
crude enzymes, half life for the wild-type enzyme is 11 min, the half-lives of T88 are: 21-32 min for T88S, 7 min for T88D, 12 min for T88F. after 50 min at 70°C, the wild-type enzyme is inactivated, while mutant T88S still shows 23.1% activity
80
37
purified recombinant enzyme AsLdc, 12 h, pH 7.5, residual activity is 96.3%
37
the recombinant immobilized enzyme CadACLEA and the recombinant free enzyme CadAfree show over 80% remaining activity after 5 h, pH 6.0
37
the recombinant immobilized enzyme CadACLEA shows about 60% remaining activity, and the recombinant free enzyme CadAfree shows below 10% remaining activity after 5 h, pH 6.0
50
purified recombinant enzyme AsLdc, 12 h, pH 7.5, residual activity is 75.2%
50
30 min, 50% loss of activity in presence of pyridoxal 5'-phosphate
60
-
5 min, 45% loss of activity, enzyme form encoded by the gene ldc. Enzyme form encoded by cadA is very stable after 15 min
60
-
pH 6.5, 0.1 mM pyridoxal 5'-phosphate, 30% loss of activity after 5 min. 90% loss of activity within 5 min, at pH 6.5 in absence of pyridoxal 5'-phosphate
80
purified recombinant enzyme AsLdc, 12 h, pH 7.5, residual activity is about 50%
80
purified recombinant His6-tagged wild-type enzyme, pH 5.6, 60% activity remaining
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
calcium alginate can completely entrap the enzyme while retaining activity and improving stability during operation and storage
Bacterium cadaveris
-
dithiothreitol is required for stabilization during purification and storage
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-80°C, stable for one month in presence of 20% glycerol, loss of activity within 2 weeks without glycerol
4°C, 0.01 M potassium phosphate buffer, pH 6.2, 0.01 mM pyridoxal 5'-phosphate, stable for several weeks
Bacterium cadaveris
-
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant C-terminally His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
-
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography
recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration
recombinant His-tagged enzyme from Escherichia coli strain Rosetta 2 (DE3) by nickel affinity chromatography, dialysis, and tag cleavage through TEV protease, followed by another step of nickel affinity chromatography, and gel filtration
recombinant His-tagged wild-type and mutant T88S from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration