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Information on EC 4.1.1.18 - lysine decarboxylase and Organism(s) Escherichia coli and UniProt Accession P0A9H3
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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
- aeromonas
-
dihydrolase
- decarboxylases
-
voges-proskauer
-
dna-dna
- esculin
-
non-motile
-
cadba
- salicin
- 1,5-diaminopentane
- d-mannitol
- melibiose
- dulcitol
- ruminantium
- adonitol
-
selenomonas
- sobria
-
enteroinvasive
- d-sorbitol
- carbenicillin
- cephalothin
- corrodens
-
simmons
- alvei
-
macconkey
-
quinolizidine
-
hafnia
- eikenella
- huperzia
- d-arabitol
-
4.1.1.17
- synthesis
- medicine
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
lysine decarboxylase, l-lysine decarboxylase, inducible lysine decarboxylase, srldc, maldc, ecldcc, ldci/cada, constitutive lysine decarboxylase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
LDC
LDC
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decarboxylation
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -, -, -, -, -, -, -
SYSTEMATIC NAME
IUBMB Comments
L-lysine carboxy-lyase (cadaverine-forming)
A pyridoxal-phosphate protein. Also acts on 5-hydroxy-L-lysine.
CAS REGISTRY NUMBER
COMMENTARY
9024-76-4
-
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
-
25% of the activity with L-Lys
-
-
?
S-Aminoethyl-L-Cys
1-Amino-2-(S-aminoethyl)mercaptoethane + CO2
-
15% of the activity with L-Lys
-
-
?
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
-
-
?
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
?
-
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
-
-
?
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-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
-
-
?
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
?
-
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
-
-
?
COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pyridoxal 5'-phosphate
dependent on, best at 0.025-0.1 mM in whole-cell assay
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
-
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Michaelis-Menten kinetics
-
1.47
L-lysine
pH 5.6, 45°C, recombinant His6-tagged mutant F14C/K44C/L7M/N8G
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.2 - 8
8 - 8.5
recombinant enzyme inclusion bodies, EcLDCc-CatIBs, the activity is dependent on the medium
6
recombinant immobilized enzyme CadACLEA and recombinant free enzyme CadAfree
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 8
-
pH 4.5: about 30% of maximal activity, pH 8: about 35% of maximal activity
6.2 - 8.8
soluble wild-type enzyme, maximal activity at pH 6.2-8.0, 30% of maximal activity at pH 8.8
7.5 - 9
recombinant enzyme inclusion bodies, EcLDCc-CatIBs, range of higher activity
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
55
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 70
activity profiles of recombinant immobilized enzyme CadACLEA and recombinant free enzyme CadAfree
40 - 70
-
40°C: about 40% of maximal activity, 70°C: about 90% of maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
physiological function
evolution
additional information
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
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
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
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
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
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
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80000
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
-
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
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
decamer
homodecamer
a pentamer of homodimers, 10 * 82000, recombinant His6-tagged wild-type enzyme, SDS-PAGE
homodecamer
additional information
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
?
-
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
additional information
three-dimensional structure analysis of enzyme CadA, overview
additional information
-
three-dimensional structure analysis of enzyme CadA, overview
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
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
-
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
additional information
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
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
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
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
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
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
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
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
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
purified recombinant His6-tagged wild-type enzyme, pH 5.6, 60% activity remaining
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
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
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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 wild-type and mutant enzymes 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
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene cadA, recombinant enzyme expression in Escherichia coli strain XL-1 Blue
gene cadA, recombinant expression of His-tagged wild-type and T88 mutants in Escherichia coli strain BL21(DE3), subcloning in Escherichia coli strain DH5alpha
gene cadA, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3)
gene cadA, recombinant induced expression of lysine decarboxylase in Escherichia coli strain BL21(DE3) for the high-level production of cadaverine from industrial grade L-lysine
gene ldcI, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta 2 (DE3)
gene ldcC, recombinant constitutive expression of lysine decarboxylase in Escherichia coli strain BL21(DE3) for the high-level production of cadaverine from industrial grade L-lysine
gene ldcC, recombinant expression in Escherichia coli strain BL21(DE3), optimization of conditions for enzyme overexpression, e.g. with respect to pH, cadaverine concentration, and IPTG concentration, overview
gene ldcC, recombinant overexpression in Escherichia coli strain BL21(DE3) in inclusion bodies with 3-10 mg/ml protein in batch cultivation. The aggregated enzyme EcLDCc-CatIBs is catalytically active
gene ldcI, sequence comparisons and phylogenetic analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta 2 (DE3)
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
synthesis
the enzyme EcLdcC can be used for whole-cell biotransformation (a whole-cell biocatalyst) using a constitutive lysine decarboxylase from Escherichia coli for the high-level production of cadaverine from industrial grade L-lysine. It is more effective in comparison to EcCadA. Cadaverine is used for synthesis of bio-polyamides
synthesis
the enzyme can be used for industrial production of cadaverine, especially mutant T88S is a promising biocatalyst
synthesis
the immobilized recombinant enzyme CadACLEA can be used as a potential catalyst for efficient production of cadaverine
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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Escherichia coli
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Lysine decarboxylase (Escherichia coli B)
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94
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Escherichia coli, Escherichia coli B / ATCC 11303
Sabo, D.L.; Fischer, E.H.
Chemical properties of Escherichia coli lysine decarboxylase including a segment of its pyridoxal 5 -phosphate binding site
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13
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Escherichia coli
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Purification and physical properties of inducible Escherichia coli lysine decarboxylase
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13
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Escherichia coli, Escherichia coli B / ATCC 11303
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Acta Crystallogr. Sect. F
64
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Escherichia coli (P0A9H3), Escherichia coli
Tateno, T.; Okada, Y.; Tsuchidate, T.; Tanaka, T.; Fukuda, H.; Kondo, A.
Direct production of cadaverine from soluble starch using Corynebacterium glutamicum coexpressing alpha-amylase and lysine decarboxylase
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82
115-121
2009
Escherichia coli
Kanjee, U.; Gutsche, I.; Alexopoulos, E.; Zhao, B.; El Bakkouri, M.; Thibault, G.; Liu, K.; Ramachandran, S.; Snider, J.; Pai, E.F.; Houry, W.A.
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30
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Escherichia coli (P0A9H3), Escherichia coli
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Structure of RavA MoxR AAA+ protein reveals the design principles of a molecular cage modulating the inducible lysine decarboxylase activity
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107
22499-22504
2010
Escherichia coli
Shin, J.; Joo, J.C.; Lee, E.; Hyun, S.M.; Kim, H.J.; Park, S.J.; Yang, Y.H.; Park, K.
Characterization of a whole-cell biotransformation using a constitutive lysine decarboxylase from Escherichia coli for the high-level production of cadaverine from industrial grade L-lysine
Appl. Biochem. Biotechnol.
185
909-924
2018
Escherichia coli (P0A9H3), Escherichia coli (P52095), Escherichia coli, Escherichia coli K-12 / MG1655 (P0A9H3), Escherichia coli K-12 / MG1655 (P52095)
Hong, E.Y.; Lee, S.G.; Park, B.J.; Lee, J.M.; Yun, H.; Kim, B.G.
Simultaneously enhancing the stability and catalytic activity of multimeric lysine decarboxylase CadA by engineering interface regions for enzymatic production of cadaverine at high concentration of lysine
Biotechnol. J.
12
1700278
2017
Escherichia coli (P0A9H3), Escherichia coli K-12 / B (P0A9H3)
Kou, F.; Zhao, J.; Liu, J.; Sun, C.; Guo, Y.; Tan, Z.; Cheng, F.; Li, Z.; Zheng, P.; Sun, J.
Enhancement of the thermal and alkaline pH stability of Escherichia coli lysine decarboxylase for efficient cadaverine production
Biotechnol. Lett.
40
719-727
2018
Escherichia coli (P0A9H3), Escherichia coli
Kim, H.J.; Kim, Y.H.; Shin, J.H.; Bhatia, S.K.; Sathiyanarayanan, G.; Seo, H.M.; Choi, K.Y.; Yang, Y.H.; Park, K.
Optimization of direct lysine decarboxylase biotransformation for cadaverine production with whole-cell biocatalysts at high lysine concentration
J. Microbiol. Biotechnol.
25
1108-1113
2015
Escherichia coli (P0A9H3), Escherichia coli, Escherichia coli K-12 / MG1655 (P0A9H3)
Kim, Y.H.; Sathiyanarayanan, G.; Kim, H.J.; Bhatia, S.K.; Seo, H.M.; Kim, J.H.; Song, H.S.; Kim, Y.G.; Park, K.; Yang, Y.H.
A Liquid-based colorimetric assay of lysine decarboxylase and its application to enzymatic assay
J. Microbiol. Biotechnol.
25
2110-2115
2015
Burkholderia thailandensis, Klebsiella aerogenes (A0A0H3FP92), Escherichia coli (P52095), Escherichia coli K-12 / MG1655 (P52095), Klebsiella aerogenes ATCC 13048 / DSM 30053 / JCM 1235 / KCTC 2190 / NBRC 13534 / NCIMB 10102 / NCTC 10006 (A0A0H3FP92)
Park, S.H.; Soetyono, F.; Kim, H.K.
Cadaverine production by using cross-linked enzyme aggregate of Escherichia coli lysine decarboxylase
J. Microbiol. Biotechnol.
27
289-296
2017
Escherichia coli (P0A9H3)
Kandiah, E.; Carriel, D.; Perard, J.; Malet, H.; Bacia, M.; Liu, K.; Chan, S.W.; Houry, W.A.; Ollagnier de Choudens, S.; Elsen, S.; Gutsche, I.
Structural insights into the Escherichia coli lysine decarboxylases and molecular determinants of interaction with the AAA+ ATPase RavA
Sci. Rep.
6
24601
2016
Escherichia coli (P0A9H3), Escherichia coli (P52095), Escherichia coli
Kloss, R.; Limberg, M.H.; Mackfeld, U.; Hahn, D.; Gruenberger, A.; Jaeger, V.D.; Krauss, U.; Oldiges, M.; Pohl, M.
Catalytically active inclusion bodies of L-lysine decarboxylase from E. coli for 1,5-diaminopentane production
Sci. Rep.
8
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Escherichia coli (P52095), Escherichia coli
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