BRENDA - Enzyme Database
show all sequences of 4.1.1.18

Lysine decarboxylase with an enhanced affinity for pyridoxal 5-phosphate by disulfide bond-mediated spatial reconstitution

Sagong, H.Y.; Kim, K.J.; PLoS ONE 12, e0170163 (2017)

Data extracted from this reference:

Application
Application
Commentary
Organism
synthesis
enzyme LDC plays a crucial role in the synthesis of cadaverine, an important industrial platform chemical. Cadaverine is utilized with a variety of applications such as the production of polyamides, polyurethanes, chelating agents, and additives
Selenomonas ruminantium
Cloned(Commentary)
Commentary
Organism
gene Srldc, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
Selenomonas ruminantium
Crystallization (Commentary)
Crystallization
Organism
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
Selenomonas ruminantium
Engineering
Amino acid exchange
Commentary
Organism
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
Selenomonas ruminantium
K2C/G227C
site-directed mutagenesis, the mutant shows reduced affinity for pyridoxal 5'-phosphate and reduced activity compared to wild-type
Selenomonas ruminantium
additional information
disulfide bond-mediated spatial reconstitution can be a platform technology for development of enzymes with enhanced pyridoxal 5'-phosphate affinity
Selenomonas ruminantium
KM Value [mM]
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetic analysis of wild-type and mutant enzymes
Selenomonas ruminantium
Natural Substrates/ Products (Substrates)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-lysine
Selenomonas ruminantium
-
cadaverine + CO2
-
-
?
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Selenomonas ruminantium
O50657
-
-
Purification (Commentary)
Commentary
Organism
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
Selenomonas ruminantium
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-lysine
-
749101
Selenomonas ruminantium
cadaverine + CO2
-
-
-
?
Subunits
Subunits
Commentary
Organism
homodimer
2 * 44000, recombinant His-tagged enzyme, SDS-PAGE
Selenomonas ruminantium
Temperature Optimum [°C]
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Selenomonas ruminantium
pH Optimum
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
-
assay at
Selenomonas ruminantium
Cofactor
Cofactor
Commentary
Organism
Structure
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
Selenomonas ruminantium
Application (protein specific)
Application
Commentary
Organism
synthesis
enzyme LDC plays a crucial role in the synthesis of cadaverine, an important industrial platform chemical. Cadaverine is utilized with a variety of applications such as the production of polyamides, polyurethanes, chelating agents, and additives
Selenomonas ruminantium
Cloned(Commentary) (protein specific)
Commentary
Organism
gene Srldc, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
Selenomonas ruminantium
Cofactor (protein specific)
Cofactor
Commentary
Organism
Structure
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
Selenomonas ruminantium
Crystallization (Commentary) (protein specific)
Crystallization
Organism
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
Selenomonas ruminantium
Engineering (protein specific)
Amino acid exchange
Commentary
Organism
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
Selenomonas ruminantium
K2C/G227C
site-directed mutagenesis, the mutant shows reduced affinity for pyridoxal 5'-phosphate and reduced activity compared to wild-type
Selenomonas ruminantium
additional information
disulfide bond-mediated spatial reconstitution can be a platform technology for development of enzymes with enhanced pyridoxal 5'-phosphate affinity
Selenomonas ruminantium
KM Value [mM] (protein specific)
KM Value [mM]
KM Value Maximum [mM]
Substrate
Commentary
Organism
Structure
additional information
-
additional information
kinetic analysis of wild-type and mutant enzymes
Selenomonas ruminantium
Natural Substrates/ Products (Substrates) (protein specific)
Natural Substrates
Organism
Commentary (Nat. Sub.)
Natural Products
Commentary (Nat. Pro.)
Organism (Nat. Pro.)
Reversibility
L-lysine
Selenomonas ruminantium
-
cadaverine + CO2
-
-
?
Purification (Commentary) (protein specific)
Commentary
Organism
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and gel filtration
Selenomonas ruminantium
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
L-lysine
-
749101
Selenomonas ruminantium
cadaverine + CO2
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
homodimer
2 * 44000, recombinant His-tagged enzyme, SDS-PAGE
Selenomonas ruminantium
Temperature Optimum [°C] (protein specific)
Temperature Optimum [°C]
Temperature Optimum Maximum [°C]
Commentary
Organism
37
-
assay at
Selenomonas ruminantium
pH Optimum (protein specific)
pH Optimum Minimum
pH Optimum Maximum
Commentary
Organism
6
-
assay at
Selenomonas ruminantium
General Information
General Information
Commentary
Organism
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
Selenomonas ruminantium
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
Selenomonas ruminantium
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
Selenomonas ruminantium
General Information (protein specific)
General Information
Commentary
Organism
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
Selenomonas ruminantium
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
Selenomonas ruminantium
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
Selenomonas ruminantium
Other publictions for EC 4.1.1.18
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
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Shin
Characterization of a whole-c ...
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1
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1
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4
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7
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3
2
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1
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1
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1
1
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7
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1
1
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749226
Wang
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Morus alba
Protein Expr. Purif.
151
30-37
2018
-
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1
-
-
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1
-
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1
-
3
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1
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1
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1
1
1
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1
-
-
-
-
1
1
-
-
-
749366
Kloss
Catalytically active inclusio ...
Escherichia coli
Sci. Rep.
8
5856
2018
-
-
1
-
1
-
-
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1
-
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1
-
3
-
-
-
-
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1
1
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2
2
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1
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1
1
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2
2
-
-
-
1
1
-
-
-
747369
Hong
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Escherichia coli, Escherichia coli K-12 / B
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12
1700278
2017
-
-
1
-
6
-
1
4
-
-
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2
-
2
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1
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2
1
1
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1
3
1
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1
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1
1
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6
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1
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4
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2
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1
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2
1
1
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1
3
1
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-
-
-
-
-
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3
3
748386
Park
Cadaverine production by usin ...
Escherichia coli
J. Microbiol. Biotechnol.
27
289-296
2017
-
1
1
-
1
-
-
-
-
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1
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1
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2
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1
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1
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2
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1
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2
1
1
-
1
-
1
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-
-
-
-
-
-
749101
Sagong
Lysine decarboxylase with an ...
Selenomonas ruminantium
PLoS ONE
12
e0170163
2017
-
1
1
1
3
-
-
1
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-
-
1
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2
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1
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1
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1
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1
1
1
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3
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1
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1
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1
1
1
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1
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3
3
-
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-
747594
Li
Heterologous expression and c ...
Klebsiella oxytoca, Klebsiella oxytoca ATCC 8724 / DSM 4798 / JCM 20051 / NBRC 3318 / NRRL B-199 / KCTC 1686
Chin. J. Biotechnol.
32
527-531
2016
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1
1
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3
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1
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2
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4
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1
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2
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2
1
1
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1
1
-
-
-
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-
-
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747655
Li
-
Improved cadaverine productio ...
Klebsiella oxytoca, Klebsiella oxytoca DSM 6673
Eng. Life Sci.
16
299-305
2016
-
-
1
-
1
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2
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3
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2
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748382
Kim
Functional study of lysine de ...
Klebsiella aerogenes, Klebsiella aerogenes ATCC 13048 / DSM 30053 / JCM 1235 / KCTC 2190 / NBRC 13534 / NCIMB 10102 / NCTC 10006
J. Microbiol. Biotechnol.
26
1586-1592
2016
-
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1
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1
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1
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6
-
4
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1
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12
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1
1
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1
1
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1
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2
2
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2
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1
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6
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2
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12
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2
2
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1
2
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1
1
748418
Kou
-
Characterization of a new lys ...
Aliivibrio salmonicida
J. Mol. Catal. B
133
S88-S94
2016
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1
1
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1
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1
1
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2
2
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1
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3
1
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1
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1
1
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2
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1
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2
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3
3
1
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4
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1
1
1
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-
-
-
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748513
Jeong
-
Alkaliphilic lysine decarboxy ...
Geobacillus thermodenitrificans
Korean J. Chem. Engin.
33
1530-1533
2016
-
1
1
-
-
-
-
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1
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1
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1
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1
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1
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1
1
1
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1
1
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-
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1
1
-
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749097
Sagong
Crystal structure and pyridox ...
Selenomonas ruminantium
PLoS ONE
11
e0166667
2016
-
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1
1
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-
-
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1
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2
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1
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2
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1
1
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1
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1
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2
2
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1
1
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749315
Kandiah
Structural insights into the ...
Escherichia coli
Sci. Rep.
6
24601
2016
-
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1
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1
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4
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4
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1
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4
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4
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3
5
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747358
Wang
-
Directed evolution and mutage ...
Hafnia alvei, Hafnia alvei AS1.1009
Biotechnol. Bioprocess Eng.
20
439-446
2015
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1
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4
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3
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2
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2
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1
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2
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1
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2
1
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1
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1
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1
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1
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2
2
748377
Kim
Optimization of direct lysine ...
Escherichia coli, Escherichia coli K-12 / MG1655
J. Microbiol. Biotechnol.
25
1108-1113
2015
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4
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1
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1
1
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748380
Kim
A Liquid-based colorimetric a ...
Burkholderia thailandensis, Escherichia coli, Escherichia coli K-12 / MG1655, Klebsiella aerogenes, Klebsiella aerogenes ATCC 13048 / DSM 30053 / JCM 1235 / KCTC 2190 / NBRC 13534 / NCIMB 10102 / NCTC 10006
J. Microbiol. Biotechnol.
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2015
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3
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10
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3
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3
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728013
Sugawara
Characterization of a pyridoxa ...
Burkholderia sp., Burkholderia sp. AIU 395
J. Biosci. Bioeng.
118
496-501
2014
-
-
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2
1
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1
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1
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-
747039
Wang
In vitro inhibition of lysine ...
Bacterium cadaveris
Biochem. Pharmacol.
92
506-516
2014
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-
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11
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1
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1
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747357
Li
-
Cadaverine production by hete ...
Klebsiella oxytoca, Klebsiella oxytoca DSM 6673
Biotechnol. Bioprocess Eng.
19
965-972
2014
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1
1
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1
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2
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727766
Romano
Three-component lysine/ornithi ...
Lactobacillus saerimneri 30a, Lactobacillus saerimneri 30a ATCC 33222
J. Bacteriol.
195
1249-1254
2013
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7
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1
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4
1
1
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1
1
1
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1
1
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1
1
728183
Lohinai
Bacterial lysine decarboxylase ...
Eikenella corrodens
J. Periodontol.
83
1048-1056
2012
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1
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728330
Burrell
Evolution of a novel lysine de ...
Streptomyces coelicolor, Streptomyces coelicolor ATCC BAA-471
Mol. Microbiol.
86
485-499
2012
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2
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6
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1
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1
1
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2
2
714832
Kanjee
Linkage between the bacterial ...
Escherichia coli
EMBO J.
30
931-944
2011
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1
3
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5
1
1
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3
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1
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1
1
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1
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1
1
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1
1
715142
Teng
-
The use of L-lysine decarboxyl ...
Bacterium cadaveris
Green Chem.
13
624-630
2011
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1
4
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1
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704086
Alvarez-Ordonez
Arginine and lysine decarboxyl ...
Salmonella enterica subsp. enterica serovar Typhimurium, Salmonella enterica subsp. enterica serovar Typhimurium CECT 443
Int. J. Food Microbiol.
136
278-282
2010
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3
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3
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3
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1
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1
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713611
Sempruch
Changes in activity of lysine ...
Secale cereale x Triticum aestivum
Acta Biol. Hung.
61
512-515
2010
-
-
-
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3
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4
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1
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1
-
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716768
El Bakkouri
Structure of RavA MoxR AAA+ pr ...
Escherichia coli
Proc. Natl. Acad. Sci. USA
107
22499-22504
2010
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-
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1
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1
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1
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4
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1
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1
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-
690395
Ohe
Putative occurrence of lysine ...
Glycine max
Amino Acids
36
65-70
2009
-
-
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1
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2
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5
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5
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1
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-
690597
Tateno
Direct production of cadaverin ...
Escherichia coli
Appl. Microbiol. Biotechnol.
82
115-121
2009
-
-
1
-
-
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-
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1
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4
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1
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1
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1
1
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1
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1
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-
-
-
-
-
690269
Alexopoulos
Crystallization and preliminar ...
Escherichia coli
Acta Crystallogr. Sect. F
64
700-706
2008
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-
1
1
-
-
-
-
-
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2
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1
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1
1
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1
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1
1
1
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1
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-
1
1
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-
-
-
-
-
-
-
-
-
-
-
-
680417
Tanaka
Lysine decarboxylase of Vibrio ...
Vibrio parahaemolyticus
J. Appl. Microbiol.
104
1283-1293
2007
1
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1
-
1
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2
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1
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1
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1
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-
1
-
-
-
-
-
-
-
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-
680484
Moreau
The lysine decarboxylase CadA ...
Escherichia coli
J. Bacteriol.
189
2249-2261
2007
1
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4
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1
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-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
698370
Lee
Thalassococcus halodurans gen. ...
no activity in Thalassobius mediterraneus, no activity in Thalassobius mediterraneus XSM19, no activity in Thalassococcus halodurans, no activity in Thalassococcus halodurans UST050418-052, Shimia aestuarii, Shimia aestuarii JC2049
Int. J. Syst. Evol. Microbiol.
57
1919-1924
2007
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6
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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665713
Snider
Formation of a distinctive com ...
Escherichia coli
J. Biol. Chem.
281
1532-1546
2006
-
-
-
-
-
-
-
-
-
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4
-
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1
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-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
680477
Kim
Lysine decarboxylase expressio ...
Vibrio vulnificus
J. Bacteriol.
188
8586-8592
2006
1
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1
-
1
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-
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1
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2
-
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-
1
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1
-
1
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-
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1
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1
-
1
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1
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1
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-
1
-
1
-
1
-
-
-
1
-
-
-
-
-
-
-
-
-
666850
Kukimoto-Niino
Crystal structures of possible ...
Thermus thermophilus, Thermus thermophilus HB8 / ATCC 27634 / DSM 579
Protein Sci.
13
3038-3042
2004
-
-
-
1
-
-
-
-
-
-
-
-
-
90
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
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-
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-
1
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-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
698364
Lau
Loktanella hongkongensis sp. n ...
no activity in Loktanella hongkongensis
Int. J. Syst. Evol. Microbiol.
54
2281-2284
2004
-
-
-
-
-
-
-
-
-
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-
1
-
-
-
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
656712
Levine
Identification of lysine decar ...
Eikenella corrodens
Microb. Pathog.
30
179-192
2001
-
-
-
-
-
-
-
-
-
-
-
-
-
3
-
-
-
-
-
-
-
-
-
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-
-
-
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-
-
-
-
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-
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-
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-
-
-
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-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
655829
Takatsuka
Gene cloning and molecular cha ...
Selenomonas ruminantium
J. Bacteriol.
182
6732-6741
2000
-
-
1
-
11
-
-
23
-
-
-
-
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9
-
-
1
-
-
-
-
-
3
-
-
-
-
22
-
-
-
-
-
-
-
-
-
1
-
-
11
-
-
-
-
23
-
-
-
-
-
-
-
1
-
-
-
-
3
-
-
-
-
22
-
-
-
-
-
-
-
-
-
-
654982
Takatsuka
Novel characteristics of Selen ...
Selenomonas ruminantium
Biosci. Biotechnol. Biochem.
63
1063-1069
1999
-
-
-
-
-
-
2
2
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2
1
-
2
-
-
1
-
-
1
1
1
4
1
1
-
2
2
1
-
1
1
4
1
-
-
-
-
1
-
-
-
-
2
4
2
-
-
2
1
-
-
-
1
-
1
1
1
4
1
1
-
2
2
1
-
1
1
-
-
-
-
-
-
654984
Takatsuka
Identification of the amino ac ...
Selenomonas ruminantium
Biosci. Biotechnol. Biochem.
63
1843-1846
1999
-
-
-
-
11
-
-
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3
-
-
-
-
-
-
-
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2
-
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-
-
-
-
-
-
-
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-
-
-
-
-
-
-
11
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
37297
Kim
Purification and characterizat ...
Glycine max
Arch. Biochem. Biophys.
354
40-46
1998
-
-
-
-
-
-
15
2
-
-
1
-
-
2
-
-
1
-
-
1
1
1
1
1
1
-
1
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
15
-
2
-
-
1
-
-
-
-
1
-
1
1
1
1
1
1
-
1
-
1
-
-
-
-
-
-
-
-
-
698361
Ruiz-Ponte
Roseobacter gallaeciensis sp. ...
no activity in Phaeobacter gallaeciensis BS107
Int. J. Syst. Bacteriol.
48 Pt 2
537-542
1998
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
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-
-
-
-
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-
-
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-
-
-
-
-
-
-
-
-
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37299
Kikuchi
Characterization of a second l ...
Escherichia coli
J. Bacteriol.
179
4486-4492
1997
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1
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1
1
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37298
Berkowitz
?-VINYLLYSINE AND ?-VINYLARGIN ...
Bacterium cadaveris
Bioorg. Med. Chem. Lett.
6
2151-2156
1996
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1
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698360
Lafay
Roseobacter algicola sp. nov., ...
no activity in Marinovum algicola, no activity in Marinovum algicola ATCC 51442
Int. J. Syst. Bacteriol.
45
290-296
1995
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37300
Yamamoto
Purification and some properti ...
Vibrio parahaemolyticus, Vibrio parahaemolyticus AQ 3627
Chem. Pharm. Bull.
39
3067-3070
1991
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2
4
1
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2
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4
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8
1
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1
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8
1
1
1
1
-
1
1
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37283
Beier
-
Lysine decarboxylase from Hafn ...
Hafnia alvei
Z. Naturforsch. C
42
1307-1312
1987
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1
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6
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1
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6
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1
1
1
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1
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37284
Pelosi
-
Lysine decarboxylase activity ...
Heimia salicifolia
Phytochemistry
25
2315-2319
1986
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4
1
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1
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1
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37285
Fecker
-
Cloning and characterization o ...
Hafnia alvei
Mol. Gen. Genet.
203
177-184
1986
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1
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1
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37286
Vienozinskiene
Lysine decarboxylase assay by ...
Escherichia coli
Anal. Biochem.
146
180-183
1985
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1
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1
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1
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1
1
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1
1
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37287
Poesoe
Inhibition of growth of Mycopl ...
Mycoplasma dispar
Biochem. Biophys. Res. Commun.
125
205-210
1984
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1
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4
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1
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37288
Schoofs
-
Lysine decarboxylase in plants ...
Anchusa italica, Arum maculatum, Asarum maculatum, Astragalus cicer, Astragalus glycyphyllos, Atropa belladonna, Baptisia australis, Calla palustris, Conium maculatum, Cytisus beanii, Cytisus canariensis, Cytisus scoparius, Dictamnus albus, Galega officinalis, Genista anglica, Genista hispanica, Genista lydia, Genista pilosa, Genista sagittalis, Genista tinctoria, Glycine max, Glycyrrhiza echinata, Laburnum alpinum, Laburnum anagyroides, Levisticum officinale, Lupinus albus, Lupinus luteus, Lupinus polyphyllus, Malva sylvestris, Medicago sativa, Melilotus albus, Mentha suaveolens, Menyanthes trifoliata, Nicotiana tabacum, Oxybasis rubra, Phaseolus vulgaris, Pisum sativum, Robinia pseudoacacia, Ruta graveolens, Sanguisorba officinalis, Saponaria officinalis, Sedum acre, Senecio fuchsii, Sophora tetraptera, Spinacia oleracea, Styphnolobium japonicum, Symphytum officinale, Trollius europaeus, Valeriana sambucifolia, Vicia faba
Phytochemistry
22
65-69
1983
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1
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50
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14
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51
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14
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51
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37289
Boeker
Lysine decarboxylase (Escheric ...
Escherichia coli, Escherichia coli B / ATCC 11303
Methods Enzymol.
94
180-184
1983
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1
3
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3
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177
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6
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6
1
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37290
Kamio
Purification and properties of ...
Selenomonas ruminantium
J. Bacteriol.
153
658-664
1983
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1
1
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5
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1
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4
1
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2
1
1
1
1
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1
1
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37296
Battersby
-
Studies of enzyme-mediated rea ...
Bacterium cadaveris
J. Chem. Soc. Perkin Trans. I
1982
449-453
1982
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1
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37291
Hartmann
A chloroplast-localized lysine ...
Lupinus polyphyllus
FEBS Lett.
115
35-38
1980
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1
1
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1
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1
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37301
Pegg
Decarboxylation of ornithine a ...
Mus musculus, no activity in Rattus norvegicus
Biochim. Biophys. Acta
568
416-427
1979
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4
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37292
Sabo
Chemical properties of Escheri ...
Escherichia coli
Biochemistry
13
670-676
1974
1
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37293
Sabo
Purification and physical prop ...
Escherichia coli, Escherichia coli B / ATCC 11303
Biochemistry
13
662-670
1974
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1
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1
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1
2
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178
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8
1
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2
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1
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8
1
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1
1
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37294
Soda
-
L-Lysine decarboxylase (Bacter ...
Bacterium cadaveris
Methods Enzymol.
17B
677-681
1971
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1
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5
2
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1
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1
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1
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3
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1
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1
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5
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1
3
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1
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1
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37295
Soda
Crystalline lysine decarboxyla ...
Bacterium cadaveris
Biochem. Biophys. Res. Commun.
34
34-39
1969
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1
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2
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1
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