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Literature summary extracted from

  • 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 (2017), Biotechnol. J., 12, 1700278 .
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.18 gene cadA, recombinant expression of His6-tagged wild-type and mutant enzymes in Escherichia coli strain BL21 (DE3) Escherichia coli

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.18 F102C/T544C site-directed mutagenesis, mutant A2 Escherichia coli
4.1.1.18 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 Escherichia coli
4.1.1.18 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 Escherichia coli
4.1.1.18 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 Escherichia coli
4.1.1.18 P233C/L628C site-directed mutagenesis, mutant C1 Escherichia coli
4.1.1.18 V91C/G445C site-directed mutagenesis, mutant A1 Escherichia coli

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.1.18 L-lysine substrate inhibition at high concentrations Escherichia coli

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.18 additional information
-
 additional information Michaelis-Menten kinetics Escherichia coli
4.1.1.18 1.22
-
 L-lysine pH 5.6, 45°C, recombinant His6-tagged wild-type enzyme Escherichia coli
4.1.1.18 1.33
-
 L-lysine pH 5.6, 45°C, recombinant His6-tagged mutant F14C/K44C Escherichia coli
4.1.1.18 1.47
-
 L-lysine pH 5.6, 45°C, recombinant His6-tagged mutant F14C/K44C/L7M/N8G Escherichia coli

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
4.1.1.18 L-lysine Escherichia coli
-
 cadaverine + CO2
-
 ?
4.1.1.18 L-lysine Escherichia coli K-12 / B
-
 cadaverine + CO2
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.18 Escherichia coli P0A9H3
-
-
4.1.1.18 Escherichia coli K-12 / B P0A9H3
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.18 recombinant His6-tagged wild-type and mutant enzymes from Escherichia coli strain BL21 (DE3) by nickel affinity chromatography and ultrafiltration Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.18 L-lysine
-
 Escherichia coli cadaverine + CO2
-
 ?
4.1.1.18 L-lysine
-
 Escherichia coli K-12 / B cadaverine + CO2
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.1.18 homodecamer a pentamer of homodimers, 10 * 82000, recombinant His6-tagged wild-type enzyme, SDS-PAGE Escherichia coli

Synonyms

EC Number Synonyms Comment Organism
4.1.1.18 CadA
-
 Escherichia coli
4.1.1.18 multimeric lysine decarboxylase
-
 Escherichia coli

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.1.18 37 50 assay at Escherichia coli

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.1.1.18 80
-
 purified recombinant His6-tagged wild-type enzyme, pH 5.6, 60% activity remaining Escherichia coli

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
4.1.1.18 146.4
-
 L-lysine pH 5.6, 45°C, recombinant His6-tagged wild-type enzyme Escherichia coli
4.1.1.18 149.3
-
 L-lysine pH 5.6, 45°C, recombinant His6-tagged mutant F14C/K44C Escherichia coli
4.1.1.18 172.1
-
 L-lysine pH 5.6, 45°C, recombinant His6-tagged mutant F14C/K44C/L7M/N8G Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.18 5.6
-
 wild-type enzyme Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.18 pyridoxal 5'-phosphate
-
 Escherichia coli

kcat/KM [mM/s]

EC Number kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.1.1.18 112.3
-
 L-lysine pH 5.6, 45°C, recombinant His6-tagged mutant F14C/K44C Escherichia coli
4.1.1.18 117.1
-
 L-lysine pH 5.6, 45°C, recombinant His6-tagged mutant F14C/K44C/L7M/N8G Escherichia coli
4.1.1.18 120.1
-
 L-lysine pH 5.6, 45°C, recombinant His6-tagged wild-type enzyme Escherichia coli