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Literature summary extracted from

  • Kou, F.; Zhao, J.; Liu, J.; Shen, J.; Ye, Q.; Zheng, P.; Li, Z.; Sun, J.; Ma, Y.
    Characterization of a new lysine decarboxylase from Aliivibrio salmonicida for cadaverine production at alkaline pH (2016), J. Mol. Catal. B, 133, S88-S94 .
No PubMed abstract available

Application

EC Number Application Comment Organism
4.1.1.18 synthesis enzyme AsLdc has a high potential for the industrial production of cadaverine Aliivibrio salmonicida

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.18 gene cadA, DNA and amino acid sequence determination and analysis, recombinant expression of C-terminally His-tagged enzyme in Escherichia coli strain BL21(DE3) Aliivibrio salmonicida

Protein Variants

EC Number Protein Variants Comment Organism
4.1.1.18 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 Aliivibrio salmonicida

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.1.18 cadaverine competitive inhibition mechanism, 90% inhibition at 10 mM Aliivibrio salmonicida

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
4.1.1.18 0.92
-
 L-lysine recombinant enzyme, pH 7.5, 37°C Aliivibrio salmonicida

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.1.18 158000
-
 dimeric enzyme, native PAGE Aliivibrio salmonicida
4.1.1.18 780000
-
 decameric enzyme, native PAGE Aliivibrio salmonicida

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 Aliivibrio salmonicida
-
 cadaverine + CO2
-
 ?
4.1.1.18 additional information Aliivibrio salmonicida 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 ?
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.18 Aliivibrio salmonicida B6EKJ5 i.e. Vibrio salmonicida
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.18 recombinant His-tagged enzyme from Escherichia coli strain BL21(DE3) by nickel affinity chromatography and ultrafiltration Aliivibrio salmonicida

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
4.1.1.18 94.1
-
 purified recombinant enzyme, pH 8.5, 37°C, substrate L-lysine Aliivibrio salmonicida
4.1.1.18 205.1
-
 purified recombinant enzyme, pH 7.5, 37°C, substrate L-lysine Aliivibrio salmonicida

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.18 L-lysine
-
 Aliivibrio salmonicida cadaverine + CO2
-
 ?
4.1.1.18 L-lysine 100% conversion by the recombinant enzyme at pH 7.5 Aliivibrio salmonicida cadaverine + CO2
-
 ?
4.1.1.18 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 Aliivibrio salmonicida ?
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.1.18 decamer
-
 Aliivibrio salmonicida
4.1.1.18 dimer
-
 Aliivibrio salmonicida
4.1.1.18 More 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 Aliivibrio salmonicida

Synonyms

EC Number Synonyms Comment Organism
4.1.1.18 AsLdc
-
 Aliivibrio salmonicida
4.1.1.18 CadA
-
 Aliivibrio salmonicida
4.1.1.18 LDC
-
 Aliivibrio salmonicida
4.1.1.18 VSAL_I2491
-
 Aliivibrio salmonicida

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
4.1.1.18 50
-
-
 Aliivibrio salmonicida

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.1.1.18 37
-
 purified recombinant enzyme AsLdc, 12 h, pH 7.5, residual activity is 96.3% Aliivibrio salmonicida
4.1.1.18 50
-
 purified recombinant enzyme AsLdc, 12 h, pH 7.5, residual activity is 75.2% Aliivibrio salmonicida
4.1.1.18 79
-
 Tm of recombinant enzyme AsLdc Aliivibrio salmonicida
4.1.1.18 80
-
 purified recombinant enzyme AsLdc, 12 h, pH 7.5, residual activity is about 50% Aliivibrio salmonicida

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.18 7.5
-
-
 Aliivibrio salmonicida

pH Range

EC Number pH Minimum pH Maximum Comment Organism
4.1.1.18 5 8.5 high activity within this range Aliivibrio salmonicida

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
4.1.1.18 8.5
-
 purified recombinant enzyme AsLdc, 10 h, 37°C, residual activity is 71% Aliivibrio salmonicida

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.18 pyridoxal 5'-phosphate
-
 Aliivibrio salmonicida

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
4.1.1.18 0.46
-
 cadaverine recombinant enzyme, pH 7.5, 37°C Aliivibrio salmonicida