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Literature summary extracted from

  • Kikuchi, Y.; Kojima, H.; Tanaka, T.; Takasuka, Y.; Kamio, Y.
    Characterization of a second lysine decarboxylase isolated from Escherichia coli (1997), J. Bacteriol., 179, 4486-4492.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
4.1.1.18
-
 Escherichia coli

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
4.1.1.18 80000
-
 10 * 80000, SDS-PAGE Escherichia coli
4.1.1.18 800000
-
 gel filtration Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.18 Escherichia coli
-
 2 enzyme form, one is encoded by the gen cadA and the other by the gene ldc
-

Purification (Commentary)

EC Number Purification (Comment) Organism
4.1.1.18 enzyme form ldc Escherichia coli

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 additional information
-
-
 Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.18 L-Lys
-
 Escherichia coli Cadaverine + CO2
-
 ?

Subunits

EC Number Subunits Comment Organism
4.1.1.18 decamer 10 * 80000, SDS-PAGE Escherichia coli

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
4.1.1.18 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 Escherichia coli

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
4.1.1.18 6.2 8
-
 Escherichia coli

pH Range

EC Number pH Minimum pH Maximum Comment Organism
4.1.1.18 5.2 8.8 pH 5.2: 40% of maximal activity, pH 8.8: 30% of maximal activity Escherichia coli