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Literature summary for 4.1.1.18 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
Search for more literature for 4.1.1.18

Cloned(Commentary)

Cloned (Comment) Organism
-
 Escherichia coli

Molecular Weight [Da]

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

Organism

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

Purification (Commentary)

Purification (Comment) Organism
enzyme form ldc Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
 Escherichia coli

Substrates and Products (Substrate)

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

Subunits

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

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.2 8
-
 Escherichia coli

pH Range

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