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Literature summary extracted from

  • Teng, Y.; Scott, E.; Van Zeeland, A.; Sanders, J.
    The use of L-lysine decarboxylase as a means to separate amino acids by electrodialysis (2011), Green Chem., 13, 624-630.
No PubMed abstract available

General Stability

EC Number General Stability Organism
4.1.1.18 calcium alginate can completely entrap the enzyme while retaining activity and improving stability during operation and storage Bacterium cadaveris

Inhibitors

EC Number Inhibitors Comment Organism Structure
4.1.1.18 1,5-pentanediamine
-
 Bacterium cadaveris
4.1.1.18 L-Arg
-
 Bacterium cadaveris
4.1.1.18 additional information at 30°C the presence of L-Arg has little effect on the activity of the enzyme Bacterium cadaveris
4.1.1.18 NaCl about 65% residual activity at 1 M Bacterium cadaveris

Organism

EC Number Organism UniProt Comment Textmining
4.1.1.18 Bacterium cadaveris
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
4.1.1.18 L-lysine
-
 Bacterium cadaveris cadaverine + CO2 cadaverine is 1,5-pentanediamine ?

Synonyms

EC Number Synonyms Comment Organism
4.1.1.18 L-lysine decarboxylase
-
 Bacterium cadaveris
4.1.1.18 LDC
-
 Bacterium cadaveris

Cofactor

EC Number Cofactor Comment Organism Structure
4.1.1.18 pyridoxal 5'-phosphate
-
 Bacterium cadaveris

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
4.1.1.18 600
-
 at 37°C, pH not specified in the publication Bacterium cadaveris L-Arg