Purification and some properties of inducible lysine decarboxylase from Vibrio parahaemolyticus.
Inducible lysine decarboxylase from Vibrio parahaemolyticus AQ 3627 was purified to apparent homogeneity and characterized. The enzyme displayed a molecular weight of 531000 by gel filtration and 79000 by sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The enzyme required pyridoxal phosphate as a cofactor, and the pH optimum was 5.5. The Km value for L-lysine was 3.2 mM, and the enzyme was inhibited by 6-aminocaproic acid and alpha-fluoromethyl analogs of cadaverine. delta-Hydroxylysine and S-aminoethyl-L-cysteine was active as substrates to a lesser extent than L-lysine. The amino-terminal amino acid sequence was determined to be Met-Asn-Ile-Phe-Ala-Ile-Leu. These properties were compared with those of other bacterial lysine decarboxylases.
Yamamoto
S
S
Faculty of Pharmaceutical Sciences, Okayama University, Japan.
Imamura
T
T
Kusaba
K
K
Shinoda
S
S
D000595:Amino Acid Sequence; D002262:Carboxy-Lyases / Q000096:biosynthesis / Q000302:isolation & purification* / Q000378:metabolism; D004790:Enzyme Induction; D008969:Molecular Sequence Data; D014736:Vibrio parahaemolyticus / Q000201:enzymology*
D002262:Carboxy-Lyases; C021520:lysine decarboxylase