Purification and Some Properties of Inducible Lysine Decarboxylase from Vibrio parahaemolyticus

概要

論文の詳細を見る
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 K_m value for L-lysine was 3.2 mM, and the enzyme was inhibited by 6-aminocaproic acid and α-fluoromethyl analogs of cadaverine. δ-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.
社団法人日本薬学会の論文
1991-11-25