Purification and some properties of inducible lysine decarboxylase from Vibrio parahaemolyticus

S. Yamamoto, T. Imamura, K. Kusaba, S. Shinoda

Research output: Contribution to journalArticle

8 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)3067-3070
Number of pages4
JournalChemical and Pharmaceutical Bulletin
Volume39
Issue number11
Publication statusPublished - 1991

ASJC Scopus subject areas

  • Drug Discovery
  • Organic Chemistry
  • Chemistry(all)
  • Pharmacology

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