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 language | English |
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Pages (from-to) | 3067-3070 |
Number of pages | 4 |
Journal | Chemical and Pharmaceutical Bulletin |
Volume | 39 |
Issue number | 11 |
Publication status | Published - 1991 |
ASJC Scopus subject areas
- Drug Discovery
- Organic Chemistry
- Chemistry(all)
- Pharmacology