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B6db references: 92191342

type Journal Article
authors Yamamoto, S.; Imamura, T.; Kusaba, K.; Shinoda, S.
title Purification and some properties of inducible lysine decarboxylase from Vibrio parahaemolyticus
journal Chem Pharm Bull (Tokyo)
sel selected
ui 92191342
year (1991)
volume 39
number 11
pages 3067-70.
keywords Amino Acid Sequence
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 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.
last changed 2018/05/23 13:21

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