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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)
Activity 4.1.1.18
Family 4.1.1.18.b
sel unselected
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 2014/07/11 10:49

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