|
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 |
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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