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 |
|---|---|
| Pages (from-to) | 3067-3070 |
| Number of pages | 4 |
| Journal | Chemical and Pharmaceutical Bulletin |
| Volume | 39 |
| Issue number | 11 |
| Publication status | Published - 1991 |
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ASJC Scopus subject areas
- Drug Discovery
- Organic Chemistry
- Chemistry(all)
- Pharmacology
Cite this
Purification and some properties of inducible lysine decarboxylase from Vibrio parahaemolyticus. / Yamamoto, S.; Imamura, T.; Kusaba, K.; Shinoda, S.
In: Chemical and Pharmaceutical Bulletin, Vol. 39, No. 11, 1991, p. 3067-3070.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Purification and some properties of inducible lysine decarboxylase from Vibrio parahaemolyticus
AU - Yamamoto, S.
AU - Imamura, T.
AU - Kusaba, K.
AU - Shinoda, S.
PY - 1991
Y1 - 1991
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=0026315061&partnerID=8YFLogxK
M3 - Article
C2 - 1799949
AN - SCOPUS:0026315061
VL - 39
SP - 3067
EP - 3070
JO - Chemical and Pharmaceutical Bulletin
JF - Chemical and Pharmaceutical Bulletin
SN - 0009-2363
IS - 11
ER -