Purification and characterization of paralytic shellfish toxin-transforming enzyme, sulfocarbamoylase I, from the Japanese bivalve Peronidia venulosa

Yuko Cho, Noriyuki Ogawa, Miyako Takahashi, Hsi Pin Lin, Yasukatsu Oshima

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    31 Citations (Scopus)

    Abstract

    The Japanese bivalve Peronidia venulosa contains paralytic shellfish toxin (PST)-transforming enzymes that convert the weakly toxic C-toxins to the more potent decarbamoyl toxins. The enzyme was purified 154-fold with a yield of 0.26% and was named sulfocarbamoylase I. It was found to be a protein with an estimated molecular weight of 300 kDa by gel filtration column chromatography. Observation of a single band equivalent to 150 kDa on SDS-PAGE with or without reducing agents suggested it to be a homodimer with ionically bound subunits. The enzyme catalyzes the hydrolysis of the carboxyl bond in the N-sulfocarbamoyl moiety of PSP-toxins. The sulfonyl moiety in the carbamoyl side chain of substrates is essential for enzyme recognition. The N-terminal amino acid sequences of nine tryptic peptides were determined by the Edman degradation method. In a database search using the BLAST program, no protein that shows remarkable homology was retrieved. Several characteristics of the enzyme were also compared with those of another PST-transforming enzyme, carbamoylase I, which was previously isolated from the Japanese clam Mactra chinensis.

    Original languageEnglish
    Pages (from-to)1277-1285
    Number of pages9
    JournalBiochimica et Biophysica Acta - Proteins and Proteomics
    Volume1784
    Issue number9
    DOIs
    Publication statusPublished - 2008 Sep

    Keywords

    • Crystalline style
    • Paralytic shellfish toxins
    • Peronidia venulosa
    • Saxitoxin
    • Sulfocarbamoylase

    ASJC Scopus subject areas

    • Analytical Chemistry
    • Biophysics
    • Biochemistry
    • Molecular Biology

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