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

Research output: Contribution to journalArticlepeer-review

26 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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