Purification and characterization of paralytic shellfish toxin-transforming enzyme, sulfocarbamoylase I, from the Japanese bivalve Peronidia venulosa.
Biochim Biophys Acta
; 1784(9): 1277-85, 2008 Sep.
Article
in En
| MEDLINE
| ID: mdl-18599388
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.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Carboxylic Ester Hydrolases
/
Bivalvia
/
Marine Toxins
Type of study:
Prognostic_studies
Limits:
Animals
Country/Region as subject:
Asia
Language:
En
Journal:
Biochim Biophys Acta
Year:
2008
Document type:
Article
Affiliation country: