Premium
The myrosinase‐glucosinolate interaction mechanism studied using some synthetic competitive inhibitors
Author(s) -
Iori Renato,
Rollin Patrick,
Streicher Harald,
Thiem Joachim,
Palmieri Sandro
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00335-3
Subject(s) - myrosinase , chemistry , non competitive inhibition , fischer–tropsch process , stereochemistry , catalysis , biochemistry , glucosinolate , enzyme , botany , biology , brassica , selectivity
Using synthetic deoxy‐glucotropaeolins (6d‐GTL, 4d‐GTL, 3d‐GTL, 2d‐GTL) as substrates, myrosinase activity was studied in comparison to that determined on native glucotropaeolin (GTL) isolated from ripe Lepidium sativum seeds. When the deoxy substrates were used, in addition to an overall strong reaction rate decline, a significant decrease in the reaction rate was observed in going from 6d‐ to 2d‐GTL. This finding allows us to propose a mechanism of catalysis which appears to be similar in many respects to that established for β‐glucosidases. Finally, 2d‐GTL was shown to be the first strong competitive inhibitor of myrosinase ever reported.