Hevea Linamarase—A Nonspecific β-Glycosidase
Author(s) -
Dirk Selmar,
R. Lieberei,
Böle Biehl,
J. Voigt
Publication year - 1987
Publication title -
plant physiology
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 3.554
H-Index - 312
eISSN - 1532-2548
pISSN - 0032-0889
DOI - 10.1104/pp.83.3.557
Subject(s) - hevea , hevea brasiliensis , glycoside hydrolase , glucoside , glycoside , euphorbiaceae , chemistry , biology , biochemistry , enzyme , botany , stereochemistry , organic chemistry , natural rubber , medicine , alternative medicine , pathology
In the leaf tissue of the cyanogenic plant Hevea brasiliensis, which contains large amounts of linamarin, there is no specific linamarase. In Hevea leaves only one beta-glucosidase is detectable. It is responsible for the cleavage of all beta-glucosides and beta-galactosides occurring in Hevea leaf tissue, including the cyanogenic glucoside linamarin. Therefore, the enzyme is referred to as a beta-glycosidase instead of the term beta-glucosidase. This beta-glycosidase has a broad substrate spectrum and occurs in multiple forms. These homo-oligomeric forms are interconvertible by dissociation-association processes. The monomer is a single protein of 64 kilodaltons.
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