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Elsevier, Bioorganic and Medicinal Chemistry Letters, 10(18), p. 3095-3098

DOI: 10.1016/j.bmcl.2007.11.063

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Substrate Specificity and Diastereoselectivity of Strictosidine Glucosidase, a Key Enzyme in Monoterpene Indole Alkaloid Biosynthesis

Journal article published in 2007 by Nancy Yerkes, Jia Xin Wu, Elizabeth McCoy, M. Carmen Galan, M. Carmen Galan ORCID, Shi Chen, Sarah E. O’Connor
This paper is available in a repository.
This paper is available in a repository.

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Abstract

Strictosidine glucosidase (SGD) from Catharanthus roseus catalyzes the deglycosylation of strictosidine, an intermediate from which thousands of monoterpene indole alkaloids are derived. The steady state kinetics of SGD with a variety of strictosidine analogs revealed the substrate preferences of this enzyme at two key positions of the strictosidine substrate. Additionally, SGD from C. roseus turns over both strictosidine and its stereoisomer vincoside, indicating that although this enzyme prefers the naturally occurring diastereomer, the enzyme is not completely diastereoselective. The implications of the substrate specificity of SGD in metabolic engineering efforts of C. roseus are highlighted.