Substrate specificity and diastereoselectivity of strictosidine glucosidase, a key enzyme in monoterpene indole alkaloid biosynthesis

Nancy Yerkes, Jia Xin Wu, Elizabeth McCoy, M. Carmen Galan, Shi Chen, Sarah E. O'Connor

Research output: Contribution to journalArticlepeer-review

16 Citations (Scopus)


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
Original languageEnglish
Pages (from-to)3095-3098
Number of pages4
JournalBioorganic & Medicinal Chemistry Letters
Issue number10
Publication statusPublished - 2008

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