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

N Yerkes, JX Wu, E McCoy, MC Galan, S Chen, SE O'Connor

Research output: Contribution to journalArticle (Academic Journal)peer-review

11 Citations (Scopus)

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.
Translated title of the contributionSubstrate specificity and diasteroselectivity of strictosidine glucosidase, a key enzyme in monoterpene indole alkaloid biosynthesis
Original languageEnglish
Pages (from-to)3095 - 9098
Number of pages4
JournalBioorganic and Medicinal Chemistry Letters
Volume18 (10)
DOIs
Publication statusPublished - May 2008

Bibliographical note

Publisher: Elsevier

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