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

Yerkes, Nancy, Wu, Jia Xin, McCoy, Elizabeth, Galan, M. Carmen, Chen, Shi and O'Connor, Sarah E. (2008) Substrate specificity and diastereoselectivity of strictosidine glucosidase, a key enzyme in monoterpene indole alkaloid biosynthesis. Bioorganic & Medicinal Chemistry Letters, 18 (10). pp. 3095-3098. ISSN 1464-3405

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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

Item Type: Article
Faculty \ School: Faculty of Science > School of Chemistry
Depositing User: Rhiannon Harvey
Date Deposited: 21 Mar 2012 15:17
Last Modified: 17 Mar 2020 16:16
URI: https://ueaeprints.uea.ac.uk/id/eprint/38415
DOI: 10.1016/j.bmcl.2007.11.063

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