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

Yerkes, N., Wu, J. X., McCoy, E., Galan, M. C., Chen, S., & O'Connor, S. E. (2008). Substrate specificity and diastereoselectivity of strictosidine glucosidase, a key enzyme in monoterpene indole alkaloid biosynthesis. Bioorganic & Medicinal Chemistry Letters, 18(10), 3095-3098. doi:10.1016/j.bmcl.2007.11.063.

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Item Permalink: https://hdl.handle.net/21.11116/0000-0002-A97F-2 Version Permalink: https://hdl.handle.net/21.11116/0000-0009-3D94-C
Genre: Journal Article

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SOC016.pdf (Publisher version), 207KB
 
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SOC016s1.pdf (Supplementary material), 302KB
 
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https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2474460/ (Postprint)
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 Creators:
Yerkes, Nancy1, Author
Wu, Jia Xin1, Author
McCoy, Elizabeth1, Author
Galan, M. Carmen1, Author
Chen, Shi1, Author
O'Connor, Sarah E.1, Author           
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1external, ou_persistent22              

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Free keywords: CATHARANTHUS-ROSEUS; PERIWINKLEPharmacology & Pharmacy; Chemistry;
 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. (c) 2007 Elsevier Ltd. All rights reserved.

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Language(s): eng - English
 Dates: 2008
 Publication Status: Issued
 Pages: 4
 Publishing info: -
 Table of Contents: -
 Rev. Type: -
 Identifiers: Other: SOC016
DOI: 10.1016/j.bmcl.2007.11.063
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Title: Bioorganic & Medicinal Chemistry Letters
  Other : Bioorg. Med. Chem. Lett.
Source Genre: Journal
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Publ. Info: Oxford : Pergamon
Pages: - Volume / Issue: 18 (10) Sequence Number: - Start / End Page: 3095 - 3098 Identifier: ISSN: 0960-894X
CoNE: https://pure.mpg.de/cone/journals/resource/954925579103