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

Bioorganic and Medicinal Chemistry Letters

Volumn 18, Issue 10, 2008, Pages 3095-3098

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

^a MASSACHUSETTS INSTITUTE OF TECHNOLOGY   (United States)

Author keywords

Alkaloid; Biosynthesis; Glucosidase; Strictosidine

Indexed keywords

GLUCOSIDASE; INDOLE ALKALOID; NATURAL PRODUCT; STRICTOSIDINE; STRICTOSIDINE GLUCOSIDASE; TERPENE; VINCOSIDE;

ARTICLE; CATHARANTHUS ROSEUS; DEGLYCOSYLATION; DIASTEREOISOMER; DRUG SYNTHESIS; ENZYME SPECIFICITY; NONHUMAN; STEADY STATE; STEREOCHEMISTRY; STEREOISOMERISM;

CATHARANTHUS; GLUCOSIDASES; INDOLE ALKALOIDS; KINETICS; MOLECULAR STRUCTURE; STEREOISOMERISM; SUBSTRATE SPECIFICITY; TERPENES;

CATHARANTHUS ROSEUS;

EID: 43549119034     PISSN: 0960894X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bmcl.2007.11.063     Document Type: Article

References (19)

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10. Strictosidine glucosidase (SGD) was expressed in Escherichia coli as an N-terminal maltose-binding protein (MBP) or C-terminal 6 His-tag fusion using a codon optimized synthetic gene previously described in Ref. 5. The MBP fusion was used for the determination of all kinetic constants.
11. Synthesis of strictosidine analogs has been previously described in Ref. 5. Briefly, strictosidine analogs 1, 2, 5, 8, and 9 were synthesized enzymatically by incubating strictosidine synthase with secologanin and the corresponding tryptamine analog followed by purification via preparative HPLC. Strictosidine analogs 3, 4, 6, and 7 were synthesized as diastereomeric mixtures chemically by incubating secologanin and the corresponding tryptamine analog in pH 2, 100 mM maleic acid. The strictosidine diastereomers were purified by preparative HPLC. Exact masses and representative NMR data of the purified products are reported in Supplementary Material.
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