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Org Lett. 2013 Jun 21;15(12):3062-5. doi: 10.1021/ol401247s. Epub 2013 May 30.

Breaking cyclic dipeptide prenyltransferase regioselectivity by unnatural alkyl donors.

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1
Institut für Pharmazeutische Biologie und Biotechnologie, Philipps-Universität Marburg, Deutschhausstrasse 17a, 35037 Marburg, Germany, and Fachbereich Chemie, Philipps-Universität Marburg, Hans-Meerwein-Strasse, 35032 Marburg, Germany.

Abstract

The behavior of five cyclic dipeptide prenyltransferases, responsible for C2-regular, C2-reverse, or C3-reverse prenylation, was investigated in the presence of the unnatural alkyl donors monomethylallyl and 2-pentenyl diphosphate. Both substrates were well accepted by the tested enzymes. Interestingly, C2-reverse and C3-reverse monoalkylated derivatives were identified as enzyme products in all of the enzyme assays. These findings indicate their similar reaction characteristics in the presence of unnatural alkyl donors.

PMID:
23721375
DOI:
10.1021/ol401247s
[Indexed for MEDLINE]
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