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通过非天然烷基供体打破环二肽香叶基转移酶的区域选择性。

Breaking cyclic dipeptide prenyltransferase regioselectivity by unnatural alkyl donors.

机构信息

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.

出版信息

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

DOI:10.1021/ol401247s
PMID:23721375
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.

摘要

五种环二肽类异戊烯基转移酶的行为,负责 C2-规则、C2-反向或 C3-反向异戊烯基化,在非天然烷基供体单甲基丙烯基和 2-戊烯基二磷酸的存在下进行了研究。两种底物都被测试的酶很好地接受了。有趣的是,在所有的酶促反应中,C2-反向和 C3-反向单烷基化衍生物被鉴定为酶产物。这些发现表明,在非天然烷基供体存在的情况下,它们具有相似的反应特性。

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