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Reinvestigation of a Cyclic Dipeptide N ‐Prenyltransferase Reveals Rearrangement of N‐1 Prenylated Indole Derivatives
Author(s) -
Ruan HanLi,
Yin WenBing,
Wu JiZhou,
Li ShuMing
Publication year - 2008
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.200700723
Subject(s) - prenyltransferase , dipeptide , prenylation , indole test , chemistry , stereochemistry , trichloroacetic acid , ring (chemistry) , amino acid , enzyme , organic chemistry , biochemistry
Converting revere to regular : Reinvestigation of cyclic dipeptide N ‐prenyltransferase (CdpNPT) revealed that the enzymatic products are derivatives that carry 3′‐(3′,3′)‐dimethylallyl moieties at the N‐1 position of the indole ring, and they undergo rearrangement in the presence of acids, such as trichloroacetic acid, used for termination of enzymatic reactions and protein precipitation (see scheme). The rearrangement can be avoided by using MeOH instead of acid for termination and protein precipitation.