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Tryptophan C5‐ , C6‐ and C7 ‐Prenylating Enzymes Displaying a Preference for C‐6 of the Indole Ring in the Presence of Unnatural Dimethylallyl Diphosphate Analogues
Author(s) -
Winkelblech Julia,
Liebhold Mike,
Gunera Jakub,
Xie Xiulan,
Kolb Peter,
Li ShuMing
Publication year - 2015
Publication title -
advanced synthesis and catalysis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.541
H-Index - 155
eISSN - 1615-4169
pISSN - 1615-4150
DOI - 10.1002/adsc.201400958
Subject(s) - prenyltransferase , chemistry , indole test , stereochemistry , tryptophan , moiety , enzyme , ring (chemistry) , alkylation , prenylation , biochemistry , organic chemistry , amino acid , catalysis
The behavior of four dimethylallyltryptophan synthases (DMATSs) (5‐DMATS and 5‐DMATS Sc as tryptophan C5‐ prenyltransferases, and 6‐DMATS Sa and 6‐DMATS Sv as C6 ‐prenyltransferases) and one L ‐tyrosine prenyltransferase with a tryptophan C7 ‐prenyltransferase activity was investigated in the presence of two unnatural alkyl donors (methylallyl and 2‐pentenyl diphosphate) and one benzyl donor (benzyl diphosphate). Detailed biochemical investigations revealed the acceptance of these dimethylallyl diphosphate (DMAPP) analogues by all tested enzymes with different relative activities. Enzyme products with the allyl or benzyl moiety attached to different positions were identified in the reaction mixtures, whereby C‐6 alkylated or benzylated L ‐tryptophan was found as one of the main products. This observation demonstrates a preference of the five prenyltransferases toward C‐6 of the indole ring in the presence of unnatural DMAPP derivatives. Molecular dynamics simulation experiments with a homologous model of 5‐DMATS explained well its reactions with methylallyl and 2‐pentenyl diphosphate. Furthermore this study expands significantly the potential usage of tryptophan prenylating enzymes as biocatalysts for Friedel–Crafts alkylation.