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Peptidyl Thiophenols as Substrates for Nonribosomal Peptide Cyclases
Author(s) -
Sieber Stephan A.,
Tao Junhua,
Walsh Christopher T.,
Marahiel Mohamed A.
Publication year - 2004
Publication title -
angewandte chemie international edition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.831
H-Index - 550
eISSN - 1521-3773
pISSN - 1433-7851
DOI - 10.1002/anie.200352787
Subject(s) - nonribosomal peptide , acylation , thioester , peptide , enzyme , chemistry , biochemistry , combinatorial chemistry , stereochemistry , biosynthesis , catalysis
Activity‐based enzyme acylation : Although small peptides are specifically cyclized by nonribosomal peptide cyclases (thioesterases, TEs) in nature, artificial N ‐acetylcysteamine thioester (SNAC) mimics have often failed to act as substrates for these enzymes in vitro. However, new reactive peptidyl aromatic thioesters solve this problem by selective acylation of the enzyme active site (see scheme).