Peptidyl Thiophenols as Substrates for Nonribosomal Peptide Cyclases

Stephan A. Sieber, Junhua Tao, Christopher T. Walsh, Mohamed A. Marahiel

Research output: Contribution to journalArticlepeer-review

55 Scopus citations


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).

Original languageEnglish
Pages (from-to)493-498
Number of pages6
JournalAngewandte Chemie International Edition in English
Issue number4
StatePublished - 16 Jan 2004
Externally publishedYes


  • Antibiotics
  • Biomimetic synthesis
  • Cyclization
  • Enzyme catalysis
  • Peptides


Dive into the research topics of 'Peptidyl Thiophenols as Substrates for Nonribosomal Peptide Cyclases'. Together they form a unique fingerprint.

Cite this