Peptidyl Thiophenols as Substrates for Nonribosomal Peptide Cyclases

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

doi:10.1002/anie.200352787

Peptidyl Thiophenols as Substrates for Nonribosomal Peptide Cyclases

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

Research output: Contribution to journal › Article › peer-review

57 Scopus citations

Abstract

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 language	English
Pages (from-to)	493-498
Number of pages	6
Journal	Angewandte Chemie International Edition in English
Volume	43
Issue number	4
DOIs	https://doi.org/10.1002/anie.200352787
State	Published - 16 Jan 2004
Externally published	Yes

Keywords

Antibiotics
Biomimetic synthesis
Cyclization
Enzyme catalysis
Peptides

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abstract = "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).",

keywords = "Antibiotics, Biomimetic synthesis, Cyclization, Enzyme catalysis, Peptides",

author = "Sieber, {Stephan A.} and Junhua Tao and Walsh, {Christopher T.} and Marahiel, {Mohamed A.}",

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AU - Tao, Junhua

AU - Walsh, Christopher T.

AU - Marahiel, Mohamed A.

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N2 - 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).

AB - 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).

KW - Antibiotics

KW - Biomimetic synthesis

KW - Cyclization

KW - Enzyme catalysis

KW - Peptides

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ER -

Peptidyl Thiophenols as Substrates for Nonribosomal Peptide Cyclases

Abstract

Keywords

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