Characterization of a Citrulline 4‐Hydroxylase from Nonribosomal Peptide GE81112 Biosynthesis and Engineering of Its Substrate Specificity for the Chemoenzymatic Synthesis of Enduracididine-Reference-Cited by-同舟云学术

Characterization of a Citrulline 4‐Hydroxylase from Nonribosomal Peptide GE81112 Biosynthesis and Engineering of Its Substrate Specificity for the Chemoenzymatic Synthesis of Enduracididine

Published:2019-11-11 Issue:52 Volume:58 Page:18854-18858
ISSN:1433-7851
Container-title:Angewandte Chemie International Edition
language:en
Short-container-title:Angewandte Chemie Intl Edit

Author:

Zwick Christian R.¹,Sosa Max B.¹,Renata Hans¹^ORCID

Affiliation:

1. Department of Chemistry The Scripps Research Institute 130 Scripps Way Jupiter FL 33458 USA

Funder

National Institute of General Medical Sciences

Publisher

Wiley

Subject

General Chemistry,Catalysis

Link

https://onlinelibrary.wiley.com/doi/pdf/10.1002/anie.201910659

Reference52 articles.

2. Specific, efficient, and selective inhibition of prokaryotic translation initiation by a novel peptide antibiotic

3. Novel Tetrapeptide Inhibitors of Bacterial Protein Synthesis Produced by a Streptomyces sp.

4. The Oligopeptide Permease Opp Mediates Illicit Transport of the Bacterial P-site Decoding Inhibitor GE81112

5. Inhibition of translation initiation complex formation by GE81112 unravels a 16S rRNA structural switch involved in P-site decoding

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