Interrupted adenylation domains: unique bifunctional enzymes involved in nonribosomal peptide biosynthesis-Reference-Cited by-同舟云学术

Interrupted adenylation domains: unique bifunctional enzymes involved in nonribosomal peptide biosynthesis

Published:2015 Issue:5 Volume:32 Page:641-653
ISSN:0265-0568
Container-title:Natural Product Reports
language:en
Short-container-title:Nat. Prod. Rep.

Author:

Labby Kristin J.¹²³⁴⁵,Watsula Stoyan G.⁶⁷⁸⁵,Garneau-Tsodikova Sylvie⁹¹⁰¹¹⁵

Affiliation:

1. Beloit College

2. Department of Chemistry

3. 700 College Street

4. Beloit

5. USA

6. University of Michigan

7. Department of Medicinal Chemistry in the College of Pharmacy

8. Ann Arbor

9. University of Kentucky

10. Department of Pharmaceutical Sciences in the College of Pharmacy

11. Lexington

Abstract

This highlight focuses on one of Nature's key strategies to doubly modify an amino acid during nonribosomal peptide biosynthesis by using a single enzyme, an interrupted adenylation domain.

Funder

National Science Board

Publisher

Royal Society of Chemistry (RSC)

Subject

Organic Chemistry,Drug Discovery,Biochemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2015/NP/C4NP00120F

Reference80 articles.

1. Nonproteinogenic Amino Acid Building Blocks for Nonribosomal Peptide and Hybrid Polyketide Scaffolds

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3. Cloning and characterization of the biosynthetic gene cluster for kutznerides

4. In Vitro Reconstitution of the Pseudomonas aeruginosa Nonribosomal Peptide Synthesis of Pyochelin: Characterization of Backbone Tailoring Thiazoline Reductase and N-Methyltransferase Activities

5. Yersiniabactin Synthetase

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