Expanding Substrate Promiscuity by Engineering a Novel Adenylating-Methylating NRPS Bifunctional Enzyme-Reference-Cited by-同舟云学术

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Expanding Substrate Promiscuity by Engineering a Novel Adenylating-Methylating NRPS Bifunctional Enzyme

Published:2016-06-03 Issue:14 Volume:17 Page:1328-1332
ISSN:1439-4227
Container-title:ChemBioChem
language:en
Short-container-title:ChemBioChem

Author:

Shrestha Sanjib K.¹,Garneau-Tsodikova Sylvie¹

Affiliation:

1. Department of Pharmaceutical Sciences; University of Kentucky; BioPharm Complex (Room 423); 789 South Limestone Street Lexington KY 40536-0596 USA

Publisher

Wiley

Subject

Organic Chemistry,Molecular Biology,Molecular Medicine,Biochemistry

Reference30 articles.

1. Nonribosomal peptides: from genes to products

2. Conformational Dynamics in the Acyl-CoA Synthetases, Adenylation Domains of Non-ribosomal Peptide Synthetases, and Firefly Luciferase

3. The A9 Core Sequence from NRPS Adenylation Domain Is Relevant for Thioester Formation

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

5. Recent developments in bisintercalator natural products

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2. Structural insights into the diverse prenylating capabilities of DMATS prenyltransferases;Natural Product Reports;2024

3. Current Trends in Biosynthesis, Extraction, Purification, and Refining of Antibiotics;Recent Advances in Industrial Biochemistry;2024

4. Unimodular Methylation by Adenylation–Thiolation Domains Containing an Embedded Methyltransferase;Journal of Molecular Biology;2020-10

5. A thorough analysis and categorization of bacterial interrupted adenylation domains, including previously unidentified families;RSC Chemical Biology;2020

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