Engineering of Chimeric Polyketide Synthases Using SYNZIP Docking Domains-Reference-Cited by-同舟云学术

Engineering of Chimeric Polyketide Synthases Using SYNZIP Docking Domains

Published:2019-01-25 Issue:3 Volume:14 Page:426-433
ISSN:1554-8929
Container-title:ACS Chemical Biology
language:en
Short-container-title:ACS Chem. Biol.

Author:

Klaus Maja¹²^ORCID,D’Souza Alicia D.²,Nivina Aleksandra²,Khosla Chaitan²^ORCID,Grininger Martin¹^ORCID

Affiliation:

1. Institute of Organic Chemistry and Chemical Biology, Buchmann Institute for Molecular Life Sciences, Goethe University Frankfurt, Max-von-Laue-Str. 15, 60438 Frankfurt am Main, Germany

2. Departments of Chemistry and Chemical Engineering and Stanford ChEM-H, Stanford University, Stanford, California 94305, United States

Funder

LOEWE Zentrum AdRIA

National Institute of General Medical Sciences

Volkswagen Foundation

Fondation pour la Recherche Medicale

Publisher

American Chemical Society (ACS)

Subject

Molecular Medicine,General Medicine,Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acschembio.8b01060

Reference36 articles.

1. Computational identification and analysis of orphan assembly-line polyketide synthases

2. Alteration of Polyketide Stereochemistry from anti to syn by a Ketoreductase Domain Exchange in a Type I Modular Polyketide Synthase Subunit

3. Comprehensive in Vitro Analysis of Acyltransferase Domain Exchanges in Modular Polyketide Synthases and Its Application for Short-Chain Ketone Production

4. Combinatorial polyketide biosynthesis by de novo design and rearrangement of modular polyketide synthase genes

5. Protein-Protein Interactions, Not Substrate Recognition, Dominate the Turnover of Chimeric Assembly Line Polyketide Synthases

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