The architectures of iterative type I PKS and FAS-Reference-Cited by-同舟云学术

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The architectures of iterative type I PKS and FAS

Published:2018 Issue:10 Volume:35 Page:1046-1069
ISSN:0265-0568
Container-title:Natural Product Reports
language:en
Short-container-title:Nat. Prod. Rep.

Author:

Herbst Dominik A.¹²³⁴^ORCID,Townsend Craig A.⁵⁶⁷⁸^ORCID,Maier Timm¹²³⁴^ORCID

Affiliation:

1. Department Biozentrum

2. University of Basel

3. 4056 Basel

4. Switzerland

5. Department of Chemistry

6. Johns Hopkins University

7. Baltimore

8. USA

Abstract

The architectures of fatty acid synthases and iterative polyketide synthases are remarkably divergent despite their related biosynthetic logics.

Funder

Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung

National Institutes of Health

Werner Siemens Foundation

Publisher

Royal Society of Chemistry (RSC)

Subject

Organic Chemistry,Drug Discovery,Biochemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2018/NP/C8NP00039E

Reference185 articles.

1. Structure and function of eukaryotic fatty acid synthases

2. An unusually large multifunctional polypeptide in the erythromycin-producing polyketide synthase of Saccharopolyspora erythraea

3. The multienzyme architecture of eukaryotic fatty acid synthases

4. Characterization of the Polyspecific Transferase of Murine Type I Fatty Acid Synthase (FAS) and Implications for Polyketide Synthase (PKS) Engineering

5. Architecture of a Fungal Fatty Acid Synthase at 5 Å Resolution

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3. The malonyl/acetyl-transferase from murine fatty acid synthase is a promiscuous engineering tool for editing polyketide scaffolds;Communications Chemistry;2024-08-24

4. The structure of full-length AFPK supports the ACP linker in a role that regulates iterative polyketide and fatty acid assembly;2024-07-23

5. Structural and Computational Insights into the Noncanonical Aromatization in Fungal Polyketide Biosynthesis;ACS Catalysis;2024-07-03

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