Engineering the Substrate Specificity of a Modular Polyketide Synthase for Installation of Consecutive Non-Natural Extender Units-Reference-Cited by-同舟云学术

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Engineering the Substrate Specificity of a Modular Polyketide Synthase for Installation of Consecutive Non-Natural Extender Units

Published:2019-01-24 Issue:5 Volume:141 Page:1961-1969
ISSN:0002-7863
Container-title:Journal of the American Chemical Society
language:en
Short-container-title:J. Am. Chem. Soc.

Author:

Kalkreuter Edward¹²,CroweTipton Jared M.¹,Lowell Andrew N.³^ORCID,Sherman David H.³⁴^ORCID,Williams Gavin J.¹²^ORCID

Affiliation:

1. Department of Chemistry, NC State University, Raleigh, North Carolina 27695, United States

2. Comparative Medicine Institute, NC State University, Raleigh, North Carolina 27695, United States

3. Life Sciences Institute, Department of Medicinal Chemistry, University of Michigan, Ann Arbor, Michigan 48109, United States

4. Department of Chemistry and Department of Microbiology & Immunology, University of Michigan, Ann Arbor, Michigan 48109, United States

Funder

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Colloid and Surface Chemistry,Biochemistry,General Chemistry,Catalysis

Link

https://pubs.acs.org/doi/pdf/10.1021/jacs.8b10521

Reference50 articles.

1. Atlas of nonribosomal peptide and polyketide biosynthetic pathways reveals common occurrence of nonmodular enzymes

2. Chapter 7 Formation and Characterization of Acyl Carrier Protein–Linked Polyketide Synthase Extender Units

3. Hydroxymalonyl-acyl carrier protein (ACP) and aminomalonyl-ACP are two additional type I polyketide synthase extender units

4. Biosynthesis of the Allylmalonyl-CoA Extender Unit for the FK506 Polyketide Synthase Proceeds through a Dedicated Polyketide Synthase and Facilitates the Mutasynthesis of Analogues

5. Uncovering the Formation and Selection of Benzylmalonyl-CoA from the Biosynthesis of Splenocin and Enterocin Reveals a Versatile Way to Introduce Amino Acids into Polyketide Carbon Scaffolds

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

3. The malonyl/acetyl-transferase from murine fatty acid synthase is a promiscuous engineering tool for editing polyketide scaffolds;2024-02-09

4. Current State‐of‐the‐Art Toward Chemoenzymatic Synthesis of Polyketide Natural Products;ChemBioChem;2023-09-15

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