The LnmK Bifunctional Acyltransferase/Decarboxylase Specifying (2R)-Methylmalonyl-CoA and Employing Substrate-Assisted Catalysis for Polyketide Biosynthesis-Reference-Cited by-同舟云学术

The LnmK Bifunctional Acyltransferase/Decarboxylase Specifying (2R)-Methylmalonyl-CoA and Employing Substrate-Assisted Catalysis for Polyketide Biosynthesis

Published:2020-10-23 Issue:43 Volume:59 Page:4143-4147
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Lohman Jeremy R.¹^ORCID,Shen Ben^ORCID

Affiliation:

1. Department of Biochemistry, Purdue University, West Lafayette, Indiana 47907, United States

Funder

National Cancer Institute

National Institute of General Medical Sciences

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/acs.biochem.0c00749

Reference16 articles.

1. Leinamycin Biosynthesis Revealing Unprecedented Architectural Complexity for a Hybrid Polyketide Synthase and Nonribosomal Peptide Synthetase

2. Structure of the Bifunctional Acyltransferase/Decarboxylase LnmK from the Leinamycin Biosynthetic Pathway Revealing Novel Activity for a Double-Hot-Dog Fold

3. Bifunctional Acyltransferase/Decarboxylase LnmK as the Missing Link for β-Alkylation in Polyketide Biosynthesis

4. Characterization of thelnmKLMGenes Unveiling Key Intermediates for β-Alkylation in Leinamycin Biosynthesis

5. Lomaiviticin Biosynthesis Employs a New Strategy for Starter Unit Generation

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