4.7 Review

Protein-protein interactions in cis-AT polyketide synthases

期刊

NATURAL PRODUCT REPORTS
卷 35, 期 10, 页码 1082-1096

出版社

ROYAL SOC CHEMISTRY
DOI: 10.1039/c8np00058a

关键词

-

资金

  1. US National Institutes of Health [DK042303, GM076477, GM115601]
  2. Margaret J. Hunter Professorship
  3. NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES [R37DK042303, R01DK042303] Funding Source: NIH RePORTER

向作者/读者索取更多资源

Covering: up to the end of 2018Polyketides are a valuable source of bioactive and clinically important molecules. The biosynthesis of these chemically complex molecules has led to the discovery of equally complex polyketide synthase (PKS) pathways. Crystallography has yielded snapshots of individual catalytic domains, di-domains, and multi-domains from a variety of PKS megasynthases, and cryo-EM studies have provided initial views of a PKS module in a series of defined biochemical states. Here, we review the structural and biochemical results that shed light on the protein-protein interactions critical to catalysis by PKS systems with an embedded acyltransferase. Interactions include those that occur both within and between PKS modules, as well as with accessory enzymes.

作者

我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。

评论

主要评分

4.7
评分不足

次要评分

新颖性
-
重要性
-
科学严谨性
-
评价这篇论文

推荐

暂无数据
暂无数据