Progress in the study of atypical keracycline structure diversity

The marine microbial metabolism engineering and biosynthesis research team of the Key Laboratory of Tropical Marine Biological Resources and Ecology, South China Sea Institute of Oceanology, Chinese Academy of Sciences, has made new progress in the study of atypical keracycline structure diversity

Atypical keracycline natural products have rich and diverse skeleton types and excellent biological activity.

Early research team by bioinformatic analysis showed fluostatins ( FSTs ) biosynthetic gene cluster flsO1 encoding an oxidoreductase, and kinamycin presumed catalytic benzo fluorene structure hydroxylation AlpK is homologous enzymes

The analysis found that in the biological gene cluster of FST , the gene encoding flsP oxidoreductase may be related to the A epoxidation and dearomatization of FSTs .

This study provides new inspiration for the in vitro functional study of oxidoreductases FlsO1 and FlsP through genetic mutations and other in vivo studies, and at the same time expands the structural diversity of benzofluorene atypical keracycline

Associate researcher Yang Chunfang and Dr.

Information about Paper 1 : Chunfang Yang, ^# Chunshuai Huang, ^# Chunyan Fang, Liping Zhang, Siqiang Chen, Qingbo Zhang, Changsheng Zhang,* Wenjun Zhang.

Cover link of Paper 1 : https://pubs.

　　Information about Paper 2 : Chunshuai Huang, Chunfang Yang,* Wenjun Zhang, Liping Zhang, Yiguang Zhu, and Changsheng Zhang* Discovery of an unexpected 1,4-oxazepine-linked seco -fluostatin heterodimer by Inactivation of the oxidoreductase-encoding gene flsP .