Characterization of SepE and SepF for the N6-Glycosylated Adenine Structure Formation in Septacidin Biosynthesis

Wei Tang; Pengwei Li; Meng Chen; Zhengyan Guo; Yihua Chen

doi:10.1021/acs.orglett.0c01918

Characterization of SepE and SepF for the N⁶-Glycosylated Adenine Structure Formation in Septacidin Biosynthesis

Org Lett. 2020 Jul 2;22(13):5251-5254. doi: 10.1021/acs.orglett.0c01918. Epub 2020 Jun 21.

Authors

Wei Tang^{1

2}, Pengwei Li¹, Meng Chen^{1

2}, Zhengyan Guo^{1

2}, Yihua Chen^{1

2}

Affiliations

¹ State Key Laboratory of Microbial Resources and CAS Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
² University of Chinese Academy of Sciences, Beijing 100049, China.

PMID: 32567317
DOI: 10.1021/acs.orglett.0c01918

Abstract

Septacidin (1) represents a group of nucleoside antibiotics possessing a unique N⁶-glycosylated adenine core. They exhibit some fascinating bioactivities that are rare for other nucleoside antibiotics. Here we demonstrate that this unique structure in septacidin is formed by SepE and SepF. SepE is an unprecedented Fe(II)-dependent glycosyltransferase decorating the N⁶-position of AMP using ADP-l-glycero-β-d-manno-heptose (6) as a sugar donor. The Fe(II) may help SepE to bind AMP. SepF is an unusual glycosidase that detaches the N⁹-ribosyl-5-phosphate.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Adenine / chemistry*
Glycoside Hydrolases / metabolism*
Glycosylation
Purine Nucleosides / biosynthesis
Purine Nucleosides / chemistry

Substances

Purine Nucleosides
septacidin
Glycoside Hydrolases
Adenine