Back to Search Start Over

Isolation, enzyme-bound structure and antibacterial activity of platencin A1 from Streptomyces platensis.

Authors :
Singh SB
Ondeyka JG
Herath KB
Zhang C
Jayasuriya H
Zink DL
Parthasarathy G
Becker JW
Wang J
Soisson SM
Source :
Bioorganic & medicinal chemistry letters [Bioorg Med Chem Lett] 2009 Aug 15; Vol. 19 (16), pp. 4756-9. Date of Electronic Publication: 2009 Jun 17.
Publication Year :
2009

Abstract

Natural products continue to serve as one of the best sources for discovery of antibacterial agents as exemplified by the recent discoveries of platensimycin and platencin. Chemical modifications as well as discovery of congeners are the main sources for gaining knowledge of structure-activity relationship of natural products. Screening for congeners in the extracts of the fermentation broths of Streptomyces platensis led to the isolation of platencin A(1), a hydroxy congener of platencin. The hydroxylation of the tricyclic enone moiety negatively affected the antibacterial activity and appears to be consistent with the hydrophobic binding pocket of the FabF. Isolation, structure, enzyme-bound structure and activity of platencin A(1) and two other congeners have been described.

Details

Language :
English
ISSN :
1464-3405
Volume :
19
Issue :
16
Database :
MEDLINE
Journal :
Bioorganic & medicinal chemistry letters
Publication Type :
Academic Journal
Accession number :
19581087
Full Text :
https://doi.org/10.1016/j.bmcl.2009.06.061