Nagar, R and Rao, Alka (2017) An iterative glycosyltransferase EntS catalyzes transfer and extension of O- and S-linked monosaccharide in enterocin 96. Glycobiology, 27 (8). pp. 766-776. ISSN 0959-6658
Full text not available from this repository. (Request a copy)Abstract
Glycosyltransferases are essential tools for in vitro-glycoengineering. Bacteria harbor an unexplored variety of protein glycosyltransferases. Here, we describe a peptide glycosyltransferase (EntS) encoded by ORF0417 of Enterococcus faecalis TX0104. EntS di-glycosylates linear peptide of enterocin 96- a known antibacterial, in vitro. It is capable of transferring as well as extending the glycan onto the peptide in an iterative sequential dissociative manner. It can catalyze multiple linkages: Glc/Gal(-O)Ser/Thr, Glc/Gal(-S)Cys and Glc/Gal(β)Glc/Gal(-O/S)Ser/Thr/Cys, in one pot. Using EntS generated glycovariants of enterocin 96 peptide, size and identity of the glycan are found to influence bioactivity of the peptide. The study identifies EntS as an enzyme worth pursuing, for in vitro peptide glycoengineering.
| Item Type: | Article |
|---|---|
| Additional Information: | Copyright of this article belongs to Oxford Academic |
| Uncontrolled Keywords: | Dissociative mechanism; Enterocin; Glycosylation; O- and S-glycosyltransferase; Sequential transfer |
| Subjects: | Q Science > QR Microbiology |
| Depositing User: | Dr. K.P.S.Sengar |
| Date Deposited: | 28 Mar 2018 07:57 |
| Last Modified: | 02 Apr 2018 09:37 |
| URI: | http://crdd.osdd.net/open/id/eprint/2076 |
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