Unknown

Dataset Information

0

Sublancin is not a lantibiotic but an S-linked glycopeptide.


ABSTRACT: Sublancin is shown to be an S-linked glycopeptide containing a glucose attached to a cysteine residue, establishing a new post-translational modification. The activity of the S-glycosyl transferase was reconstituted in vitro, and the enzyme is shown to have relaxed substrate specificity, allowing the preparation of analogs of sublancin. Glycosylation is essential for its antimicrobial activity.

SUBMITTER: Oman TJ 

PROVIDER: S-EPMC3060661 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature

altmetric image

Publications

Sublancin is not a lantibiotic but an S-linked glycopeptide.

Oman Trent J TJ   Boettcher John M JM   Wang Huan H   Okalibe Xenia N XN   van der Donk Wilfred A WA  

Nature chemical biology 20110102 2


Sublancin is shown to be an S-linked glycopeptide containing a glucose attached to a cysteine residue, establishing a new post-translational modification. The activity of the S-glycosyl transferase was reconstituted in vitro, and the enzyme is shown to have relaxed substrate specificity, allowing the preparation of analogs of sublancin. Glycosylation is essential for its antimicrobial activity. ...[more]

Similar Datasets

| S-EPMC3985867 | biostudies-literature
| S-EPMC5732038 | biostudies-literature
| S-EPMC4336743 | biostudies-literature
| S-EPMC6551518 | biostudies-literature
| S-EPMC6112209 | biostudies-literature
| S-EPMC3191765 | biostudies-literature
| S-EPMC7331092 | biostudies-literature
| S-EPMC6408254 | biostudies-literature
| S-EPMC105782 | biostudies-literature
| S-EPMC2680678 | biostudies-literature