DUF3380 Domain from a Salmonella Phage Endolysin Shows Potent N-Acetylmuramidase Activity.

ABSTRACT:

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Bacteriophage-encoded endolysins are highly diverse enzymes that cleave the bacterial peptidoglycan layer. Current research focuses on their potential applications in medicine, in food conservation, and as biotechnological tools. Despite the wealth of applications relying on the use of endolysin, little is known about the enzymatic properties of these enzymes, especially in the case of endolysins of bacteriophages infecting Gram-negative species. Automated genome annotations therefore remain to be confirmed. Here, we report the biochemical analysis and cleavage site determination of a novel Salmonella bacteriophage endolysin, Gp110, which comprises an uncharacterized domain of unknown function (DUF3380; pfam11860) in its C terminus and shows a higher specific activity (3

SUBMITTER: Rodriguez-Rubio L 

PROVIDER: S-EPMC4968549 | biostudies-literature | 2016 Aug

REPOSITORIES: biostudies-literature