Functional analysis of AtlA, the major N-acetylglucosaminidase of Enterococcus faecalis.

Article, Other literature type English OPEN
Eckert , Catherine; Lecerf , Maxime; Dubost , Lionel; Arthur , Michel; Mesnage , Stéphane;
(2006)
  • Publisher: American Society for Microbiology
  • Related identifiers: doi: 10.1128/JB.01145-06, pmc: PMC1698247
  • Subject: MESH: Acetylglucosaminidase | Enzymes and Proteins | MESH : Peptidoglycan | MESH: Peptidoglycan | MESH : Bacterial Proteins | MESH : Recombinant Proteins | MESH: Escherichia coli | MESH: Humans | MESH: Tandem Mass Spectrometry | MESH: Bacterial Proteins | MESH: Enterococcus faecalis | MESH : Escherichia coli | MESH: Recombinant Proteins | [ SDV.BBM ] Life Sciences [q-bio]/Biochemistry, Molecular Biology | MESH : Tandem Mass Spectrometry | [SDV.BBM]Life Sciences [q-bio]/Biochemistry, Molecular Biology | MESH : Humans | MESH : Enterococcus faecalis | MESH : Acetylglucosaminidase

International audience; The major peptidoglycan hydrolase of Enterococcus faecalis, AtlA, has been identified, but its enzyme activity remains unknown. We have used tandem mass spectrometry analysis of peptidoglycan hydrolysis products obtained using the purified protei... View more
Share - Bookmark