title: Analysis of the enzymatic cleavage (beta elimination) of the capsular K5 polysaccharide of Escherichia coli by the K5-specific coliphage: reexamination.
abstract: The capsular K5 polysaccharide of Escherichia coli is the receptor of the capsule-specific coliphage K5, which harbors an enzyme that degrades the capsular K5 polysaccharide to a number of oligosaccharides. Analysis of the degradation products using gel permeation chromatography, the periodate-thiobarbituric acid and bicinchoninic acid reactions, and nuclear magnetic resonance spectroscopy showed that the major reaction products are hexa-, octa-, and decasaccharides with 4,5-unsaturated glucuronic acid (delta4,5GlcA) at their nonreducing end. Thus, the bacteriophage enzyme is a K5 polysaccharide lyase and not, as we had reported previously, an endo-N-acetylglucosaminidase.
authors: Max-Planck-Institut für Immunbiologie, Freiburg, Germany.
authors: P
authors: P
authors: Hänfling
authors: A S
authors: AS
authors: Shashkov
authors: B
authors: B
authors: Jann
authors: K
authors: K
authors: Jann
mesh_terms: D016667:Bacterial Capsules; D002240:Carbohydrate Sequence; D003090:Coliphages / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism* / Q000821:virology*; D009682:Magnetic Resonance Spectroscopy; D008969:Molecular Sequence Data; D015394:Molecular Structure; D011133:Polysaccharide-Lyases / Q000378:metabolism; D011135:Polysaccharides, Bacterial / Q000737:chemistry / Q000378:metabolism*
chemical_list: D011135:Polysaccharides, Bacterial; C050673:capsular polysaccharide K5; D011133:Polysaccharide-Lyases