Analysis of the enzymatic cleavage (beta elimination) of the capsular K5 polysaccharide of Escherichia coli by the K5-specific coliphage: reexamination.
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.
Hänfling
P
P
Max-Planck-Institut für Immunbiologie, Freiburg, Germany.
Shashkov
A S
AS
Jann
B
B
Jann
K
K
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*
D011135:Polysaccharides, Bacterial; C050673:capsular polysaccharide K5; D011133:Polysaccharide-Lyases