Preparation of branched hexasaccharides by the action of a viral lyase on Klebsiella K14 polysaccharide.
Klebsiella K14 capsular polysaccharide was degraded by a bacteriophage-borne enzyme to afford oligosaccharides A-C which were studied by one- and two-dimensional n.m.r. spectroscopy. A and B were the repeating-unit hexasaccharide and pyruvylated hexasaccharide, respectively, while C was a dodecasaccharide. Each oligomer was terminated by a reducing mannose and a non-reducing 4-deoxy-alpha-L-threo-hex-4-enopyranosyluronic acid residue, indicating that the phage enzyme had cleaved the beta-D-Manp-(1----4)-beta-D-GlcpA linkages in the polysaccharide by a lyase, rather than the more common glycosidase, activity found with other Klebsiella bacteriophages. In this respect, the depolymerisation resembles those reported for the capsular polysaccharides of Klebsiella K5 and K64
Parolis
H
H
School of Pharmaceutical Sciences, Rhodes University, Grahamstown, South Africa.
Parolis
L A
LA
Dutton
G G
GG
D007709:Klebsiella / Q000378:metabolism*; D008190:Lyases / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D009844:Oligosaccharides / Q000378:metabolism*; D011135:Polysaccharides, Bacterial / Q000378:metabolism*; D014764:Viral Proteins / Q000378:metabolism*
D009844:Oligosaccharides; D011135:Polysaccharides, Bacterial; D014764:Viral Proteins; D008190:Lyases