A bacteriophage-associated glycanase cleaving beta-pyranosidic linkages of 3-deoxy-D-manno-2-octulosonic acid (KDO).
A bacteriophage growing on Escherichia coli K13, K20, and K23 strains carries a glycanase that catalyzes the hydrolytic cleavage of the beta-ketopyranosidic linkages of 3-deoxy-D-manno-2-octulosonic acid (KDO) in the respective capsular polysaccharides. The main cleavage product of the K23 polysaccharide has been identified by 1H- and 13C-n.m.r. spectroscopy as beta beta Ribfl----7 beta KDOp2----3-beta Ribfl----7KDO. Cleavage of polysaccharides containing alpha-pyranosidic, or 5-substituted beta-pyranosidic KDO is not catalyzed by the enzyme.
F
F
Altmann
B
B
Kwiatkowski
S
S
Stirm
L
L
März
F M
FM
Unger
D002236:Carbohydrate Conformation; D003090:Coliphages / Q000201:enzymology*; D006026:Glycoside Hydrolases / Q000378:metabolism*; D009682:Magnetic Resonance Spectroscopy; D013379:Substrate Specificity; D013400:Sugar Acids / Q000378:metabolism*
D013400:Sugar Acids; C002532:2-keto-3-deoxyoctonate; D006026:Glycoside Hydrolases; C020668:glycanase