Literature DB >> 3707579

A bacteriophage-associated glycanase cleaving beta-pyranosidic linkages of 3-deoxy-D-manno-2-octulosonic acid (KDO).

F Altmann, B Kwiatkowski, S Stirm, L März, F M Unger.   

Abstract

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.

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Year:  1986        PMID: 3707579     DOI: 10.1016/0006-291x(86)90914-9

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  2 in total

1.  Escherichia coli K1's capsule is a barrier to bacteriophage T7.

Authors:  Dean Scholl; Sankar Adhya; Carl Merril
Journal:  Appl Environ Microbiol       Date:  2005-08       Impact factor: 4.792

2.  Detection of Escherichia coli K95 strains by bacteriophages.

Authors:  W Nimmich
Journal:  J Clin Microbiol       Date:  1994-11       Impact factor: 5.948

  2 in total

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