Article (Scientific journals)
Acetylhexosamine compounds enzymically released from Micrococcus lysodeikticus cell walls: III. The structure of di- and tetra-saccharides released from cell walls by lysozyme and Streptomyces F1 enzyme
Salton, M. R. J.; Ghuysen, Jean-Marie
1960In Biochimica et Biophysica Acta, 45, p. 355-363
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Keywords :
Carbohydrates; Micrococcus; Muramidase; Streptomyces; Chemistry; Metabolism
Abstract :
[en] Two compounds, both of which have been isolated from cell walls of Micrococcus lysodeikticus digested with lysozyme or Streptomyces F1 enzyme, have been identified as di- and tetra-saccharides. The reducing groups of the di- and tetra-saccharides and those of the high-molecular weight, non-dialysable compounds belong to muramic acid. [beta]-glucosidase yields free N-acetylglucosamine and N-acetylmuramic acid from the di- and tetra-saccharides. The proposed structure for the di-saccharide liberated by lysozyme and F1 is: 6-O-[beta]-N-acetylglucosaminyl-N-acetylmuramic acid. The tetra-saccharides isolated from lysozyme and F1 digests appear to be identical. The structure proposed for the tetra-saccharide isolated from lysozyme digested walls is: O-[beta]-N-acetylglucosaminyl-(I-->6)-O-[beta]-N-acetylmuraminyl-(I-->4)-O-[beta]-N-acetylglucosaminyl- (I-->6)-[beta]-N-acetylmuramic acid. Both lysozyme and Streptomyces F1 enzyme degrade di- and tetra-chitobiose, indicating their [beta](I-->4) N-acetyl hexosaminidase activity.
Disciplines :
Biochemistry, biophysics & molecular biology
Author, co-author :
Salton, M. R. J.;  Berkeley University of California - UC Berkeley > Department of Bacteriology
Ghuysen, Jean-Marie ;  Université de Liège - ULiège
Language :
English
Title :
Acetylhexosamine compounds enzymically released from Micrococcus lysodeikticus cell walls: III. The structure of di- and tetra-saccharides released from cell walls by lysozyme and Streptomyces F1 enzyme
Publication date :
04 December 1960
Journal title :
Biochimica et Biophysica Acta
ISSN :
0006-3002
eISSN :
1878-2434
Publisher :
Elsevier, Amsterdam, Netherlands
Volume :
45
Pages :
355-363
Peer reviewed :
Peer Reviewed verified by ORBi
Available on ORBi :
since 01 September 2011

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