Reference : LL-diaminopimelic acid containing peptidoglycans in walls of Streptomyces sp. and of ...
Scientific journals : Article
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/2268/85150
LL-diaminopimelic acid containing peptidoglycans in walls of Streptomyces sp. and of Clostridium perfringens (type A).
English
Leyh-Bouille, Mélina [Université de Liège - ULg > > Service de Bactériologie > >]
Bonaly, Roger [Faculté de Pharamacie de Nancy > Service de Chimie Biologique > > >]
Ghuysen, Jean-Marie [Université de Liège - ULg > > Service de Bactériologie > > >]
Tinelli, Regina [Institut Pasteur (Paris) > > > >]
Tipper, Donald [University of Wisconsin > Department of Pharmacology > > >]
21-Jul-1970
Biochemistry
American Chemical Society
9
15
2944-2952
Yes (verified by ORBi)
International
0006-2960
1520-4995
Washington
DC
[en] alanine analysis ; amino acid sequence ; amino acids ; cell wall ; chromatography ; chromatography ; clostridium perfringens ; electrophoresis ; endopeptidases ; escherichia coli ; glutamates ; glycine ; muramidase ; myxococcales ; peptides analysis ; pimelic acids ; polysaccharides analysis ; stereoisomerism ; streptomyces analysis ; gel ; thin layer
[en] In a major part of the wall peptidoglycans of Streptomyces sp. and of Clostridium perfringens, L-alanyl-D-isoglutaminyl-(L1)-LL-diaminopimelyl-(L1)-D-alanine peptides are cross-linked via D-alanylglycyl-(L2)-LL-diaminopimelic acid linkages (peptidoglycan of the chemotype II group). The Myxobacter AL-I endopeptidase hydrolyzes both D-alanyl-glycine and glycyl-LL-diaminopimelic acid linkages in the walls of C. perfringens, liberating free glycine. In contrast, the Myxobacter AL-I endopeptidase hydrolyzes only D-alanyl-glycine linkages in walls of Streptomyces sp. and the liberation of the glycine residues requires subsequent treatment with an aminopeptidase. No explanation for this observation can be proposed at this time. A minor component of the AL-I endopeptidase hydrolysate of the Streptomyces and C. perfringens walls is a resistant peptide dimer. Analyses indicate that the cross-link in this dimer may be mediated through LL-diamino-pimelylglycyl-LL-diaminopimelic acid linkages.
The C termini of the peptide moieties in the wall peptidoglycans are either D-alanine or LL-diarninopimelic acid but never D-alanyl-D-alanine, thus indicating the presence in these microorganisms of carboxypeptidases similar to those of Escherichia coli.
Fonds de la Recherche Fondamentale Collective
Researchers ; Professionals
http://hdl.handle.net/2268/85150
10.1021/bi00817a002

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