References of "Bonaly, Roger"
     in
Bookmark and Share    
Full Text
Peer Reviewed
See detailLL-diaminopimelic acid containing peptidoglycans in walls of Streptomyces sp. and of Clostridium perfringens (type A).
Leyh-Bouille, Mélina; Bonaly, Roger; Ghuysen, Jean-Marie ULg et al

in Biochemistry (1970), 9(15), 2944-2952

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 ... [more ▼]

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. [less ▲]

Detailed reference viewed: 6 (1 ULg)
Full Text
Peer Reviewed
See detailIsolation of DD carboxypeptidase from Streptomyces albus G culture filtrates
Ghuysen, Jean-Marie ULg; Leyh-Bouille, Mélina; Bonaly, Roger et al

in Biochemistry (1970), 9(15), 2955-2961

Streptomyces albus G secretes a soluble DD carboxypeptidase whose catalytic activities are similar to those of the particulate DD carboxypeptidase from Escherichia coli. Both enzymes hydrolyze the C ... [more ▼]

Streptomyces albus G secretes a soluble DD carboxypeptidase whose catalytic activities are similar to those of the particulate DD carboxypeptidase from Escherichia coli. Both enzymes hydrolyze the C-terminal D-alanyl-D-alanine linkage of UDP-N-acetylmuramyl-L-alanyl-γ-D-glutamyl-(L)-meso-diaminopimelyl-(L)-D-alanyl-D-aIanine and the enzyme-peptide interactions have identical Michaelis constants. Like the E. coli enzyme, the Streptomyces DD carboxypeptidase exhibits endopeptidase activities. The Streptomyces enzyme is lytic for those walls in which the peptidoglycan interpeptide bonds are mediated through C-terminal D-alanyl-D linkages. There is no strict requirement for a specific structure of the C-terminal D-amino acid residue. The tripeptide Nα , Nє -bisacetyl-L-lysyl-D-alanyl-D-alanine is an excellent substrate for the Streptomyces DD carboxypeptidase. [less ▲]

Detailed reference viewed: 20 (1 ULg)
Full Text
Peer Reviewed
See detailSubstrate requirements of the Streptomyces albus G DD carboxypeptidase
Leyh-Bouille, Mélina; Ghuysen, Jean-Marie ULg; Bonaly, Roger et al

in Biochemistry (1970), 9(15), 2961-2970

Detailed reference viewed: 9 (1 ULg)