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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 ▲]

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See detailOn the Streptomyces albus G DD carboxypeptidase mechanism of action of penicillin, vancomycin, and ristocetin
Leyh-Bouille, Mélina; Ghuysen, Jean-Marie ULg; Nieto, Manuel et al

in Biochemistry (1970), 9(15), 2971-2975

The activity of the D-alanyl-D carboxypeptidase from the penicillin-resistant Streptomyces albus G is not or very little affected by penicillins and related antibiotics. The molecular basis for the ... [more ▼]

The activity of the D-alanyl-D carboxypeptidase from the penicillin-resistant Streptomyces albus G is not or very little affected by penicillins and related antibiotics. The molecular basis for the mechanism of action of penicillin is discussed. The Streptomyces albus G D-alanyl-D carboxypeptidase appears as a model for the study of a mechanism of penicillin resistance that does not involve the enzymatic degradation of the antibiotic. Vancomycin and ristocetin are shown to inhibit the hydrolysis of sensitive peptides by the Streptomyces albus G D-alanyl-D carboxypeptidase and the mechanism of inhibition is discussed. [less ▲]

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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

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See detailThe peptidoglycan in walls of Butyribacterium rettgeri
Guinand, Micheline; Ghuysen, Jean-Marie ULg; Schleifer, Karl H. et al

in Biochemistry (1969), 8(1), 200-207

The wall peptidoglycan in Butyribacterium rettgeri is composed of Nα-(L-seryl-γ-D-glutamyl)-L-ornithyl-D-alanine subunits. The peptide subunits are cross-linked by means of a D-lysine or a D-ornithine ... [more ▼]

The wall peptidoglycan in Butyribacterium rettgeri is composed of Nα-(L-seryl-γ-D-glutamyl)-L-ornithyl-D-alanine subunits. The peptide subunits are cross-linked by means of a D-lysine or a D-ornithine residue, extending from the α-carboxyl group of the glutamic acid of one peptide subunit, to which D-lysine is linked through its є-amino group or D-ornithine through its δ-amino group, to the carboxyl group of the C-terminal D-alanine residue of another peptide subunit. D-Lysine and D-ornithine bridges occur in the ratio of 2:1. The Streptomyces KM endopeptidase hydrolyses the Nα-( D-alanyl)-D-lysine and Nα-(D-alanyl)-D-ornithine linkages and causes wall solubilization. The walls, as they are prepared, have a low degree of cross-linking. About 59% of the peptide subunits occur as monomers (18%), dimers (24%), and trimers (17%). Higher oligomers account for the remaining 41 %. The disaccharide units obtained after sequential treatment with Streptomyces F1 endo-N-acetylmuramidase and Streptomyces N-acetylmuramyl-L-alanine amidase are all β-1,4-N-acetylglucosaminyl-N-acetylmuramic acid. [less ▲]

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