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See detailTranspeptidase activity of Streptomyces D-alanyl-D carboxypeptidases
Pollock, J. J.; Ghuysen, Jean-Marie ULg; Linder, R. et al

in Proceedings of the National Academy of Sciences of the United States of America (1972), 69(3), 662-666

In the presence of N(alpha),N(epsilon)-diacetyl-L-Lys-D-Ala-D-Ala as donor, and either D-[(14)C]alanine, [(14)C]-glycine, or meso-[(3)H]diaminopimelic acid as acceptor, the DD carboxypeptidases from ... [more ▼]

In the presence of N(alpha),N(epsilon)-diacetyl-L-Lys-D-Ala-D-Ala as donor, and either D-[(14)C]alanine, [(14)C]-glycine, or meso-[(3)H]diaminopimelic acid as acceptor, the DD carboxypeptidases from Streptomyces R61 and R39 catalyze a transpeptidation reaction with the release of terminal D-alanine from the donor and the formation of either N(alpha),N(epsilon)-diacetyl-L-Lys-D-Ala-D-[(14)C]Ala, N(alpha),N(epsilon)-diacetyl-L-Lys-D-Ala-[(14)C] Gly, or N(alpha),N(epsilon)-diacetyl-L-Lys-D-Ala-D-meso- [(3)H]diaminopimelic acid. The reaction appears to be a true transpeptidation, and is not simply a "reversal of hydrolysis". Transpeptidation is inhibited by pencillin at concentrations that inhibit hydrolysis (carboxypeptidase action) of the donor peptide. There are differences in the specificity profiles of the Streptomyces enzymes for acceptor molecules:only the R61 enzyme used [(14)C]Gly-Gly as acceptor; transfer of N(alpha),N(epsilon)-diacetyl-L-Lys-D-Ala to this acceptor resulted in the formation of N(alpha),N(epsilon)-diacetyl-Lys-D-Ala-[(14)C] Gly-Gly, with the synthesis of a (D-Ala-Gly) peptide bond in an endoposition. [less ▲]

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See detailThe primary structure of bacterial wall peptidoglycans
Ghuysen, Jean-Marie ULg; Leyh-Bouille, Mélina; Salton, M. R. J.

in Journal of General Microbiology (1969, August 01), 57(3), -

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See detailAcetylhexosamine 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 ULg

in Biochimica et Biophysica Acta (1960), 45

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 ... [more ▼]

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. [less ▲]

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See detailAcetylhexosamine compounds enzymically released from Micrococcus lysodeikticus cell walls: I. Isolation and composition of acetylhexosamine and acetylhexosamine-peptide complexes
Ghuysen, Jean-Marie ULg; Salton, M. R. J.

in Biochimica et Biophysica Acta (1960), 40

Some of the dialyzable products of the digestion of Micrococcus lysodeikticus cell walls by lysozyme and by a similar enzyme secreted by a Streptomyces have been isolated and their compositions determined ... [more ▼]

Some of the dialyzable products of the digestion of Micrococcus lysodeikticus cell walls by lysozyme and by a similar enzyme secreted by a Streptomyces have been isolated and their compositions determined. The two simplest substances released by both enzymes are (a) a di-saccharide of N-acetylmuramic acid-N-acetylglucosamine and (b) an N-acetylmuramic acid-N-acetylglucosamine complex. Seven peptide-acetyl-amino sugar complexes have been isolated. All seven compounds contain lysine, glutamic acid, glycine, alanine in the same molecular proportions as found in the original cell wall and a di-saccharide moiety of N-acetylmuramic acid and N-acetylglucosamine. One of the peptide-amino sugar complexes contains in addition a polysaccharide moiety [N-acetylmuramic acid-N-acetylglucosamine]10. [less ▲]

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See detailAction de l'actinomycetine sur les parois cellulaires bacteriennes
Salton, M. R. J.; Ghuysen, Jean-Marie ULg

in Biochimica et Biophysica Acta (1957), 24(1), 160-173

The cell walls of a number of gram-positive bacteria can be digested by two different enzymes, present in actinomycetin, which have been obtained in a purified form. In contrast to lysozyme and the ... [more ▼]

The cell walls of a number of gram-positive bacteria can be digested by two different enzymes, present in actinomycetin, which have been obtained in a purified form. In contrast to lysozyme and the streptolytic enzyme of McCarty, these two enzymes are peptidases, their lytic action on the cell walls being accompanied by the liberation of alanine and/or glycine and small dialysable peptides. The ionic strength of the medium plays an essential role in the lysis. This role has been described and it probably depends on the electric charge of the cell walls. The products of the digestion of cell walls of staphylococci have been specially studied: at least some of the liberated alanine has the D-form; the non-dialysable fractions have been examined by electrophoresis and by ultra-centrifugation. [less ▲]

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