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See detailStreptomyces K15 DD-peptidase-catalysed reactions with suicide β-lactam carbonyl donors
Leyh-Bouille, Mélina; Nguyen-Distèche, Martine ULg; Pirlot, Suzanne et al

in Biochemical Journal (1986), 235(1), 177-182

The values of the kinetic parameters that govern the interactions between the Streptomyces K15 DD-peptidase and beta-lactam compounds were determined by measuring the inactivating effect that these ... [more ▼]

The values of the kinetic parameters that govern the interactions between the Streptomyces K15 DD-peptidase and beta-lactam compounds were determined by measuring the inactivating effect that these compounds exert on the transpeptidase activity of the enzyme and, in the case of [14C]benzylpenicillin and [14C]cefoxitin, by measuring the amounts of acyl-enzyme formed during the reaction. K15 DD-peptidase binds benzylpenicillin or cefoxitin at a molar ratio of 1:1. Benzylpenicilloate is the major product released during breakdown of the acyl-enzyme formed with benzylpenicillin. Benzylpenicillin is not a better acylating agent than the amide Ac2-L-Lys-D-Ala-D-Ala and ester Ac2-L-Lys-D-Ala-D-lactatecarbonyl-donor substrates. beta-Lactam compounds possessing a methoxy group on the alpha-face of the molecule show high inactivating potency. [less ▲]

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See detailActive-site-serine D-alanyl-D-alanine-cleaving-peptidase-catalysed acyl-transfer reactions. Procedures for studying the penicillin-binding proteins of bacterial plasma membranes
Ghuysen, Jean-Marie ULg; Frère, Jean-Marie ULg; Leyh-Bouille, Mélina et al

in Biochemical Journal (1986), 235(1), 159-165

Under certain conditions, the values of the parameters that govern the interactions between the active-site-serine D-alanyl-D-alanine-cleaving peptidases and both carbonyl-donor substrates and beta-lactam ... [more ▼]

Under certain conditions, the values of the parameters that govern the interactions between the active-site-serine D-alanyl-D-alanine-cleaving peptidases and both carbonyl-donor substrates and beta-lactam suicide substrates can be determined on the basis of the amounts of (serine ester-linked) acyl-protein formed during the reactions. Expressing the 'affinity' of a beta-lactam compound for a DD-peptidase in terms of second-order rate constant of enzyme acylation and first-order rate constant of acyl-enzyme breakdown rests upon specific features of the interaction (at a given temperature) and permits study of structure-activity relationships, analysis of the mechanism of intrinsic resistance and use of a 'specificity index' to define the capacity of a beta-lactam compound of discriminating between various sensitive enzymes. From knowledge of the first-order rate constant of acyl-enzyme breakdown and the given time of incubation, the beta-lactam compound concentrations that are necessary to achieve given extents of DD-peptidase inactivation can be converted into the second-order rate constant of enzyme acylation. The principles thus developed can be applied to the study of the multiple penicillin-binding proteins that occur in the plasma membranes of bacteria. [less ▲]

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See detailStreptomyces K15 DD-peptidase-catalysed reactions with ester and amide carbonyl donors
Nguyen-Distèche, Martine ULg; Leyh-Bouille, Mélina; Pirlot, Suzanne et al

in Biochemical Journal (1986), 235(1), 167-176

In water, the purified 26 000-Mr membrane-bound DD-peptidase of Streptomyces K15 hydrolyses the ester carbonyl donor Ac2-L-Lys-D-Ala-D-lactate (release of D-lactate) and the amide carbonyl donor Ac2-L-Lys ... [more ▼]

In water, the purified 26 000-Mr membrane-bound DD-peptidase of Streptomyces K15 hydrolyses the ester carbonyl donor Ac2-L-Lys-D-Ala-D-lactate (release of D-lactate) and the amide carbonyl donor Ac2-L-Lys-D-Ala-D-Ala (release of D-alanine) with accumulation of acyl- (Ac2-L-Lys-D-alanyl-)enzyme. Whereas hydrolysis of the ester substrate proceeds to completion, hydrolysis of the amide substrate is negligible because of the capacity of the K15 DD-peptidase for utilizing the released D-alanine in a transfer reaction (Ac2-L-Lys-D-Ala-D-Ala + D-Ala----Ac2-L-Lys-D-Ala-D-Ala + D-Ala) that maintains the concentration of the amide substrate at a constant level. In the presence of an amino acceptor X-NH2 (Gly-Gly or Gly-L-Ala) related to the Streptomyces peptidoglycan, both amide and ester carbonyl donors are processed without detectable accumulation of acyl-enzyme. Under proper conditions, the acceptor activity of water and, in the case of the amide substrate, the acceptor activity of the released D-alanine can be totally overcome so that the two substrates are quantitatively converted into transpeptidated product Ac2-L-Lys-D-Ala-NH-X (and hydrolysis is prevented). Experimental evidence suggests that the amino acceptor modifies both the binding of the carbonyl donor to the enzyme and the ensuing rate of enzyme acylation. [less ▲]

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See detailβ-Lactam-induced Proteus L-forms
Ghuysen, Jean-Marie ULg; Nguyen-Distèche, Martine ULg; Rousset, André

in Madoff, Sarabelle (Ed.) The Bacterial L-Forms, vol. 17 (1986)

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See detailBacterial wall peptidoglycan, DD-peptidases and beta-lactam antibiotics
Ghuysen, Jean-Marie ULg; Frère, Jean-Marie ULg; Leyh-Bouille, Mélina et al

in Scandinavian Journal of Infectious Diseases (1984), 42

Wall peptidoglycan expansion in bacteria rests upon a cytoplasmic D-Ala: D-Ala ligase (ADP) which catalyses synthesis of a D-Ala-D-Ala dipeptide (with accompanying hydrolysis of one molecule of ATP) and a ... [more ▼]

Wall peptidoglycan expansion in bacteria rests upon a cytoplasmic D-Ala: D-Ala ligase (ADP) which catalyses synthesis of a D-Ala-D-Ala dipeptide (with accompanying hydrolysis of one molecule of ATP) and a set of DD-peptidases which utilize this D-Ala-D-Ala dipeptide--once it has been translocated at the outer face of the plasma membrane as the C-terminal portion of a disaccharide peptide unit--as carbonyl donor for transpeptidation and carboxypeptidation reactions (without additional energy expenditure). Four DD-peptidases have been selected which differ from each other with respect to the effects that amino compounds exert on the fate and rate of consumption of a D-Ala-D-Ala terminated amide carbonyl donor analogue. They serve as models to understand the different mechanisms by which the DD-peptidases perform catalysis and show widely varying responses to the action of beta-lactams, from extreme sensitivity to very high resistance. [less ▲]

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See detailInstrinct Resistance to beta-lactam antibiotics at the level of the enzyme sites. Many challenges, some achievements
Ghuysen, Jean-Marie ULg; Charlier, P.; Coyette, Jean et al

in Wiedemann, B.; Guysen, Jean-Marie; Spitzy, K. H. (Eds.) et al Symposium Mechanisms of resistance to beta-lactam antibiotics : Proceedings (1983)

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See detailPenicillin-binding proteins and carboxypeptidase/transpeptidase activities in Proteus vulgaris P18 and its penicillin-induced stable L-forms
Rousset, André; Nguyen-Distèche, Martine ULg; Minck, Raymond et al

in Journal of Bacteriology (1982), 152(3), 1042-1048

The originally penicillin-induced, wall-less stable L-forms of Proteus vulgaris P18, isolated by Tulasne in 1949 and since then cultured in he absence of penicillin, have kept the ability to synthesize ... [more ▼]

The originally penicillin-induced, wall-less stable L-forms of Proteus vulgaris P18, isolated by Tulasne in 1949 and since then cultured in he absence of penicillin, have kept the ability to synthesize the seven penicillin-binding proteins and the various DD- and LD-peptidase activities found in the parental bacteria and known to be involved in wall peptidoglycan metabolism. The stable L-forms, however, secrete during growth both the highly penicillin-sensitive, DD-carboxy-peptidase-transpeptidase penicillin-binding protein PBP4 (which in normal bacteria is relatively loosely bound to the plasma membrane) and the penicillin-insensitive LD-carboxypeptidase (which in normal bacteria is located in the periplasmic region). [less ▲]

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See detailIsolation of the membrane-bound 26 000-Mr penicillin-binding protein of Streptomyces strain K15 in the form of a penicillin-sensitive D-alanyl-D-alanine-cleaving transpeptidase
Nguyen-Distèche, Martine ULg; Leyh-Bouille, Mélina; Ghuysen, Jean-Marie ULg

in Biochemical Journal (1982), 207(1), 109-115

The membrane-bound, 26 000-Mr penicillin-binding protein of Streptomyces K15 has been isolated in the form of an effective, penicillin-sensitive D-alanyl-D-alanine-cleaving peptidase exhibiting high ... [more ▼]

The membrane-bound, 26 000-Mr penicillin-binding protein of Streptomyces K15 has been isolated in the form of an effective, penicillin-sensitive D-alanyl-D-alanine-cleaving peptidase exhibiting high transpeptidase activity (greater than 95%) and very low carboxy-peptidase activity (less than 5%). The penicillin-binding protein/transpeptidase can be extracted directly from the mycelium with N-cetyl-NNN-trimethylammonium bromide (Cetavlon) and subsequently obtained at 90% purity and with an 8000-fold specific enrichment (when compared with the activity of the isolated membranes) by a two-step procedure involving Sephadex filtration and affinity chromatography on ampicillin-linked CH Sepharose 4B in the presence of detergent. At saturating concentrations of the co-substrates diacetyl-L-Lys-D-Ala-D-Ala and Gly-Gly, the catalytic-centre activity is about 0.3 s-1. [less ▲]

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See detailOn the DD-carboxypeptidase enzyme system of Streptomyces strain K15
Leyh-Bouille, Mélina; Nguyen-Distèche, Martine ULg; Ghuysen, Jean-Marie ULg

in European Journal of Biochemistry (1981), 115(3), 579-584

Streptomyces K15 possesses a set of exocellular and cell-bound D-alanyl-D-alanine carboxypeptidases. Four of them have been isolated to the stage where each enzyme preparation contains on single ... [more ▼]

Streptomyces K15 possesses a set of exocellular and cell-bound D-alanyl-D-alanine carboxypeptidases. Four of them have been isolated to the stage where each enzyme preparation contains on single penicillin-binding protein. The exocellular 54000-Mr enzyme is extremely sensitive to benzylpenicillin and performs low transpeptidase activity on the carbonyl-donor/amino-acceptor tetrapeptide ACLLys(Gly)-DAla-DAla. The exocellular 40 000-Mr enzyme and the two lysozyme-releasable 40 000-Mr and 38 000-Mr enzymes are moderately sensitive to benzylpenicillin and have a high propensity to catalyse dimer formation from the aforementioned tetrapeptide monomer. [less ▲]

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See detailPenicillin-binding proteins in the membranes of Streptomyces sp
Dusart, Jean; Leyh-Bouille, Mélina; Nguyen-Distèche, Martine ULg et al

in Archives Internationales de Physiologie et de Biochimie (1980, February 01), 88(1), 27-29

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See detailOn the Active Centers of Serine and Zn II DD-carboxyppetidases
Charlier, Paulette ULg; Coyette, Jacques ULg; Dideberg, Otto et al

in Gregory, G.I. (Ed.) Recent advances in the Chemistry of beta-lactam antibiotics (1980)

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See detailUse of model enzymes in the determination of the mode of action of penicillins and delta 3-cephalosporins
Ghuysen, Jean-Marie ULg; Frère, Jean-Marie ULg; Leyh-Bouille, Mélina et al

in Annual Review of Biochemistry (1979), 48

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See detailThe peptidoglycan crosslinking enzyme system in Streptomyces R61, K15 and rimosus. Immunological studies
Nguyen-Distèche, Martine ULg; Frère, Jean-Marie ULg; Dusart, Jean et al

in European Journal of Biochemistry (1977), 81(1), 29-32

The exocellular DD-carboxypeptidases from Streptomyces R61, K 15, the lysozyme-releasable DD-carboxypeptidases from Streptomyces R61, K15 and rimosus, and the membrane-bound DD-carboxypeptidase of ... [more ▼]

The exocellular DD-carboxypeptidases from Streptomyces R61, K 15, the lysozyme-releasable DD-carboxypeptidases from Streptomyces R61, K15 and rimosus, and the membrane-bound DD-carboxypeptidase of Streptomyces K15 are immunologically related to each other. [less ▲]

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See detailThe DD-carboxypeptidase-transpeptidase system in Escherichia coli mutant strain
Pollock, J. J.; Nguyen-Distèche, Martine ULg; Ghuysen, Jean-Marie ULg et al

in Annals of the New York Academy of Sciences (1974), 235

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See detailEnzymes involved in wall peptide crosslinking in Escherichia coli K12, strain 44
Nguyen-Distèche, Martine ULg; Ghuysen, Jean-Marie ULg; Pollock, Jerry J. et al

in European Journal of Biochemistry (1974), 41(3), 447-455

By using the glutamate-amidated tetrapeptide l-alanyl-d-isoglutaminyl-(l)-meso-diamino-pimelyl-(l)-d-alanine as a probe, there appears to exist in the membranes of Escherichia coli K12 strain 44 a dd ... [more ▼]

By using the glutamate-amidated tetrapeptide l-alanyl-d-isoglutaminyl-(l)-meso-diamino-pimelyl-(l)-d-alanine as a probe, there appears to exist in the membranes of Escherichia coli K12 strain 44 a dd-carboxypoptidase-transpeptidase system which does not recognize this peptide and a dd-carboxypoptidase-transpeptidase system which recognizes it. The dd-carboxypeptidase-endopeptidase system is essentially hydrolytic. It catalyzes the hydrolysis of UDP-N-acetyl-muramyl-pentapeptide into UDP-N-acetylmuramyl-tetrapeptide and the hydrolysis of the wall peptidoglycan peptide dimer into monomers. These activities are not inhibited by the glutamate-amidated tetrapeptide. The system may consist either of two enzyme proteins having predominantly carboxypeptidase activity and endopeptidase activity, respectively, or of one enzyme protein of which the functioning would depend upon the environmental conditions. The dd-carboxypeptidase-transpeptidase system (a) catalyzes concomitant hydrolysis (carboxypeptidase activity) and transfer (natural model transpeptidase activity) reactions with the pentapeptide l-alanyl-γ-d-glutamyl-(l)-meso-diaminopimelyl-(l)-d-alanyl-d-alanine. The transfer reaction leads to the synthesis of a dimer that is identical to the one which occurs in the E. coli wall peptidoglycan; (b) utilizes the glutamate-amidated tetrapeptide as an acceptor. Simultaneous exposure of the pentapeptide and the glutamate-amidated tetrapeptide to the enzyme system leads to the formation of an hybrid monoamidated peptide dimer and causes a decreased hydrolysis of the pentapeptide; (c) by virtue of its own carboxypeptidase activity, it appears to exert some endopeptidase activity. Both carboxypeptidase and endopeptidase activities of this system are inhibited by the glutamate-amidated tetrapeptide, but this represents only a small fraction of the total hydrolytic activity of the membrane Brij-36T extract. (d) The system catalyzes an unnatural model transpeptidation reaction in which glycine replaces d-alanine at the C-terminal position of the nucleotide UDP-N-acetylmuramyl-pentapeptide. This system may also consist either of two enzyme proteins having predominantly natural model transpeptidase activity and unnatural model transpeptidase activity, respectively, or of one enzyme protein of which the functioning would depend upon the environmental conditions. Whatever the exact situation, the E. colidd-carboxypeptidase-transpeptidase system is in many respects, similar to the dd-carboxy-peptidase-transpeptidase single polypeptide enzymes isolated from Streptomyces strains R39 and R61. [less ▲]

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See detailSensitivity to ampicillin and cephalothin of enzymes involved in wall peptide crosslinking in Escherichia coli K12, strain 44
Nguyen-Distèche, Martine ULg; Pollock, Jerry J.; Ghuysen, Jean-Marie ULg et al

in European Journal of Biochemistry (1974), 41(3), 457-463

After extraction of the membranes of Escherichia coli K12 strain 44 by Brij-36T, each of the four enzyme activities (natural transpeptidase, unnatural transpeptidase, carboxypeptidase and endopeptidase ... [more ▼]

After extraction of the membranes of Escherichia coli K12 strain 44 by Brij-36T, each of the four enzyme activities (natural transpeptidase, unnatural transpeptidase, carboxypeptidase and endopeptidase) of the wall peptide crosslinking system, occurs in two forms characterized by large differences in their sensitivity to ampicillin (but much smaller differences in their sensitivity to cephalothin). The fractionation of the enzyme activities into two groups of low and high sensitivity to ampicillin is achieved essentially by chromatography of the membrane extract on DEAE-cellulose. [less ▲]

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See detailComment la Pénicilline tue les bactéries
Ghuysen, Jean-Marie ULg; Leyh-Bouille, Mélina; Frère, Jean-Marie ULg et al

in Annales de Microbiologie (1974), 125 B(2), 209-210

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