References of "Nguyen-Distèche, Martine"
     in
Bookmark and Share    
Full Text
Peer Reviewed
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 ▲]

Detailed reference viewed: 5 (0 ULg)
Full Text
Peer Reviewed
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

Detailed reference viewed: 8 (0 ULg)
Full Text
Peer Reviewed
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 ▲]

Detailed reference viewed: 18 (2 ULg)
Full Text
Peer Reviewed
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

Detailed reference viewed: 9 (0 ULg)
Full Text
Peer Reviewed
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 ▲]

Detailed reference viewed: 4 (2 ULg)
Full Text
Peer Reviewed
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 ▲]

Detailed reference viewed: 8 (1 ULg)