References of "Coyette, Jacques"
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See detailPenicillin and Beyond: Evolution, Protein Fold, Multimodular Polypeptides, and Multiprotein Complexes
Ghuysen, Jean-Marie ULg; Charlier, Paulette ULg; Coyette, Jacques et al

in Microbial Drug Resistance : Mechanism, Epidemiology, & Disease (1996), 2(2, Summer), 163-175

As the protein sequence and structure databases expand, the relationships between proteins, the notion of protein superfamily, and the driving forces of evolution are better understood. Key steps of the ... [more ▼]

As the protein sequence and structure databases expand, the relationships between proteins, the notion of protein superfamily, and the driving forces of evolution are better understood. Key steps of the synthesis of the bacterial cell wall peptidoglycan are revisited in light of these advances. The reactions through which the D-alanyl-D-alanine depeptide is formed, utilized, and hydrolyzed and the sites of action of the glycopeptide and beta-lactam antibiotics illustrate the concept according to which new enzyme functions evolve as a result of tinkering of existing proteins. This occurs by the acquisition of local structural changes, the fusion into multimodular polypeptides, and the association into multiprotein complexes. [less ▲]

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See detailSerine-Type D-Ala-D-Ala Peptidases and Penicillin-Binding Proteins
Granier, Benoît; Jamin, Marc; Adam, Maggy et al

in Methods in Enzymology (1994), 244

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See detailCloning and Sequencing of the Low-Affinity Penicillin-Binding Protein 3r-Encoding Gene of Enterococcus Hirae S185: Modular Design and Structural Organization of the Protein
Piras, Graziella; Raze, Dominique; el Kharroubi, Aboubaker et al

in Journal of Bacteriology (1993), 175(10), 2844-2852

The clinical isolate Enterococcus hirae S185 has a peculiar mode of resistance to penicillin in that it possesses two low-affinity penicillin-binding proteins (PBPs): the 71-kDa PBP5, also found in other ... [more ▼]

The clinical isolate Enterococcus hirae S185 has a peculiar mode of resistance to penicillin in that it possesses two low-affinity penicillin-binding proteins (PBPs): the 71-kDa PBP5, also found in other enterococci, and the 77-kDa PBP3r. The two PBPs have the same low affinity for the drug and are immunochemically related to each other. The PBP3r-encoding gene has been cloned and sequenced, and the derived amino acid sequence has been compared by computer-assisted hydrophobic cluster analysis with that of the low-affinity PBP5 of E. hirae R40, the low-affinity PBP2' of Staphylococcus aureus, and the PBP2 of Escherichia coli used as the standard of reference of the high-M(r) PBPs of class B. On the basis of the shapes, sizes, and distributions of the hydrophobic and nonhydrophobic clusters along the sequences and the linear amino acid alignments derived from this analysis, the dyad PBP3r-PBP5 has an identity index of 78.5%, the triad PBP3r-PBP5-PBP2' has an identity index of 29%, and the tetrad PBP3r-PBP5-PBP2'-PBP2 (of E. coli) has an identity index of 13%. In spite of this divergence, the low-affinity PBPs are of identical modular design and possess the nine amino acid groupings (boxes) typical of the N-terminal and C-terminal domains of the high-M(r) PBPs of class B. At variance with the latter PBPs, however, the low-affinity PBPs have an additional approximately 110-amino-acid polypeptide stretch that is inserted between the amino end of the N-terminal domain and the carboxy end of the membrane anchor. While the enterococcal PBP5 gene is chromosome borne, the PBP3r gene appears to be physically linked to the erm gene, which confers resistance to erythromycin and is known to be plasmid borne in almost all the Streptococcus spp. examined. [less ▲]

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See detailSynthèse, étude théorique et évaluation biologique de dérivés du 4-amino-4H-1,2,4-triazole analogues des antibiotiques b-lactamiques
Pirotte, Bernard ULg; Dive, Georges ULg; Delarge, Jacques et al

in European Journal of Medicinal Chemistry (1992), 27(3), 193-205

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See detailThe Enterococcus Hirae R40 Penicillin-Binding Protein 5 and the Methicillin-Resistant Staphylococcus Aureus Penicillin-Binding Protein 2' Are Similar
el Kharroubi, Aboubaker; Jacques, Philippe; Piras, Graziella et al

in Biochemical Journal (1991), 280(Pt 2), 463-469

The penicillin-resistant Enterococcus hirae R40 has a typical profile of membrane-bound penicillin-binding proteins (PBPs) except that the 71 kDa PBP5 of low penicillin affinity represents about 50% of ... [more ▼]

The penicillin-resistant Enterococcus hirae R40 has a typical profile of membrane-bound penicillin-binding proteins (PBPs) except that the 71 kDa PBP5 of low penicillin affinity represents about 50% of all the PBPs present. Water-soluble tryptic-digest peptides were selectively produced from PBP5, their N-terminal regions were sequenced and synthetic oligonucleotides were used as primers to generate a 476 bp DNA fragment by polymerase chain reaction. On the basis of these data, the PBP5-encoding gene was cloned in Escherichia coli by using pBR322 as vector. The gene, included in a 7.1 kb insert, had the information for a 678-amino acid-residue protein. PBP5 shows similarity, in the primary structure, with the high-molecular-mass PBPs of class B. In particular, amino acid alignment of the enterococcal PBP5 and the methicillin-resistant staphylococcal PBP2' generates scores that are 30, for the N-terminal domains, and 53, for the C-terminal domains, standard deviations above that expected for a run of 20 randomized pairs of proteins having the same amino acid compositions as the two proteins under consideration. [less ▲]

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See detailMode of Membrane Insertion and Sequence of a 32-Amino Acid Peptide Stretch of the Penicillin-Binding Protein 4 of Enterococcus Hirae
Jacques, Philippe; el Kharroubi, Aboubaker; Van Beeumen, Jozef et al

in FEMS Microbiology Letters (1991), 66(2), 119-123

Analysis of water-soluble derivatives of the Enterococcus hirae 75-kDa membrane-bound penicillin-binding protein 4 (PBP4) has yielded the amino acid sequence of a 32-amino acid polypeptide stretch. This ... [more ▼]

Analysis of water-soluble derivatives of the Enterococcus hirae 75-kDa membrane-bound penicillin-binding protein 4 (PBP4) has yielded the amino acid sequence of a 32-amino acid polypeptide stretch. This peptide is similar to peptide segments known to occur in the N-terminal domain of high-Mr PBPs of class B. The E. hirae PBP4 probably belongs to the same class. It is anchored in the membrane at the N-terminus of the polypeptide chain. [less ▲]

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See detailActive-Site and Membrane Topology of the Dd-Peptidase/Penicillin-Binding Protein No. 6 of Enterococcus Hirae (Streptococcus Faecium) A.T.C.C. 9790
El Kharroubi, Aboubaker; Piras, Graziella; Jacques, Philippe et al

in Biochemical Journal (1989), 262(2), 457-462

The membrane-bound 43,000-Mr penicillin-binding protein no. 6 (PBP6) of Enterococcus hirae consists of a 30,000-Mr DD-peptidase/penicillin-binding domain and a approximately 130-residue C-terminal ... [more ▼]

The membrane-bound 43,000-Mr penicillin-binding protein no. 6 (PBP6) of Enterococcus hirae consists of a 30,000-Mr DD-peptidase/penicillin-binding domain and a approximately 130-residue C-terminal appendage. Removal of this appendage by trypsin proteolysis has no marked effect on the catalytic activity and penicillin-binding capacity of the PBP. Anchorage of the PBP in the membrane appears to be mediated by a short 15-20-residue stretch at the C-terminal end of the appendage. The sequence of the 50-residue N-terminal region of the PBP shows high degree of homology with the sequences of the corresponding regions of the PBPs5 of Escherichia coli and Bacillus subtilis. On this basis the active-site serine residue occurs at position 35 in the enterococcal PBP. [less ▲]

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See detailFunction of Penicillin-binding protein 3 in Streptococcus Faecium
Coyette, Jacques; Somzé, Anne; Briquet, Jean-Jacques et al

in Hakenbeck, Regine; Höltje, Joachim-Volker; Labischinski, Harald (Eds.) The Target Penicillin : the Murein Sacculus of Bacterial Cell Walls Architecture and Growth : Proceedings (1983)

Cefotaxime at concns. around the min. inhibitory concn. (MIC, 5 μM) or below (0.1-1.0 μM) causes transformation of the normal S. faecium cells to bacilliform cells whose length increases with increasing ... [more ▼]

Cefotaxime at concns. around the min. inhibitory concn. (MIC, 5 μM) or below (0.1-1.0 μM) causes transformation of the normal S. faecium cells to bacilliform cells whose length increases with increasing duration of treatment. Septa are initiated but never reach completion. Affinity detn. for cefotaxime binding showed that the antibiotic binds preferentially to the 3 highest mol. wt. penicillin-binding proteins (PBP); PBP-2 and PBP-3 are about 100-fold more sensitive to cefotaxime than PBP-1. It appears, therefore, that PbP-2 and PBP-3 are involved in cell septation. This was confirmed by using cefatoxime in subinhibitory concns. (1 μM). From cell samples collected 30 and 60 min after addn. of cefotaxime, membranes were isolated, labeled with satg. [3H]benzylpenicillin and examd. by fluorog. Under these conditions only PBP-2 and PBP-3 were satd. by cefotaxime. At this stage no distinction could be made between the 2 proteins; either both or 1 of them may be involved in cell division. Cefoxitin produced morphol. alteration of a different nature than cefotaxime. The cefoxitin-treated cells had increased diam. and were slightly elongated. The most striking alteration was the frequent presence of conical poles contrasting with round poles obsd. in control cells. The morphol. alteration obsd. in cefoxitin-treated cells could be attributed to the inhibition of the function of PBP-1, PBP-2, or PBP-3. Elongated cells similar to those obtained with cefotaxime were not found with cefoxitin at concns. sufficient to sat. PBP-2. The main difference between cefotaxime- and cefoxitin-treated cells is that PBP-3 is satd. by cefotaxime but not altered at all by cefoxitin. Thus, septation inhibition must be due to the interaction of cefotaxime with PBP-3 [less ▲]

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See detailNifurzide, a nitrofuran antiinfectious agent: interaction with Escherichia coli cells.
Delsarte, Anne; Faway, Michel; Frère, Jean-Marie et al

in Antimicrobial Agents and Chemotherapy (1981), 19(3), 477-86

This paper presents a study of the interactions between Escherichia coli cells and nifurzide, a nitrofuran derivative which is used as an intestinal antiinfectious agent. At low concentrations of ... [more ▼]

This paper presents a study of the interactions between Escherichia coli cells and nifurzide, a nitrofuran derivative which is used as an intestinal antiinfectious agent. At low concentrations of nifurzide, the growth rate of the cultures decreased, and elongated, nonseptate cells appeared. At high concentrations, complete growth inhibition occurred, accompanied by a rather strong bactericidal effect, but the appearance of the cells was normal; in particular, no bacteriolytic effect was observed. A very large number of antibiotic molecules were bound per bacterial cell. After cell disruption, similar amounts of nifurzide were found in the cytoplasm, cytoplasmic membranes, and cell wall, respectively. Most of the bound nifurzide was rapidly degraded or became protein bound. The structure of the outer membrane lipopolysaccharide appeared to have little influence on the activity of nifurzide. [less ▲]

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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 detailSolubilization and isolation of the membrane-bound DD-carboxypeptidase of Streptococcus faecalis ATCC9790. Properties of the purified enzyme
Coyette, Jacques; Ghuysen, Jean-Marie ULg; Fontana, Roberta

in European Journal of Biochemistry (1978), 88(1), 297-305

Streptococcus faecalis ATCC 9790 possesses six membrane-bound, penicillin-binding proteins. That numbered 6 (Mr 43000) is the most abundant one and is the DD-carboxypeptidase studied previously. The ... [more ▼]

Streptococcus faecalis ATCC 9790 possesses six membrane-bound, penicillin-binding proteins. That numbered 6 (Mr 43000) is the most abundant one and is the DD-carboxypeptidase studied previously. The enzyme has been solubilized and purified to the stage where one single protein band can be detected by gel electrophoresis. The purification procedure does not alter the properties that the enzyme exhibits when it is membrane-bound. The DD-carboxypeptidase itself may be a killing target for penicillin in S. faecalis. [less ▲]

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See detailThe exchange reaction of peptides R-D-alanyl-D-alanine with D-[14C]alanine to R-D-alanyl-D-[14C]alanine and D-alanine, catalysed by the membranes of Streptococcus faecalis ATCC 9790
Coyette, Jacques; Ghuysen, Jean-Marie ULg; Perkins, Harold R.

in European Journal of Biochemistry (1977), 75(1), 225-229

Under alkaline conditions, the membrane-bound DD-carboxypeptidase of Streptococcus faecalis ATCC 9790 catalyses exchange reactions in which the X-L-R3-D-Ala moiety of peptides of the type X-L-R3-D-Ala-D ... [more ▼]

Under alkaline conditions, the membrane-bound DD-carboxypeptidase of Streptococcus faecalis ATCC 9790 catalyses exchange reactions in which the X-L-R3-D-Ala moiety of peptides of the type X-L-R3-D-Ala-D-Ala is transferred to simple amino compounds such as D-alanine, glycine and glycyl-glycine. The enzyme system is unable, however, to catalyse complex reactions that would simulate the natural transpeptidation reaction. [less ▲]

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See detailInteractions between beta-lactam antibiotics and isolated membranes of Streptococcus faecalis ATCC 9790
Coyette, Jacques; Ghuysen, Jean-Marie ULg; Binot, Françoise ULg et al

in European Journal of Biochemistry (1977), 75(1), 231-239

The DD-carboxypeptidase-exchange membrane-bound enzyme in Streptococcus faecalis ATCC 9790 reacts with beta-lactam antibiotics to form complexes with rather long half-lives. Depending upon the antibiotic ... [more ▼]

The DD-carboxypeptidase-exchange membrane-bound enzyme in Streptococcus faecalis ATCC 9790 reacts with beta-lactam antibiotics to form complexes with rather long half-lives. Depending upon the antibiotic, the second-order rate constants for complex formation range from 0.75-560 M-1 S-1 (at 37 degrees C and in water) and the first-order rate constants for complex breakdown range from 1.3 to 26 x 10(-5) s-1 (at 37 degrees C and in 5 mM phosphate buffer pH 7.5). There are about 30 pmol of DD-carboxypeptidase-exchange enzyme per mg of membrane protein. The degradation products arising from benzylpenicillin are phenylacetylglycine and probably N-formyl-D-penicillamine. Isolated membranes also contain other penicillin binding sites (about 70 pmol/mg membrane protein). That part of benzylpenicillin which reacts with at least some of these latter sites is slowly degraded into penicilloic acid. Normal functioning of the DD-carboxypeptidase-exchange membrane-bound enzyme is important, if not essential, for cell growth. With the beta-lactam antibiotics tested inhibition of cell growth is mainly related to the rates of formation of the inactive enzyme-antibiotic complexes. The relationship, however, is not a direct one probably due to the competitive effect exerted by the other penicillin binding sites. [less ▲]

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See detailMembrane-bound DD-carboxypeptidase and LD-transpeptidase of Streptococcus faecalis ATCC 9790
Coyette, Jacques; Perkins, Harnold R.; Polacheck, Itzhack et al

in European Journal of Biochemistry (1974), 44(2), 459-468

Isolated membranes of Streptococcus faecalis ATCC 9790 exhibit DD-carboxypeptidase activity (standard reaction: Ac2-l-Lys-d-Ala-d-Ala →d-alanine + Ac2-l-Lys-d-Ala) and ld-trans-peptidase activity ... [more ▼]

Isolated membranes of Streptococcus faecalis ATCC 9790 exhibit DD-carboxypeptidase activity (standard reaction: Ac2-l-Lys-d-Ala-d-Ala →d-alanine + Ac2-l-Lys-d-Ala) and ld-trans-peptidase activity (standard reaction: Ac2-l-Lys-d-Ala + acceptor →d-alanine + Ac2-l-Lys-acceptor). The DD-carboxypeptidase activity has a considerable specificity for peptides with a C-terminal l-R3-d-Ala-d-Ala sequence where R3 is an amino acid residue and a long side-chain at the l-R3 position. A corresponding DD-transpeptidation reaction yielding the product Ac2-l-Lys-d-Ala-d-[14C]Ala from the system Ac2-l-Lys-d-Ala-d-Ala-f-d-[14C] alanine was not detected. The ld-transpeptidase activity has a considerable specificity for peptide donors that have an Nα-substituted, C-terminal l-R3-d-Ala sequence with a free ω-amino group at the end of a long side-chain at the l-R3 position, and a considerable specificity for amino group acceptors that are located on a d-carbon in α-position to a free carboxyl group. In the absence of acceptor, hydrolysis of the dipeptide Ac2-l-Lys-d-Ala (ld-carboxypeptidase activity) was not observed. Both DD-carboxypeptidase and ld-transpeptidase activities are inhibited by β-lactam antibiotics, but their relative sensitivity differs according to the particular antibiotic used. [less ▲]

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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 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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See detailPenicillin-sensitive DD-carboxypeptidase from Streptomyces strain R 61
Leyh-Bouille, Mélina; Coyette, Jacques; Ghuysen, Jean-Marie ULg et al

in Biochemistry (1971), 10(11), 2163-2170

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See detailStructure of the walls of Lactobacillus acidophilus strain 63 AM Gasser
Coyette, Jacques; Ghuysen, Jean-Marie ULg

in Biochemistry (1970), 9(15), 2935-2943

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