References of "Joris, Bernard"
     in
Bookmark and Share    
Peer Reviewed
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 ▲]

Detailed reference viewed: 59 (14 ULg)
Full Text
Peer Reviewed
See detailThe complete amino acid sequence of the Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase of streptomyces albus G
Joris, Bernard ULg; Van Beeumen, Jozef; Casagrande, Fabiana et al

in European Journal of Biochemistry (1983), 130(1), 53-69

The 22076-Mr Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase of Streptomyces abuls G effectively catalyses the transfer of the N alpha, N epsilon-diacetyl-L-lysyl-D-alanyl electrophilic group ... [more ▼]

The 22076-Mr Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase of Streptomyces abuls G effectively catalyses the transfer of the N alpha, N epsilon-diacetyl-L-lysyl-D-alanyl electrophilic group of the standard tripeptide substrate N alpha, N epsilon-diacetyl-L-lysyl-D-alanyl-D-alanine to water. It also performs a weak beta-lactamase activity, hydrolysing penicillin into penicilloate at a very low rate. This protein consists of 212 amino acid residues in a single polypeptide chain. The N terminus is partially blocked as a result of the cyclization of the dipeptide Asn-Gly into anhydroaspartylglycine imide. The protein has been fragmented by cyanogen bromide into five fragments whose sequences have been determined via appropriate subcleavages with various proteases. The ordering of the cyanogen bromide peptide fragments has been carried out (a) by submitting the S-carboxymethylated protein to complete tryptic digestion and labelling the methionine-containing peptides thus obtained with iodo[14C]-acetamide, and (b) by submitting to limited tryptic digestion the S-[2-(4'-pyridyl)ethyl]-cysteine protein whose amino groups have been blocked by reaction with exo-cis-3,6-endoxo-delta 4-tetrahydrophthalic anhydride prior to digestion. The protein contains six cysteine residues in the form of three disulfide bridges. No homology is found by comparing this peptidase with other Zn2+-containing enzymes (carboxypeptidase A, thermolysin, carbonic anhydrase B and alcohol dehydrogenase) and several completely or partially sequenced, serine-containing D-alanyl-D-alanine-cleaving peptidases and Zn2+/serine-containing beta-lactamases. [less ▲]

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

Detailed reference viewed: 7 (0 ULg)
Full Text
Peer Reviewed
See detailStructure of a Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase at 2.5 A resolution.
Dideberg, O.; Charlier, Paulette ULg; Dive, Georges ULg et al

in Nature (1982), 299(5882), 469-470

Bacteria possess proteases that are specific for the peptide bonds between D-alanine residues, one of which has a free alpha-carboxyl group. These D-alanyl-D-alanine peptidases catalyse carboxypeptidation ... [more ▼]

Bacteria possess proteases that are specific for the peptide bonds between D-alanine residues, one of which has a free alpha-carboxyl group. These D-alanyl-D-alanine peptidases catalyse carboxypeptidation and transpeptidation reactions involved in bacterial cell wall metabolism1,2, and are inactivated by beta-lactam antibiotics. We have now elucidated the structure, at 2.5 Å resolution, of the penicillin-resistant Zn2+-containing D-alanyl-D-alanine peptidase of Streptomyces albus (Zn2+ G peptidase)3,4. The enzyme is shown to consist of two globular domains, connected by a single link. The N-terminal domain has three alpha-helices, and the C-terminal domain has three alpha-helices and five beta-strands. The Zn2+ ion is ligated by three histidine residues, and located in a cleft in the C-terminal domain. The mechanism of action of the enzyme may be related to that of other carboxypeptidases, which also contain functional Zn2+ ions. [less ▲]

Detailed reference viewed: 36 (12 ULg)
Full Text
Peer Reviewed
See detailThe penicillin-binding site in the exocellular DD-carboxypeptidase-transpeptidase of Actinomadura R39
Duez, Colette ULg; Joris, Bernard ULg; Frère, Jean-Marie ULg et al

in Biochemical Journal (1981), 193

Heat denaturation and Pronase degradation of the complex previously formed between benzylpenicillin and the exocellular DD-carboxypeptidase-transpeptidase of Actinomadura R39 yields a heptapeptide H-Leu ... [more ▼]

Heat denaturation and Pronase degradation of the complex previously formed between benzylpenicillin and the exocellular DD-carboxypeptidase-transpeptidase of Actinomadura R39 yields a heptapeptide H-Leu-Pro-Ala-Ser-Asn-Gly-Val-OH, where the benzylpenicilloyl group is ester-linked to the serine residue. This linkage is very labile and its hydrolysis causes the release of benzylpenicilloate. In contrast, the native benzylpenicilloyl-enzyme complex is very stable (half-life 70h at 370C) and its breakdown proceeds via fragmentation of the bound benzylpenicilloyl group [Fuad, Frere, Ghuysen, Duez & Iwatsubo (1976) Biochem. J. 155, 623-6291. [less ▲]

Detailed reference viewed: 8 (3 ULg)
Full Text
Peer Reviewed
See detailThe exocellular DD-carboxypeptidase of Streptomyces albus G: A metallo (Zn2+) enzyme
Dideberg, O.; Joris, Bernard ULg; Frère, Jean-Marie ULg et al

in FEBS Letters (1980), 117(1-2), 215-218

Detailed reference viewed: 10 (0 ULg)
Full Text
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)

Detailed reference viewed: 8 (1 ULg)
Full Text
Peer Reviewed
See detailParvalbumins from the lungfish (Protopterus dolloi).
Gerday, Charles ULg; Joris, Bernard ULg; Gerardin, Nicole ULg et al

in Biochimie (1979), 61

Five parvalbumins have been isolated from the white muscles of the lungfish. They can be divided into two sub families showing typical amino acid compositions, C-terminal amino acid residues, peptide maps ... [more ▼]

Five parvalbumins have been isolated from the white muscles of the lungfish. They can be divided into two sub families showing typical amino acid compositions, C-terminal amino acid residues, peptide maps and immuno-reactivity. The red muscles including the cardiac muscle also contain parvalbumins in amounts roughly inversely related to the concentration of myoglobin in the muscle. Parvalbumins have also been detected in the brain and kidney. [less ▲]

Detailed reference viewed: 1 (0 ULg)