References of "Charlier, Paulette"
     in
Bookmark and Share    
Full Text
Peer Reviewed
See detailStudy of the Zn-containing DD-carboxypeptidase of Streptomyces albus G by small-angle X-ray scattering in solution.
Labischinski, Harald; Giesbrecht, Peter; Fischer, E. et al

in European Journal of Biochemistry (1984), 138(1), 83-87

Study of the Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase of Streptomyces albus G by small-angle X-ray scattering in solution yielded the following molecular parameters: radius of gyration ... [more ▼]

Study of the Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase of Streptomyces albus G by small-angle X-ray scattering in solution yielded the following molecular parameters: radius of gyration R = 1.82 +/- 0.05 nm; largest diameter D = 5.9 +/- 0.2 nm; relative molecular mass Mr = 17000 +/- 2000; volume V approximately equal to 35 +/- 2 nm3; degree of hydration: 0.25 +/- 0.02 g water/g protein. By reference to theoretical scattering curves of rigid triaxial homogeneous bodies, a model which fits all experimental data is an elliptical cylinder. Such a model is compatible with that observed in the crystal structure. At those high concentrations necessary to form inactive enzyme-ligand associations the non-competitive beta-lactam inhibitors, cephalothin and cephalosporin C, drastically altered the scattering behaviour of the protein. [less ▲]

Detailed reference viewed: 11 (0 ULg)
Full Text
Peer Reviewed
See detailActive-site-directed inactivators of the Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase of Streptomyces albus G.
Charlier, Paulette ULg; Dideberg, Otto; Jamoulle, Jean-Claude et al

in Biochemical Journal (1984), 219(3), 763-772

Several types of active-site-directed inactivators (inhibitors) of the Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase were tested. (i) Among the heavy-atom-containing compounds examined ... [more ▼]

Several types of active-site-directed inactivators (inhibitors) of the Zn2+-containing D-alanyl-D-alanine-cleaving carboxypeptidase were tested. (i) Among the heavy-atom-containing compounds examined, K2Pt(C2O4)2 inactivates the enzyme with a second-order rate constant of about 6 X 10(-2)M-1 X S-1 and has only one binding site located close to the Zn2+ cofactor within the enzyme active site. (ii) Several compounds possessing both a C-terminal carboxylate function and, at the other end of the molecule, a thiol, hydroxamate or carboxylate function were also examined. 3-Mercaptopropionate (racemic) and 3-mercaptoisobutyrate (L-isomer) inhibit the enzyme competitively with a Ki value of 5 X 10 X 10(-9)M. (iii) Classical beta-lactam compounds have a very weak inhibitory potency. Depending on the structure of the compounds, enzyme inhibition may be competitive (and binding occurs to the active site) or non-competitive (and binding causes disruption of the protein crystal lattice). (iv) 6-beta-Iodopenicillanate inactivates the enzyme in a complex way. At high beta-lactam concentrations, the pseudo-first-order rate constant of enzyme inactivation has a limit value of 7 X 10(-4)S-1 X 6-beta-Iodopenicillanate binds to the active site just in front of the Zn2+ cofactor and superimposes histidine-190, suggesting that permanent enzyme inactivation is by reaction with this latter residue. [less ▲]

Detailed reference viewed: 15 (3 ULg)
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)
Peer Reviewed
See detailCrystallographic data for the beta-lactamase from Enterobacter cloacae P99.
Charlier, Paulette ULg; Dideberg, O.; Frère, Jean-Marie ULg et al

in Journal of Molecular Biology (1983), 171(2), 237-8

The beta-lactamase from Enterobacter cloacae P99 has been crystallized from polyethylene glycol solution at pH 7. X-ray examination of the orthorhombic crystals shows the space group is P2(1)2(1)2 with ... [more ▼]

The beta-lactamase from Enterobacter cloacae P99 has been crystallized from polyethylene glycol solution at pH 7. X-ray examination of the orthorhombic crystals shows the space group is P2(1)2(1)2 with unit cell dimensions a = 77.4 A, b = 69.4 A, and c = 63.6 A. There is one molecule of molecular weight 39,000 in the asymmetric unit. [less ▲]

Detailed reference viewed: 22 (1 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)
Peer Reviewed
See detailCrystallization and preliminary X-ray data for parvalbumin IIIf of Opsanus tau.
Hamoir, G.; Dideberg, O.; Charlier, Paulette ULg

in Journal of Molecular Biology (1981), 153(2), 487-9

Detailed reference viewed: 17 (1 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 detailThe 4.5 A resolution structure analysis of the exocellular DD-carboxypeptidase of Streptomyces albus G.
Dideberg, Otto; Charlier, Paulette ULg; Dupont, Léon et al

in FEBS Letters (1980), 117(1), 212-214

Detailed reference viewed: 17 (2 ULg)
Peer Reviewed
See detailCrystallographic studies of low penicillin-sensitive enzyme excreted by Streptomyces albus G [proceedings]
Dideberg, O.; Charlier, Paulette ULg

in Archives Internationales de Physiologie et de Biochimie (1979), 87(5), 1045

Detailed reference viewed: 16 (1 ULg)