References of "Dive, Georges"
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See detailTheoretical study of the C-N bond breakage catalyzed by the serine peptidases
Dive, Georges ULg; Peeters, Daniel; Leroy, Georges et al

in Journal of Molecular Structure : Theochem (1984), 16

The conditions of C---N bond breakage by the serine peptidases have been analysed. A two-way table has been generated where either formamide or protonated formamide serves as minimal model of the scissile ... [more ▼]

The conditions of C---N bond breakage by the serine peptidases have been analysed. A two-way table has been generated where either formamide or protonated formamide serves as minimal model of the scissile C---N bond and where either methanol or the couple CH3O− H+ serves as minimal model of the attacking nucleophile. An addition-elimination reaction is proposed which links the enzyme acylation and deacylation steps. [less ▲]

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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 ▲]

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See detailOn the structural analogy between D-alanyl-D-alanine terminated peptides and β-lactam antibiotics
Brasseur, Josette ULg; Dive, Georges ULg; Ghuysen, Jean-Marie ULg

in European Journal of Medicinal Chemistry (1984), 4

Structural analogy between D-alanyl-D-alanine terminated peptides (and analogues) of varying substrate activity toward D-alanyl-D-alanine-cleaving peptidases, and bicyclic fused ring azetidinone ... [more ▼]

Structural analogy between D-alanyl-D-alanine terminated peptides (and analogues) of varying substrate activity toward D-alanyl-D-alanine-cleaving peptidases, and bicyclic fused ring azetidinone structures of varying inactivating potency toward the same enzymes has been exa-mihed by comparing the relative spatial disposition of the carboxylate function at the C-terminal position and the amide function at the N-terminal position with respect to the scissile amide bond at the central position. The observed variations in the geometric parameters and the molecular electrostatic potential maps generated by these functional groups suggest multiple modes of binding. In the monobactam sulfazecin, the relative disposition of at least the scissile amide bond and the terminal sulphamate group is comparable to that of the corresponding functions in the bicyclic β-lactams. [less ▲]

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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 detailThe active sites of the D-alanyl-D-alanine-cleaving peptidases
Charlier, Paulette ULg; Dideberg, Otto; Dive, Georges ULg 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)

The active site structures of D-alanyl-D-alanine-cleaving peptidases G, R61, R39, and K15 from Streptomyces and Actinomadura are discussed in relation to their substrate specificities and kinetic ... [more ▼]

The active site structures of D-alanyl-D-alanine-cleaving peptidases G, R61, R39, and K15 from Streptomyces and Actinomadura are discussed in relation to their substrate specificities and kinetic mechanisms. [less ▲]

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See detailA statistical analysis of the theoretical results obtained for concerted 1,3-dipolar cycloaddition
Sana, Michel; Leroy, Georges; Dive, Georges ULg et al

in Journal of Molecular Structure : Theochem (1982), 89(1-2), 147-163

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See detailAcide cyclohexyl-4 naphtalène-1-propionique
Dupont, Léon; Dideberg, Otto; Dive, Georges ULg et al

in Acta Crystallographica. Section B-Structural Crystallography and Crystal Chemistry (1982), 38(9), 2409-2411

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See detailStructure de l'hydrogénonitrate de l'isopropyl-1 {[(pipéridyl-1 amino)-4 pyridyl-3]sulfonyl}-3 urée
Dupont, Léon; Dideberg, Otto; Delarge, Jacques et al

in Acta Crystallographica. Section B-Structural Crystallography and Crystal Chemistry (1982), 38(5), 1495-1500

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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 ▲]

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See detailTorasemide: a comparison of two refinement computer programs and effects on CNDO/2 calculations
Dupont, Léon; Dive, Georges ULg

in Extrait du Bulletin de la Société Royale des Sciences de Liège (1982), 5-8

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See detailComparison of levels of cytosol estrogen receptors with "arterial" and "venous" concentrations of gonadic steroids in mammary tumors.
Duvivier, Joseph; Colin, Claude; Hustin, Jean et al

in Clinica Chimica Acta (1981), 112(1), 21-32

Plasma steroid concentrations measured in the post-menopausal women with breast cancer showed a close correlation between the various androgens. The post-menopausal women exhibited a correlation between ... [more ▼]

Plasma steroid concentrations measured in the post-menopausal women with breast cancer showed a close correlation between the various androgens. The post-menopausal women exhibited a correlation between estrogen receptors (ER) and "arterial" 17 alpha-hydroxyprogesterone levels in the breast. ER levels expressed as a function of plasma (arterial) steroid (P/17 P) molar concentration ratio were distributed within a hyperbola, suggesting the existence of a control mechanism for breast cell ER levels. [less ▲]

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See detailTetrakis(propylthio)-2,2,6,6' azoxy-3,3' pyridine
Lamotte, Josette; Dupont, Léon; Dideberg, Otto et al

in Acta Crystallographica. Section B-Structural Crystallography and Crystal Chemistry (1980), 36

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See detailNouvelle version du programme CNINDO
Dive, Georges ULg; Lapière, Charles Léon

in Bulletin des Sociétés Chimiques Belges (1980), 89

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See detailLe programme BMDP7M d'analyse discriminante et son application à l'étude d'une structure chimique
Dive, Georges ULg; Lennes, Georges

in collection des publications de la faculté des sciences appliquées de l'université de Liège (1978), 73

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See detailComparaison des tests d'hypothèse dans les programmes BMD11V et BMDP7M
Lennes, Georges; Dive, Georges ULg

in Collection des publications de la faculté des sciences appliquées de l'université de Liège (1978), 73

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See detailL'utilisation des programmes de description des "Biomedical Computer Programs (BMD - BMDP)
Dive, Georges ULg; Monfort, Franz

in collection des publications de la faculté des sciences appliquées de l'université de Liège (1978), 73

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See detailAnalyse conformationnelle de dérivés arylacétiques et proprioniques à activité antiinflammatoire
Dive, Georges ULg; Lapière, Charles Léon; Leroy, Georges

in Bulletin des Sociétés Chimiques Belges (1977), 86(1-2), 73-80

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