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See detailCompetitive inhibitors of the CphA metallo-beta-lactamase from Aeromonas hydrophila
Horsfall, L. E.; Garau, G.; Lienard, B. M. et al

in Antimicrobial Agents and Chemotherapy (2007), 51(6), 2136-2142

Various inhibitors of metallo-beta-lactamases have been reported; however, none are effective for all subgroups. Those that have been found to inhibit the enzymes of subclass B2 (catalytically active with ... [more ▼]

Various inhibitors of metallo-beta-lactamases have been reported; however, none are effective for all subgroups. Those that have been found to inhibit the enzymes of subclass B2 (catalytically active with one zinc) either contain a thiol (and show less inhibition towards this subgroup than towards the dizinc members of B1 and B3) or are inactivators behaving as substrates for the dizinc family members. The present work reveals that certain pyridine carboxylates are competitive inhibitors of CphA, a subclass B2 enzyme. X-ray crystallographic analyses demonstrate that pyridine-2,4-dicarboxylic acid chelates the zinc ion in a bidentate manner within the active site. Salts of these compounds are already available and undergoing biomedical testing for various nonrelated purposes. Pyridine carboxylates appear to be useful templates for the development of more-complex, selective, nontoxic inhibitors of subclass B2 metallo-beta-lactamases. [less ▲]

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See detailUpdate of the standard numbering scheme for class B beta-lactamases
Garau, G.; Garcia-Saez, I.; Bebrone, Carine ULg et al

in Antimicrobial Agents and Chemotherapy (2004), 48(7), 2347-2349

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See detailThe structures and catalytic mechanisms of active-site serine beta-lactamases.
Lamotte, Josette ULg; Knox, J.; Kelly, J. A. et al

in Biotechnology & Genetic Engineering Reviews (1994), 12

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See detailCrystallization of a genetically engineered water-soluble primary penicillin target enzyme. The high molecular mass PBP2x of Streptococcus pneumoniae.
Charlier, Paulette ULg; Buisson, G.; Dideberg, O. et al

in Journal of Molecular Biology (1993), 232(3), 1007-9

A genetically engineered water-soluble derivative of PBP2x of Streptococcus pneumoniae has been produced, purified and crystallized in a form suitable for X-ray diffraction analysis. The best crystals ... [more ▼]

A genetically engineered water-soluble derivative of PBP2x of Streptococcus pneumoniae has been produced, purified and crystallized in a form suitable for X-ray diffraction analysis. The best crystals have been grown at 15 degrees C, from solutions containing 8% polyethylene glycol 10,000 at pH values ranging from 3.9 to 6.0. These crystals diffract to a resolution of 3.5 A and have a space group P6(1)22 (or enantiomorph) with unit cell dimensions of a = b = 162.2 A, c = 171.8 A, alpha = beta = 90 degrees, gamma = 120 degrees. The molecular mass and cell dimensions suggest that there is one molecule of enzyme per asymmetric unit. The breakdown of a chromogenic cephalosporin derivative diffused into a crystal reveals clearly that the enzyme is active in the crystalline state. [less ▲]

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See detailStructure du 8-chloro-11-(méthylpipérazin-1-yl)dibenzo[b,f]-1,4-thiazépine
Dupont, L.; Dideberg, O.; Liégeois, Jean-François ULg et al

in Acta Crystallographica Section C-Crystal Structure Communications (1992), C48

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See detailStructure du 6-(4-méthylpipérazin-1-yl)-11H-pyrido[2,3-b][1,4]benzodiazépine 1,5-hydrate
Dupont, L.; Englebert, S.; Dideberg, O. et al

in Acta Crystallographica Section C-Crystal Structure Communications (1992), C48

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See detailComparison of the Sequences of Class a β-lactamase and of the Secondary Structure Elements of Penicillin-Recognizing Proteins
Joris, Bernard ULg; Ledent, P.; Dideberg, O. et al

in Antimicrobial Agents and Chemotherapy (1991), 35(11), 2294-2301

The sequences of class A beta-lactamases were compared. Four main groups of enzymes were distinguished: those from the gram-negative organisms and bacilli and two distinct groups of Streptomyces spp. The ... [more ▼]

The sequences of class A beta-lactamases were compared. Four main groups of enzymes were distinguished: those from the gram-negative organisms and bacilli and two distinct groups of Streptomyces spp. The Staphylococcus aureus PC1 enzyme, although somewhat closer to the enzyme from the Bacillus group, did not belong to any of the groups of beta-lactamases. The similarities between the secondary structure elements of these enzymes and those of the class C beta-lactamases and of the Streptomyces sp. strain R61 DD-peptidase were also analyzed and tentatively extended to the class D beta-lactamases. A unified nomenclature of secondary structure elements is proposed for all the penicillin-recognizing enzymes. [less ▲]

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See detailStructures du 11-formyl-5-(4-méthylpipérazin-1-yl)-11H-pyrido[2,3b][1,5]benzodiazépine et du 6-(4-méthylpipérazin-1-yl)-11-méthyl-11H-pyrido[2,3-b][1,4]benzodiazépine
Dupont, L.; Englebert, S.; Dideberg, O. et al

in Acta Crystallographica Section C-Crystal Structure Communications (1991), C47

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See detailStructure du méthyl-4 pipérazinyl-1)-10 pyrido[4,3-b][1,4]benzothiazépine
Dupont, L.; Dideberg, O.; Liégeois, Jean-François ULg et al

in Acta Crystallographica Section C-Crystal Structure Communications (1991), C47

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See detailStructure de la bétaïne du carboxyméthyl-1 méthylamino-4 triazolium-1,2,4
Dupont, L.; Englebert, S.; Dideberg, O. et al

in Acta Crystallographica (1991), C47

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See detailStructure de l'acide (tert-butylamino-4 oxo-5 triazol-1,2,4 yle-1)acétique
Dupont, L.; Englebert, S.; Dideberg, O. et al

in Acta Crystallographica (1991), C47

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See detailStructures du cyclohexyl-1[(cycloheptylamino-4 pyridyl-3)sulfonyl]-3 urée et de l'hydrogénonitrate du cyclohexyl-1[(cyclooctylamino-4 pyridyl-3)sulfonyl]-3 urée
Dupont, L.; Dideberg, O.; Masereel, B. et al

in Acta Crystallographica (1991), C47

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See detailStructure du [4-phénylacétylimino-1-(1,2,4-triazolio)]acétate de sodium dihydrate
Dupont, L.; Englebert, S.; Dideberg, O. et al

in Acta Crystallographica (1991), C47

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See detailMolecular size and symmetry of Pseudomonas aeruginosa catabolic ornithine carbamoyltransferase. An X-ray crystallography analysis.
Marcq, S.; Diaz-Ruano, A.; Charlier, Paulette ULg et al

in Journal of Molecular Biology (1991), 220(1), 9-12

The catabolic ornithine carbamoyltransferase (EC 2.1.3.3) from Pseudomonas aeruginosa, that shows allosteric behaviour, and a mutant version of this enzyme has been crystallized in several different ... [more ▼]

The catabolic ornithine carbamoyltransferase (EC 2.1.3.3) from Pseudomonas aeruginosa, that shows allosteric behaviour, and a mutant version of this enzyme has been crystallized in several different crystal forms. All of these have been characterized by X-ray diffraction methods. A 4.5 A resolution data set has been collected on a triclinic crystal. Analysis of the data using the self-rotation function shows that 12 monomers associate to form a particle with cubic 23 point group symmetry. [less ▲]

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See detailEngineering a Novel β-Lactamase by a Single Point Mutation
Jacob, F.; Joris, Bernard ULg; Dideberg, O. et al

in Protein Engineering (1990), 4(1), 79-86

beta-Lactamases are widespread and efficient bacterial enzymes which play a major role in bacterial resistance to penicillins and cephalosporins. In order to elucidate the role of the residues lying in a ... [more ▼]

beta-Lactamases are widespread and efficient bacterial enzymes which play a major role in bacterial resistance to penicillins and cephalosporins. In order to elucidate the role of the residues lying in a conserved loop of the enzymatic cavity of the active-site serine Streptomyces albus G beta-lactamase, modified proteins were produced by oligo-directed mutagenesis. Mutation of Asn116, which lies on one side of the active site cavity pointing to the substrate-binding site, into a serine residue resulted in spectacular modifications of the specificity profile of the enzyme. That replacement yielded an enzyme with a nearly unchanged activity towards good penicillin substrates. In sharp contrast its efficiency in hydrolysing cephalosporins was drastically reduced, the best substrates suffering the largest decrease in the second-order rate constant for serine acylation. In fact that single mutation generated a truly new enzyme behaving exclusively as a penicillinase, a situation which is never encountered to the same degree in any of the numerous naturally occurring variants of class A beta-lactamases. [less ▲]

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See detailStructure du N-diméthylaminoéthyl Méthoxy-4 Pyridinesulfonamide-3 et du N-[(éthyl-1pyrrolidinyl-2) méthyl] Pyridinesulfonamide-3
Dupont, L.; Dideberg, O.; Liégeois, Jean-François ULg et al

in Acta Crystallographica Section C-Crystal Structure Communications (1990), C46

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See detailBeta-lactamase of Bacillus licheniformis 749/C at 2 A resolution.
Moews, P. C.; Knox, J. R.; Dideberg, O. et al

in Proteins (1990), 7(2), 156-71

Two crystal forms (A and B) of the 29,500 Da Class A beta-lactamase (penicillinase) from Bacillus licheniformis 749/C have been examined crystallographically. The structure of B-form crystals has been ... [more ▼]

Two crystal forms (A and B) of the 29,500 Da Class A beta-lactamase (penicillinase) from Bacillus licheniformis 749/C have been examined crystallographically. The structure of B-form crystals has been solved to 2 A resolution, the starting model for which was a 3.5 A structure obtained from A-form crystals. The beta-lactamase has an alpha + beta structure with 11 helices and 5 beta-strands seen also in a penicillin target DD-peptidase of Streptomyces R61. Atomic parameters of the two molecules in the asymmetric unit were refined by simulated annealing at 2.0 A resolution. The R factor is 0.208 for the 27,330 data greater than 3 sigma (F), with water molecules excluded from the model. The catalytic Ser-70 is at the N-terminus of a helix and is within hydrogen bonding distance of conserved Lys-73. Also interacting with the Lys-73 are Asn-132 and the conserved Glu-166, which is on a potentially flexible helix-containing loop. The structure suggests the binding of beta-lactam substrates is facilitated by interactions with Lys-234, Thr-235, and Ala-237 in a conserved beta-strand peptide, which is antiparallel to the beta-lactam's acylamido linkage; an exposed cavity near Asn-170 exists for acylamido substituents. The reactive double bond of clavulanate-type inhibitors may interact with Arg-244 on the fourth beta-strand. A very similar binding site architecture is seen in the DD-peptidase. [less ▲]

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See detailStructure de la bétaïne du carboxyméthyl-1 phénylacétylamino-4 triazolium-1,2,4
Dupont, L.; Dideberg, O.; Pirotte, Bernard ULg et al

in Acta Crystallographica (1989), C45

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See detailStructure de la bétaïne phénylacétylamino-5 thiazolium acétate-3 2,63 hydrate
Dupont, L.; Dideberg, O.; Sbit, M. et al

in Acta Crystallographica (1989), C45

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See detailStructure de la panarine Dihydratée, un Nouvel Alcaloïde Extrait d'un Curare Vénézuélien
Dupont, L.; Dideberg, O.; Sbit, M. et al

in Acta Crystallographica Section C-Crystal Structure Communications (1988), C44

The crystal structure of Panarine dihydrate was solved by direct methods. This new alkaloid has a conformation very similar to that of macusine A with a 3-alpha cis configuration. The positive charge on ... [more ▼]

The crystal structure of Panarine dihydrate was solved by direct methods. This new alkaloid has a conformation very similar to that of macusine A with a 3-alpha cis configuration. The positive charge on the quaternary nitrogen coexists with a negative charge on the carboxylate group. Molecules are linked together through van der Waals interactions and five hydrogen bonds involving water molecules. [less ▲]

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