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See detailThe Beta-Lactamase Cycle: A Tale of Selective Pressure and Bacterial Ingenuity
Matagne, André ULg; Dubus, Alain; Galleni, Moreno ULg et al

in Natural Product Reports (1999), 16(1), 1-19

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See detailMechanistic Diversity of Beta-Lactamases
Frère, Jean-Marie ULg; Dubus, Alain; Galleni, Moreno ULg et al

in Biochemical Society Transactions (1999), 27(2), 58-63

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See detailThe Folding Process of Hen Lysozyme: A Perspective from the 'New View'
Matagne, André ULg; Dobson, Christopher M.

in Cellular and Molecular Life Sciences : CMLS (1998), 54(4), 363-71

How a conformationally disordered polypeptide chain rapidly and efficiently achieves its well-defined native structure is still a major question in modern structural biology. Although much progress has ... [more ▼]

How a conformationally disordered polypeptide chain rapidly and efficiently achieves its well-defined native structure is still a major question in modern structural biology. Although much progress has been made towards rationalizing the principles of protein structure and dynamics, the mechanism of the folding process and the determinants of the final fold are not yet known in any detail. One protein for which folding has been studied in great detail by a combination of diverse techniques is hen lysozyme. In this article we review the present state of our knowledge of the folding process of this enzyme and focus in particular on recent experiments to probe some of its specific features. These results are then discussed in the context of the 'new view' of protein folding based on energy surfaces and landscapes. It is shown that a schematic energy surface for lysozyme folding, which is broadly consistent with our experimental data, begins to provide a unified model for protein folding through which experimental and theoretical ideas can be brought together. [less ▲]

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See detailCatalytic Properties of Class a Beta-Lactamases: Efficiency and Diversity
Matagne, André ULg; Lamotte-Brasseur, Josette; Frère, Jean-Marie ULg

in Biochemical Journal (1998), 330((Pt 2)), 581-98

beta-Lactamases are the main cause of bacterial resistance to penicillins, cephalosporins and related beta-lactam compounds. These enzymes inactivate the antibiotics by hydrolysing the amide bond of the ... [more ▼]

beta-Lactamases are the main cause of bacterial resistance to penicillins, cephalosporins and related beta-lactam compounds. These enzymes inactivate the antibiotics by hydrolysing the amide bond of the beta-lactam ring. Class A beta-lactamases are the most widespread enzymes and are responsible for numerous failures in the treatment of infectious diseases. The introduction of new beta-lactam compounds, which are meant to be 'beta-lactamase-stable' or beta-lactamase inhibitors, is thus continuously challenged either by point mutations in the ubiquitous TEM and SHV plasmid-borne beta-lactamase genes or by the acquisition of new genes coding for beta-lactamases with different catalytic properties. On the basis of the X-ray crystallography structures of several class A beta-lactamases, including that of the clinically relevant TEM-1 enzyme, it has become possible to analyse how particular structural changes in the enzyme structures might modify their catalytic properties. However, despite the many available kinetic, structural and mutagenesis data, the factors explaining the diversity of the specificity profiles of class A beta-lactamases and their amazing catalytic efficiency have not been thoroughly elucidated. The detailed understanding of these phenomena constitutes the cornerstone for the design of future generations of antibiotics. [less ▲]

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See detailThe origin of the alpha-domain intermediate in the folding of hen lysozyme
Matagne, André ULg; Chung, E. W.; Ball, L. J. et al

in Journal of Molecular Biology (1998), 277(5), 997-1005

Stopped-flow fluorescence and circular dichroism spectroscopy have been used in conjunction with quenched-flow hydrogen exchange labelling, monitored by electrospray ionization mass spectrometry, to ... [more ▼]

Stopped-flow fluorescence and circular dichroism spectroscopy have been used in conjunction with quenched-flow hydrogen exchange labelling, monitored by electrospray ionization mass spectrometry, to compare the refolding kinetics of hen egg-white lysozyme at 20 degrees C and 50 degrees C. At 50 degrees C there is clear evidence for distinct fast and slow refolding populations, as observed at 20 degrees C, although folding occurs significantly more rapidly. The folding process is, however, substantially more cooperative at the higher temperature. In particular, the transient intermediate on the major refolding pathway at 20 degrees C, having persistent native-like structure in the alpha-helical domain of the protein, is not detected by hydrogen exchange labelling at 50 degrees C. Ln addition, the characteristic maximum in negative ellipticity and the minimum in fluorescence intensity observed in far UV CD and intrinsic fluorescence experiments at 20 degrees C, respectively, are not seen at 50 degrees C. Addition of 2 M NaCl to the refolding buffer at 50 degrees C, however, regenerates both the hydrogen exchange and optical properties associated with the alpha-domain intermediate but has no significant effect on the overall refolding kinetics. Together with previous findings, these results indicate that non-native interactions within the alpha-domain intermediate are directly responsible for the unusual optical properties observed during refolding, and that this intermediate accumulates as a consequence of its intrinsic stability in a folding process where the formation of stable structure in the beta-domain constitutes the rate-limiting step for the majority of molecules. (C) 1998 Academic Press Limited. [less ▲]

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See detailFast and slow tracks in lysozyme folding: Insight into the role of domains in the folding process
Matagne, André ULg; Radford, S. E.; Dobson, C. M.

in Journal of Molecular Biology (1997), 267(5), 1068-1074

The folding of lysozyme involves parallel events in which hydrogen exchange kinetics indicate the development of persistent structure at very different rates. We have monitored directly the kinetics of ... [more ▼]

The folding of lysozyme involves parallel events in which hydrogen exchange kinetics indicate the development of persistent structure at very different rates. We have monitored directly the kinetics of formation of the native molecule by the binding of a fluorescently labelled inhibitor, MeU-diNAG (4-methylumbelliferyl-N,N'-diacetyl-beta-D-chitobioside). The data show that native character monitored in this way also develops with different timescales. Although the rate determining step on the slow pathway (similar to 75% of molecules at pH 5.5, 20 degrees C) can be attributed to the need to reorganise structure formed early in the folding process, the data indicate that the rate determining step on the fast track (involving similar to 25% of molecules) involves the docking of the two constituent domains of the protein. In the fast folding track the data are consistent with a model in which each domain forms persistent structure prier to their docking in a locally cooperative manner on a timescale comparable to the folding of small single domain proteins. (C) 1997 Academic Press Limited. [less ▲]

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See detailContribution of Mutant Analysis to the Understanding of Enzyme Catalysis: The Case of Class a Beta-Lactamases
Matagne, André ULg; Frère, Jean-Marie ULg

in Biochimica et Biophysica Acta (1995), 1246(2), 109-27

Class A beta-lactamases represent a family of well studied enzymes. They are responsible for many antibiotic resistance phenomena and thus for numerous failures in clinical chemotherapy. Despite the facts ... [more ▼]

Class A beta-lactamases represent a family of well studied enzymes. They are responsible for many antibiotic resistance phenomena and thus for numerous failures in clinical chemotherapy. Despite the facts that five structures are known at high resolution and that detailed analyses of enzymes modified by site-directed mutagenesis have been performed, their exact catalytic mechanism remains controversial. This review attempts to summarize and to discuss the many available data. [less ▲]

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See detailKinetic Study of Interaction between Brl 42715, Beta-Lactamases, and D-Alanyl-D-Alanine Peptidases
Matagne, André ULg; Ledent, Philippe; Monnaie, Didier et al

in Antimicrobial Agents and Chemotherapy (1995), 39(1), 227-31

A detailed kinetic study of the interactions between BRL 42715, a beta-lactamase-inhibiting penem, and various beta-lactamases (EC 3.5.2.6) and D-alanyl-D-alanine peptidases (DD-peptidases, EC 3.4.16.4 ... [more ▼]

A detailed kinetic study of the interactions between BRL 42715, a beta-lactamase-inhibiting penem, and various beta-lactamases (EC 3.5.2.6) and D-alanyl-D-alanine peptidases (DD-peptidases, EC 3.4.16.4) is presented. The compound was a very efficient inactivator of all active-site serine beta-lactamases but was hydrolyzed by the class B, Zn(2+)-containing enzymes, with very different kcat values. Inactivation of the Streptomyces sp. strain R61 extracellular DD-peptidase was not observed, and the Actinomadura sp. strain R39 DD-peptidase exhibited a low level of sensitivity to the compound. [less ▲]

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See detailSTRUCTURAL AND KINETIC CHARACTERIZATION OF A BETA-LACTAMASE-INHIBITOR PROTEIN
STRYNADKA, N. C. J.; JENSEN, S. E.; JOHNS, K. et al

in Nature (1994), 368(6472), 657-660

THE past decade has seen an alarming worldwide increase in resistance to beta-lactam antibiotics among many pathogenic bacteria1, which is due mainly to plasmid- or chromosomally encoded beta-lactamases ... [more ▼]

THE past decade has seen an alarming worldwide increase in resistance to beta-lactam antibiotics among many pathogenic bacteria1, which is due mainly to plasmid- or chromosomally encoded beta-lactamases that specifically cleave penicillin and cephalosporins, rendering them inactive. There is therefore a need to develop new strategies in the design of effective inhibitors of beta-lactamase. All the small-molecule inhibitors in clinical use are not very effective and are rapidly degraded2,3. Furthermore, newly characterized mutants of the plasmid-mediated beta-lactamase TEM-1 are highly resistant to these small-molecule inhibitors, including clavulanic acid and tazobactam4. It has been shown that Streptomyces clavuligerus produces an exocellular beta-lactamase inhibitory protein (BLIP; M(r) 17.5 K)5. Here we present data defining BLIP as the most effective known inhibitor of a variety of beta-lactamases, with K(i) values in the subnanomolar to picomolar range. To identify those features in BLIP that make it such a potent inhibitor, we have determined its molecular structure at 2.1 angstrom resolution. BLIP is a relatively flat molecule with a unique fold, comprising a tandem repeat of a 76-amino-acid domain. Each domain consists of a helix-loop-helix motif that packs against a four-stranded antiparallel beta-sheet (Fig. 1a). To our knowledge, BLIP is the first example of a protein inhibitor having two similarly folded domains that interact with and inhibit a single target enzyme. [less ▲]

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See detailInteractions between Active-Site-Serine Beta-Lactamases and Mechanism-Based Inactivators: A Kinetic Study and an Overview
Matagne, André ULg; Ghuysen, M. F.; Frère, Jean-Marie ULg

in Biochemical Journal (1993), 295((Pt 3)), 705-711

The interactions between three class A beta-lactamases and three beta-lactamase inactivators (clavulanic acid, sulbactam and olivanic acid MM13902) were studied. Interestingly, the interaction between the ... [more ▼]

The interactions between three class A beta-lactamases and three beta-lactamase inactivators (clavulanic acid, sulbactam and olivanic acid MM13902) were studied. Interestingly, the interaction between the Streptomyces cacaoi beta-lactamase and clavulanate indicated little irreversible inactivation. With sulbactam, irreversible inactivation was found to occur with the three studied enzymes, but no evidence for transiently inactivated adducts was found. Irreversible inactivation of the S. albus G and S. cacaoi enzymes was particularly slow. With olivanate, irreversible inactivation was also observed with the three enzymes, but with the S. cacaoi enzyme, no hydrolysis could be detected. A tentative summary of the results found in the literature is also presented (including 6 beta-halogenopenicillanates), and the general conclusions underline the diversity of the mechanisms and the wide variations of the rate constants observed when class A beta-lactamases interact with beta-lactamase inactivators, in agreement with the behaviours of the same enzymes towards their good and poor substrates. [less ▲]

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See detailInteractions between Active-Site Serine Beta-Lactamases and So-Called Beta-Lactamase-Stable Antibiotics. Kinetic and Molecular Modelling Studies
Matagne, André ULg; Lamotte-Brasseur, J.; Frère, Jean-Marie ULg

in European Journal of Biochemistry (1993), 217(1), 61-67

The interactions between imipenem and four monobactams and three class A beta-lactamases have been studied in detail. Despite their reputation as being beta-lactamase-stable, some of these compounds were ... [more ▼]

The interactions between imipenem and four monobactams and three class A beta-lactamases have been studied in detail. Despite their reputation as being beta-lactamase-stable, some of these compounds were significantly hydrolysed by the enzymes. The results obtained with the Streptomyces albus G beta-lactamase have been analysed in the light of molecular modelling studies. The discussion is extended to include other so-called beta-lactamase-stable antibiotics to demonstrate that this appellation can often be misleading. [less ▲]

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See detailInteractions between Active-Site-Serine Beta-Lactamases and Compounds Bearing a Methoxy Side Chain on the Alpha-Face of the Beta-Lactam Ring: Kinetic and Molecular Modelling Studies
Matagne, André ULg; Lamotte-Brasseur, J.; Dive, Georges ULg et al

in Biochemical Journal (1993), 293((Pt 3)), 607-611

The interactions between three class A beta-lactamases and compounds bearing a methoxy side chain on the alpha-face of the beta-lactam ring (cefoxitin, moxalactam and temocillin) have been studied. When ... [more ▼]

The interactions between three class A beta-lactamases and compounds bearing a methoxy side chain on the alpha-face of the beta-lactam ring (cefoxitin, moxalactam and temocillin) have been studied. When compared with the situation prevailing with good substrates, both acylation and deacylation steps appeared to be severely impaired. Molecular modelling studies of the structures of the Henri-Michaelis complexes and of the acyl-enzymes indicate a major displacement of the crystallographically observed water molecule which connects the glutamate-166 and serine-70 side chains and underline the role of this water molecule in both reaction steps. [less ▲]

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See detailInduction of a Streptomyces Cacaoi Beta-Lactamase Gene Cloned in S. Lividans
Lenzini, V. M.; Magdalena, J.; Fraipont, Claudine ULg et al

in Molecular & General Genetics [=MGG] (1992), 235(1), 41-8

The previously cloned class A beta-lactamase gene (bla) of Streptomyces cacaoi was shown to be inducible by beta-lactam compounds in the host organism S. lividans. A regulatory region of 2.75 kb was ... [more ▼]

The previously cloned class A beta-lactamase gene (bla) of Streptomyces cacaoi was shown to be inducible by beta-lactam compounds in the host organism S. lividans. A regulatory region of 2.75 kb was identified and the nucleotide sequence determined. It contained four open reading frames (ORFs) of which only two were complete and required for induction. ORF1-ORF2 exerted a positive regulatory effect on the expression of bla. Inactivation of ORF1 or of ORF2 resulted not only in the loss of induction, but also in a 30- to 60-fold decrease in the basal (non-induced) level of beta-lactamase production. ORF1 codes for a DNA-binding protein related to the AmpR repressor/activator, which controls the expression of ampC (class C beta-lactamase) genes in several Enterobacteria. [less ▲]

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See detailAnomalous Behaviour of a Protein During Sds/Page Corrected by Chemical Modification of Carboxylic Groups
Matagne, André ULg; Joris, Bernard ULg; Frère, Jean-Marie ULg

in Biochemical Journal (1991), 280((Pt 2)), 553-6

The 29,000-Mr Actinomadura R39 beta-lactamase exhibited a remarkably low electrophoretic mobility on SDS/PAGE, yielding an Mr value almost twice that computed from the corresponding gene sequence. We ... [more ▼]

The 29,000-Mr Actinomadura R39 beta-lactamase exhibited a remarkably low electrophoretic mobility on SDS/PAGE, yielding an Mr value almost twice that computed from the corresponding gene sequence. We showed that chemical modification of the carboxylic groups of glutamic acid and aspartic acid residues restored a normal electrophoretic mobility and that the anomalous behaviour of that protein on SDS/PAGE was due to its very large negative charge at neutral pH. We also compared the behaviour of the same enzyme on gel filtration in the presence of SDS with those of other class A beta-lactamases (Mr approx. 30,000). These experiments suggested that the very low electrophoretic mobility of the Actinomadura R39 beta-lactamase upon SDS/PAGE was more probably due to a low degree of SDS binding rather than to an unusual shape of the SDS-protein complex. [less ▲]

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See detailRagged N-Termini and Other Variants of Class a Beta-Lactamases Analysed by Chromatofocusing
Matagne, André ULg; Joris, Bernard ULg; Van Beeumen, J. et al

in Biochemical Journal (1991), 273(273), 503-10

Four beta-lactamases excreted by Gram-positive bacteria exhibited microheterogeneity when analysed by chromatofocusing or ion-exchange chromatography. Ragged N-termini were in part responsible for the ... [more ▼]

Four beta-lactamases excreted by Gram-positive bacteria exhibited microheterogeneity when analysed by chromatofocusing or ion-exchange chromatography. Ragged N-termini were in part responsible for the charge variants, but deamidation of an asparagine residue was also involved, at least for the Bacillus licheniformis enzyme. The activity of a contaminating proteinase could also be demonstrated in the case of Actinomadura R39 beta-lactamase. With that enzyme, proteolysis resulted in partial inactivation, but the inactivated fragments were easily separated from the active forms. With these, as with the other enzymes, the kinetic parameters of the major variants were identical with those of the mixture within the limits of experimental error, so that the catalytic properties of these enzymes can be determined with the 'heterogeneous' preparations. [less ▲]

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See detailMechanism of action of β-lactamases and DD-peptidases
Frère, Jean-Marie ULg; Joris, Bernard ULg; Jacob, Françoise et al

in Pandit, U.K.; Alderweireldt, F.C. (Eds.) Bioorganic Chemistry in Healthcare and Technology (1991)

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See detailTHE MUTATION LYS234HIS YIELDS A CLASS-A BETA-LACTAMASE WITH A NOVEL PH-DEPENDENCE
BRANNIGAN, J.; Matagne, André ULg; Jacob, Françoise et al

in Biochemical Journal (1991), 278(Part 3), 673-678

The lysine-234 residue is highly conserved in beta-lactamases and in nearly all active-site-serine penicillin-recognizing enzymes. Its replacement by a histidine residue in the Streptomyces albus G class ... [more ▼]

The lysine-234 residue is highly conserved in beta-lactamases and in nearly all active-site-serine penicillin-recognizing enzymes. Its replacement by a histidine residue in the Streptomyces albus G class A beta-lactamase yielded an enzyme the pH-dependence of which was characterized by the appearance of a novel pK, which could be attributed to the newly introduced residue. At low pH, the k(cat.) value for benzylpenicillin was as high as 50 % of that of the wild-type enzyme, demonstrating that an efficient active site was maintained. Both k(cat.) and k(cat.)/K(m) dramatically decreased above pH 6 but the decrease in k(cat.)/K(m) could not be attributed to larger K(m) values. Thus a positive charge on the side chain of residue 234 appears to be more essential for transition-state stabilization than for initial recognition of the substrate ground state. [less ▲]

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See detailDiversity of the Mechanisms of Resistance to Beta-Lactam Antibiotics
Frère, Jean-Marie ULg; Joris, Bernard ULg; Granier, B. et al

in Research in Microbiology (1991), 142(6, Jul-Aug), 705-10

The sensitivity of a bacterium to beta-lactam antibiotics depends upon the interplay between 3 independent factors: the sensitivity of the essential penicillin-binding enzyme(s), the quantity and ... [more ▼]

The sensitivity of a bacterium to beta-lactam antibiotics depends upon the interplay between 3 independent factors: the sensitivity of the essential penicillin-binding enzyme(s), the quantity and properties of the beta-lactamase(s) and the diffusion barrier that the outer-membrane of Gram-negative bacteria can represent. Those three factors can be modified by mutations or by the horizontal transfer of genes or portions of genes. [less ▲]

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See detailThe Diversity of the Catalytic Properties of Class a Beta-Lactamases
Matagne, André ULg; Misselyn-Bauduin, A. M.; Joris, Bernard ULg et al

in Biochemical Journal (1990), 265(1), 131-46

The catalytic properties of four class A beta-lactamases were studied with 24 different substrates. They exhibit a wide range of variation. Similarly, the amino acid sequences are also quite different ... [more ▼]

The catalytic properties of four class A beta-lactamases were studied with 24 different substrates. They exhibit a wide range of variation. Similarly, the amino acid sequences are also quite different. However, no relationships were found between the sequence similarities and the substrate profiles. Lags and bursts were observed with various compounds containing a large sterically hindered side chain. As a group, the enzymes could be distinguished from the class C beta-lactamases on the basis of the kappa cat. values for several substrates, particularly oxacillin, cloxacillin and carbenicillin. Surprisingly, that distinction was impossible with the kappa cat./Km values, which represent the rates of acylation of the active-site serine residue by the beta-lactam. For several cephalosporin substrates (e.g. cefuroxime and cefotaxime) class A enzymes consistently exhibited higher kappa cat. values than class C enzymes, thus belying the usual distinction between 'penicillinases' and 'cephalosporinases'. The problem of the repartition of class A beta-lactamases into sub-classes is discussed. [less ▲]

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See detailUnexpected Influence of Ionic Strength on Branched-Pathway Interactions between Beta-Lactamases and Beta-Halogenopenicillanates
De Meester, F.; Matagne, André ULg; Dive, Georges ULg et al

in Biochemical Journal (1989), 257(1), 245-9

Ionic strength strongly influenced the turnover/inactivation ratio in the interaction between beta-halogenopenicillanates and some class A beta-lactamases. This suggested the stabilization of a highly ... [more ▼]

Ionic strength strongly influenced the turnover/inactivation ratio in the interaction between beta-halogenopenicillanates and some class A beta-lactamases. This suggested the stabilization of a highly charged intermediate by solvation. Those data could be interpreted on the basis of a reaction pathway where an episulphonium ion was transiently formed. The various mechanisms proposed for explaining the formation of the dihydrothiazine chromophore are discussed. [less ▲]

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