References of "Frère, Jean-Marie"
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See detailThe Active-Site-Serine Penicillin-Recognizing Enzymes as Members of the Streptomyces R61 Dd-Peptidase Family
Joris, Bernard ULiege; Ghuysen, Jean-Marie ULiege; Dive, Georges ULiege et al

in Biochemical Journal (1988), 250(2), 313-324

Homology searches and amino acid alignments, using the Streptomyces R61 DD-peptidase/penicillin-binding protein as reference, have been applied to the beta-lactamases of classes A and C, the Oxa-2 beta ... [more ▼]

Homology searches and amino acid alignments, using the Streptomyces R61 DD-peptidase/penicillin-binding protein as reference, have been applied to the beta-lactamases of classes A and C, the Oxa-2 beta-lactamase (considered as the first known member of an additional class D), the low-Mr DD-peptidases/penicillin-binding proteins (protein no. 5 of Escherichia coli and Bacillus subtilis) and penicillin-binding domains of the high-Mr penicillin-binding proteins (PBP1A, PBP1B, PBP2 and PBP3 of E. coli). Though the evolutionary distance may vary considerably, all these penicillin-interactive proteins and domains appear to be members of a single superfamily of active-site-serine enzymes distinct from the classical trypsin or subtilisin families. The amino acid alignments reveal several conserved boxes that consist of strict identities or homologous amino acids. The significance of these boxes is highlighted by the known results of X-ray crystallography, chemical derivatization and site-directed-mutagenesis experiments. [less ▲]

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See detailStructure-Activity Relationships in the Beta-Lactam Family: An Impossible Dream
Frère, Jean-Marie ULiege; Joris, Bernard ULiege; Varetto, Louis ULiege et al

in Biochemical Pharmacology (1988), 37(1), 125-32

The difficulty of establishing structure-activity relationships in the beta-lactam family of antibiotics stems from the fact that: (1) The targets in various bacteria exhibit widely different ... [more ▼]

The difficulty of establishing structure-activity relationships in the beta-lactam family of antibiotics stems from the fact that: (1) The targets in various bacteria exhibit widely different sensitivities. (2) Some bacteria produce beta-lactamases, enzymes capable of destroying the antibiotics. The rates of the reactions with the beta-lactamases and the target enzymes are not necessarily related. (3) In Gram-negative bacteria, the diffusion rate through the outer membrane varies independently from the two other factors. [less ▲]

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See detailCitrobacter diversus ULA-27 beta-lactamases. Improved purification and general properties.
Amicosante, G.; Oratore, A.; Franceschini, N. et al

in The Biochemical journal (1988), 254(3), 885-90

Two chromosome-encoded beta-lactamases have been purified from Citrobacter diversus ULA-27. They exhibited slightly different isoelectric points (6.8 and 6.2) and very similar Mr values (congruent to 29 ... [more ▼]

Two chromosome-encoded beta-lactamases have been purified from Citrobacter diversus ULA-27. They exhibited slightly different isoelectric points (6.8 and 6.2) and very similar Mr values (congruent to 29,000). Their specificity spectrum was rather wide, since they hydrolysed some cephalosporins with kcat: values similar to those observed with the best penicillin substrates. Cloxacillin, methicillin and imipenem were hydrolysed very slowly. Hydrolysis of azthreonam could not be detected. [less ▲]

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See detailNucleotide sequence of the gene encoding the active-site serine β-lactamase from Streptomyces cacaoi
Lenzini, Mauro V.; Ishihara, Hiroshi; Dusart, Jean et al

in FEMS Microbiology Letters (1988), 49(3), 371-376

The gene encoding the extracellular active-site serine β-lactamase of Streptomyces cacaoi previously cloned into Streptomyces lividans, has the information for the synthesis of a 303 amino-acid precursor ... [more ▼]

The gene encoding the extracellular active-site serine β-lactamase of Streptomyces cacaoi previously cloned into Streptomyces lividans, has the information for the synthesis of a 303 amino-acid precursor. The β-lactamase as excreted by the host S. lividans ML1, has a ragged amino-terminus, indicating either the presence of a leader peptidase of poor specificity or the action of an amino-peptidase. The deduced primary structure has been confirmed by amino acid sequencing of a 10-residue stretch at the amino terminus of the mature protein and an 8-residue stretch containing the active-site serine. The S. cacaoiβ-lactamase is highly homologous with the class A β-lactamases of Streptomyces albus G and Staphylococcus aureus of known three-dimensional structure. Amino acid alignments show that the S. cacaoiβ-lactamase essentially differs from these two latter enzymes by short insertions and deletions that do not affect the spatial disposition of the secondary structures. [less ▲]

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See detailChromosome-encoded beta-lactamases of Citrobacter diversus. Interaction with beta-iodopenicillanate and labelling of the active site.
Amicosante, G; Oratore, A; Joris, Bernard ULiege et al

in Biochemical Journal (1988), 254(3), 891-3

Both forms of the chromosome-encoded beta-lactamase of Citrobacter diversus react with beta-iodopenicillanate at a rate characteristic of class A beta-lactamases. The active site of form I was labelled ... [more ▼]

Both forms of the chromosome-encoded beta-lactamase of Citrobacter diversus react with beta-iodopenicillanate at a rate characteristic of class A beta-lactamases. The active site of form I was labelled with the same reagent. The sequence of the peptide obtained after trypsin hydrolysis is identical with that of a peptide obtained in a similar manner from the chromosome-encoded beta-lactamase of Klebsiella pneumoniae. [less ▲]

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See detailPenicillin-recognizing enzymes
Frère, Jean-Marie ULiege; Joris, Bernard ULiege; Dideberg, Otto et al

in Biochemical Society Transactions (1988), 16(6), 934-938

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See detailBeta-Lactamases as the Main Resistance Factor to Penicillin-Related Antibiotics
Frère, Jean-Marie ULiege; Joris, Bernard ULiege

in Annales de Biologie Clinique (1988), 46(2), 151-6

The interplay between the three factors involved in the resistance of bacteria to beta-lactam antibiotics (sensitivity of target, synthesis of beta-lactamase, permeability barrier) is analysed and ... [more ▼]

The interplay between the three factors involved in the resistance of bacteria to beta-lactam antibiotics (sensitivity of target, synthesis of beta-lactamase, permeability barrier) is analysed and discussed on the basis of a simple kinetic model. The three factors do not act independently. In Gram-negative bacteria, the permeability barrier is only significant when the bacterial cell also produces a beta-lactamase. Special attention is devoted to cases where large periplasmic beta-lactamase concentrations prevail, a situation which has been observed in some clinical isolates. [less ▲]

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See detailBeta-Lactamase-induced resistance
Frère, Jean-Marie ULiege; Joris, Bernard ULiege

in Actor, Paul; Daneo-Moore, Lolita; Higgins, Michael, L. (Eds.) et al Antibiotic Inhibition of Bacterial Cell Surface Assembly and Function (1988)

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See detailThe importance of the negative charge of β-lactam compounds for the inactivation of the active-site serine DD-peptidase of Streptomyces R61
Varetto, Louis ULiege; Frère, Jean-Marie ULiege; Ghuysen, Jean-Marie ULiege

in FEBS Letters (1987), 225(1-2), 218-222

The interaction between the Streptomyces R61 penicillin-sensitive DD-peptidase and deacetyl-cephalosporin C or its lactone derivative has been studied at different pH values. The results show the ... [more ▼]

The interaction between the Streptomyces R61 penicillin-sensitive DD-peptidase and deacetyl-cephalosporin C or its lactone derivative has been studied at different pH values. The results show the importance of an enzyme group of pK approximately equal to 9 which might form an ion pair with the free carboxylate of the former compound. This electrostatic interaction is shown to contribute to the formation of the first, non-covalent enzyme-inactivator complex by a factor of at least 50. [less ▲]

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See detailCloning and amplified expression in Streptomyces lividans of the gene encoding the extracellular β-lactamase from Streptomyces cacaoi
Lenzini, Mauro V; Nojima, Shiego; Dusart, Jean et al

in Journal of General Microbiology (1987), 133(10), 2915-2920

A 19 kb SphI DNA fragment containing the gene for the extracellular active-site serine beta-lactamase of Streptomyces cacaoi KCC-SO352 was cloned in Streptomyces lividans TK24 using the high-copy-number ... [more ▼]

A 19 kb SphI DNA fragment containing the gene for the extracellular active-site serine beta-lactamase of Streptomyces cacaoi KCC-SO352 was cloned in Streptomyces lividans TK24 using the high-copy-number plasmid pIJ702 as vector. A 30-fold higher yield of beta-lactamase was obtained from S. lividans strain ML1, carrying the recombinant plasmid pDML51, than from S. cacaoi grown under optimal production conditions. In all respects (molecular mass, isoelectric point, kinetics of inhibition by beta-iodopenicillanate) the overproduced S. lividans ML1 beta-lactamase was identical to the original S. cacaoi enzyme. A considerable reduction of beta-lactamase production was caused by elimination of a 12.8 kb portion of the 19 kb DNA fragment by cleavage at an internal SphI site located more than 3 kb upstream of the beta-lactamase structural gene. The beta-lactamase gene was located within a 1.8 NcoI-BclI fragment but when this fragment was cloned in S. lividans pIJ702, the resulting strain produced hardly any more beta-lactamase than the original S. cacaoi. [less ▲]

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See detailNucleotide sequence of the gene encoding the Streptomyces albus G β-lactamase precursor
Dehottay, Philippe; Dusart, Jean; De Meester, Fabien et al

in European Journal of Biochemistry (1987), 166(2), 345-350

A 1400-base DNA fragment, which contains the gene encoding the extracellular active-site serine beta-lactamase of Streptomyces albus G previously cloned into Streptomyces lividans [Dehottay et al. (1986 ... [more ▼]

A 1400-base DNA fragment, which contains the gene encoding the extracellular active-site serine beta-lactamase of Streptomyces albus G previously cloned into Streptomyces lividans [Dehottay et al. (1986) Gene 42, 31-36], was sequenced. The gene codes for a 314-amino-acid precursor, the N-terminal region of which has the characteristics of a signal peptide. The beta-lactamase as excreted by the host strain S. lividans PD6 has a ragged N-terminus, indicating either the presence of a leader peptidase of poor specificity or the action of an aminopeptidase. The primary structure (as deduced from the nucleotide sequence) was confirmed by amino acid sequencing of a 16-residue stretch at the amino terminus of the protein, a 12-residue stretch containing the active-site serine [De Meester et al. (1987) Biochem. J. 244, 427-432] and a 23-residue stretch obtained by trypsin digestion of the protein. The beta-lactamase belongs to class A, has three half-cystine residues (one of which occurs on the amino side of the active-site serine) and is inactivated by thiol reagents. Putative ribosome binding site and terminator region were identified. [less ▲]

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See detailPrimary structure of the Streptomyces R61 extracellular DD-peptidase. 2. Amino acid sequence data
Joris, Bernard ULiege; Jacques, Philippe ULiege; Frère, Jean-Marie ULiege et al

in European Journal of Biochemistry (1987), 162(3), 519-524

In order to confirm the Streptomyces codon usage, the Streptomyces R61 DD-peptidase was fragmented by cyanogen bromide cleavage of the carboxymethylated protein, trypsin digestion of the carboxymethylated ... [more ▼]

In order to confirm the Streptomyces codon usage, the Streptomyces R61 DD-peptidase was fragmented by cyanogen bromide cleavage of the carboxymethylated protein, trypsin digestion of the carboxymethylated protein and trypsin digestion of the protein treated with beta-iodopenicillinate and endoxo-delta 4-tetrahydrophthalic acid. The isolated peptides, which altogether represented more than 50% of the polypeptide chain, were sequenced. The data thus obtained were in excellent agreement with the primary structure of the protein as deduced from the nucleotide sequence of the cloned gene. Though a weak acylating agent, beta-iodopenicillanate reacted selectively with the active site of the DD-peptidase and formed an adduct which mas much more stable than that formed with benzylpenicillin, thus facilitating the isolation and characterization of the active-site peptide. [less ▲]

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See detailThe pH dependence of the active-site serine DD-peptidase of Streptomyces R61
Varetto, Louis; Frère, Jean-Marie ULiege; Nguyen-Distèche, Martine ULiege et al

in European Journal of Biochemistry (1987), 162(3), 525-531

Titration of the active-site serine DD-peptidase of Streptomyces R61 shows that formation of acyl enzyme during hydrolysis of the substrate Ac2-L-Lys-D-Ala-D-Ala and enzyme inactivation by the beta-lactam ... [more ▼]

Titration of the active-site serine DD-peptidase of Streptomyces R61 shows that formation of acyl enzyme during hydrolysis of the substrate Ac2-L-Lys-D-Ala-D-Ala and enzyme inactivation by the beta-lactam compounds benzylpenicillin, N-acetylampicillin and ampicillin relies on the acidic form of an enzyme's group of pK approximately equal to 9.5. It is proposed that protonation of a lysine epsilon-amino group facilitates initial binding by charge pairing with the free carboxylate of the substrate and the beta-lactam molecules. Lowering the pH from 7 to 5 has no effect on the second-order rate constant of enzyme acylation by benzylpenicillin and N-acetylampicillin but results in a decreased rate constant of acylation by ampicillin and Ac2-L-Lys-D-Ala-D-Ala. Protonation of the side-chain amino group of ampicillin and a decreased efficacy of the initial binding of the peptide to the enzyme seem to be responsible for the observed effects. Whatever the molecule bound to the enzyme, there is no sign for the active involvement of an enzyme's histidine residue of pK 6.5-7.0 in the hydrolysis pathway. [less ▲]

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See detailPrimary structure of the Streptomyces R61 extracellular DD‐peptidase
Joris, Bernard ULiege; Jacques, Philippe ULiege; Frère, Jean-Marie ULiege et al

in European Journal of Biochemistry (1987), 162(3), 519-524

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See detailThe crystal structure of the β-lactamase of Streptomyces albus G at 0.3 nm resolution
Dideberg, Otto; Charlier, Paulette ULiege; Wery, Jean-Paul et al

in Biochemical Journal (1987), 245(3), 911-913

The crystal structure of the beta-lactamase of Streptomyces albus G has been solved at 0.3 nm resolution by X-ray-diffraction methods. The enzyme is a typical two-domain protein. One domain consists of ... [more ▼]

The crystal structure of the beta-lactamase of Streptomyces albus G has been solved at 0.3 nm resolution by X-ray-diffraction methods. The enzyme is a typical two-domain protein. One domain consists of five alpha-helices, and the other is five-stranded beta-sheet with alpha-helices on both sides of the sheet. The active-site serine residue (Ser-48) is within a cleft located between the two domains. [less ▲]

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See detailThe active sites of the β-lactamases of Streptomyces cacaoi and Streptomyces albus G
Demeester, Fabien; Joris, Bernard ULiege; Lenzini, Mauro V. et al

in Biochemical Journal (1987), 244(2), 427-432

The active-site serine of the extracellular beta-lactamases of Streptomyces cacaoi and Streptomyces albus G has been labelled with beta-iodopenicillanate. The determination of the sequence of the labelled ... [more ▼]

The active-site serine of the extracellular beta-lactamases of Streptomyces cacaoi and Streptomyces albus G has been labelled with beta-iodopenicillanate. The determination of the sequence of the labelled peptides obtained after trypsin digestion of the denatured proteins indicate both enzymes to be class A beta-lactamases. Surprisingly the two Streptomyces enzymes do not appear to be especially homologous, and none of them exhibited a high degree of homology with the Streptomyces R61 DD-peptidase. Our data confirm that, as a family of homologous enzymes, class A is rather heterogeneous, with only a small number of conserved residues in all members of the class. [less ▲]

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See detailThe K1 beta-lactamase of Klebsiella pneumoniae.
Joris, Bernard ULiege; De Meester, F; Galleni, Moreno ULiege et al

in Biochemical Journal (1987), 243(2), 561-7

beta-Lactamase K1 was purified from Klebsiella pneumoniae SC10436. It is very similar to the enzyme produced by Klebsiella aerogenes 1082E and described by Emanuel, Gagnon & Waley [Biochem. J. (1986) 234 ... [more ▼]

beta-Lactamase K1 was purified from Klebsiella pneumoniae SC10436. It is very similar to the enzyme produced by Klebsiella aerogenes 1082E and described by Emanuel, Gagnon & Waley [Biochem. J. (1986) 234, 343-347]. An active-site peptide was isolated after labelling of the enzyme with tritiated beta-iodopenicillanate. A cysteine residue was found just before the active-site serine residue. This result could explain the properties of the enzyme after modification by thiol-blocking reagents. The sequence of the active-site peptide clearly established the enzyme as a class A beta-lactamase. [less ▲]

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See detailAutomated analysis of enzyme inactivation phenomena. Application to beta-lactamases and DD-peptidases.
De Meester, Fabien; Joris, Bernard ULiege; Reckinger, Georges et al

in Biochemical Pharmacology (1987), 36

In the presence of a reporter substrate, the progressive inactivation of an enzyme was easily studied by directly transmitting absorbance readings to a microcomputer. Pseudo-first order rate constants as ... [more ▼]

In the presence of a reporter substrate, the progressive inactivation of an enzyme was easily studied by directly transmitting absorbance readings to a microcomputer. Pseudo-first order rate constants as high as 0.3 sec-1 were rapidly and accurately measured. When utilization of the reporter substrate did not exceed 10%, the rate of the reaction (vt) could be considered as proportional to the active enzyme concentration at any time during the analysis and the decrease of vt was first order with time. This simple method was used to follow the inactivation of beta-lactamases (EC 3.5.2.6) by various physical and chemical agents. When a large proportion (30-80%) of reporter substrate was destroyed, a correction was introduced to account for the corresponding decrease of its rate of utilization. This enabled experiments to be performed with a DD-peptidase and a substrate exhibiting a low delta epsilon upon hydrolysis. For the first time, the inactivation of a penicillin-sensitive enzyme by a beta-lactam could be continuously and directly observed. Finally, the method was extended to the study of hysteresis phenomena. [less ▲]

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See detailPrimary structure of the Streptomyces R61 extracellular DD-peptidase. 1. Cloning into Streptomyces lividans and nucleotide sequence of the gene
Duez, Colette ULiege; Fraipont, Claudine ULiege; Joris, Bernard ULiege et al

in European Journal of Biochemistry (1987), 162

An 11450-base DNA fragment containing the gene for the extracellular active-site serine DD-peptidase of Streptomyces R61 was cloned in Streptomyces lividans using the high-copy-number plasmid pIJ702 as ... [more ▼]

An 11450-base DNA fragment containing the gene for the extracellular active-site serine DD-peptidase of Streptomyces R61 was cloned in Streptomyces lividans using the high-copy-number plasmid pIJ702 as vector. Amplified expression of the excreted enzyme was observed. Producing clones were identified with the help of a specific antiserum directed against the pure DD-peptidase. The coding sequence of the gene was then located by hybridization with a specific nucleotide probe and sub-fragments were obtained from which the nucleotide sequence of the structural gene and the putative promoter and terminator regions were determined. The sequence suggests that the gene codes for a 406-amino-acid protein precursor. When compared with the excreted, mature DD-peptidase, this precursor possesses a cleavable 31-amino-acid N-terminal extension which has the characteristics of a signal peptide, and a cleavable 26-amino-acid C-terminal extension. On the basis of the data of Joris et al. (following paper in this journal), the open reading frame coding for the synthesis of the DD-peptidase was established. Comparison of the primary structure of the Streptomyces R61 DD-peptidase with those of several active-site serine β-lactamases and penicillin-binding proteins of Escherichia coli shows homology in those sequences that comprise the active-site serine residue. When the comparison is broadened to the complete amino acid sequences, significant homology is observed only for the pair Streptomyces R61 DD-peptidase/Escherichia coli ampC β-lactamase (class C). Since the Streptomyces R61 DD-peptidase and β-lactamases of class A have very similar three-dimensional structures [Kelly et al. (1986) Science (Wash. DC) 231, 1429–1431; Samraoui et al. (1986) Nature (Lond.) 320, 378–380], it is concluded that these tertiary features are probably also shared by the β-lactamases of class C, i.e. that the Streptomyces R61 DD-peptidase and the β-lactamases of classes A and C are related in an evolutionary sense. [less ▲]

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See detailActive-site-serine D-alanyl-D-alanine-cleaving-peptidase-catalysed acyl-transfer reactions. Procedures for studying the penicillin-binding proteins of bacterial plasma membranes
Ghuysen, Jean-Marie ULiege; Frère, Jean-Marie ULiege; Leyh-Bouille, Mélina et al

in Biochemical Journal (1986), 235(1), 159-165

Under certain conditions, the values of the parameters that govern the interactions between the active-site-serine D-alanyl-D-alanine-cleaving peptidases and both carbonyl-donor substrates and beta-lactam ... [more ▼]

Under certain conditions, the values of the parameters that govern the interactions between the active-site-serine D-alanyl-D-alanine-cleaving peptidases and both carbonyl-donor substrates and beta-lactam suicide substrates can be determined on the basis of the amounts of (serine ester-linked) acyl-protein formed during the reactions. Expressing the 'affinity' of a beta-lactam compound for a DD-peptidase in terms of second-order rate constant of enzyme acylation and first-order rate constant of acyl-enzyme breakdown rests upon specific features of the interaction (at a given temperature) and permits study of structure-activity relationships, analysis of the mechanism of intrinsic resistance and use of a 'specificity index' to define the capacity of a beta-lactam compound of discriminating between various sensitive enzymes. From knowledge of the first-order rate constant of acyl-enzyme breakdown and the given time of incubation, the beta-lactam compound concentrations that are necessary to achieve given extents of DD-peptidase inactivation can be converted into the second-order rate constant of enzyme acylation. The principles thus developed can be applied to the study of the multiple penicillin-binding proteins that occur in the plasma membranes of bacteria. [less ▲]

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