Frère, Nguyen-Distèche, Coyette, Joris (1992) Mode of action: Interaction with the penicillin binding proteins. The Chemistry of β-lactams , MI Page, Blackie Academic & Professional, Glasgow, an imprint of Chapman & Hall; 148-195.
Nikaido, Normark (1987) Sensitivity of Escherichia coli to various β-lactams is determined by the interplay of outer membrane permeability and degradation by periplasmic β-lactamase: A quantitative predictive treatment. Mol Microbiol 1:29-36.
Waley (1987) An explicit model for bacterial resistance: Application to beta-lactam antibiotics. Microbiol Sci 4:143-146.
Frère, Joris, Crine, Martin (1989) Quantitative relationship between sensitivity to β-lactam antibiotics and β-lactamase production in Gramnegative bacteriaâII Non-steady-state treatment and progress curves. Biochemical Pharmacology 38:1427-1433.
Waley (1992) β-lactamase: Mechanism of action. The Chemistry of β-lactams , MI Page, Blackie Academic & Professional, Glasgow, an imprint of Chapman & Hall; 198-228.
Coyette, Nguyen-Distèche, Lamotte-Brasseur, Joris, Fonzé, Frère (1994) Molecular adaptations in resistance to penicillins and other β-lactam antibiotics. Adv Comp Environ Physiol 20:233-267.
Payne (1993) Metallo-β-lactamases—a new therapeutic challenge. J Med Microbiol 39:93-99.
Christensen, Martin, Waley (1990) β-Lactamases as fully efficient enzymes. Determination of all the rate constants in the acyl-enzyme mechanism. Biochem J 266:853-861.
Hechler, Van Den Weghe, Martin, Frère (1989) Overproduced β-lactamase and the outer membrane barrier as resistance factors in Serratia marcescens highly resistant to β-lactamase stable β-lactam antibiotics. J Gen Microbiol 135:1275-1290.
Joris, Ghuysen, Dive, Renard, Dideberg, Charlier, Frère, Kelly, Boyington, Moews, Knox (1988) The active-site-serine penicillin-recognizing enzymes as members of the Streptomyces R61 dd-peptidase family. Biochem J 250:313-324.
Herzberg (1991) Refined crystal structure of β-lactamase from Staphylococcus aureus PC1 at 2.0 Å resolution. J Mol Biol 217:701-719.
Moews, Knox, Dideberg, Charlier, Frère (1990) β-Lactamase of Bacilus licheniformis 749/C at 2 Å resolution. Proteins Struct Funct Genet 7:156-171.
Jelsch, Lenfant, Masson, Samama (1992) β-Lactamase TEM1 of E. coli. Crystal structure determination at 2.5 Å resolution. FEBS Lett 299:135-142.
Oefner, D'Arcy, Daly, Gubernator, Charnas, Heinze, Hubschwerlen, Winkler (1990) Refined crystal structure of β-lactamase from Citrobacter freundii indicates a mechanism for β-lactam hydrolysis. Nature 343:284-288.
Lobkovsky, Moews, Liu, Zhao, Frère, Knox (1994) Evolution of an enzyme activity Crystallographic structure at 2-Ã resolution of cephalosporinase from the amp C gene of Enterobacter cloacae P99 and comparison with a class A penicillinase. Proceedings of the National Academy of Sciences , 2nd edn; 90:11257-11261.
Joris, Ledent, Dideberg, Fonzé, Lamotte-Brasseur, Kelly, Ghuysen, Frère (1991) Comparison of the sequences of class-A β-lactamases and of the secondary structure elements of penicillin-recognizing proteins. Antimicrob Agents Chemother 35:2294-2301.
Sigal, Harwood, Arentzen (1982) Thiol-β-lactamase: Replacement of the active-site serine of RTEM β-lactamase by a cysteine residue. Proc Natl Acad Sci USA , 2nd edn; 79:7157-7160.
Jacob, Joris, Frère (1991) Active-site serine mutants of the Streptomyces albus G β-lactamase. Biochem J 277:647-652.
Kelly, Knox, Zhao, Frère, Ghuysen (1989) Crystallographic mapping of β-lactams bound to a d-alanyl-d-alanine peptidase target enzyme. J Mol Biol 209:281-295.
Fersht, Blow, Fastrez (1973) Leaving group specificity in the chymotrypsin-catalysed hydrolysis of peptides. A stereochemical interpretation. Biochemistry 12:2035-2041.
Brady, Brzozowski, Derewenda, Dodson, Dodson, Tolley, Turkenburg, Christiansen, Huge-Jensen, Norskov, Thim, Menge (1990) A serine protease triad forms the catalytic centre of a triacylglycerol lipase. Nature 343:767-770.
Ambler, Coulson, Frère, Ghuysen, Joris, Levesque, Tiraby, Waley (1991) A standard numbering scheme for the class A β-lactamases. Biochem J 276:269-270.
Lamotte-Brasseur, Dive, Dideberg, Charlier, Frère, Ghuysen (1991) Mechanism of acyl transfer by the class A serine β-lactamase of Streptomyces albus G. Biochem J 279:213-221.
Herzberg, Kapadia, Blanco, Smith, Coulson (1991) Structural basis for the inactivation of the P54 mutant of β-lactamase from Staphylococcus aureus PC1. Biochemistry 30:9503-9509.
Gibson, Christensen, Waley (1990) Site-directed mutagenesis of β-lactamase I. Single and double mutants of Glu-166 and Lys-73. Biochem J 272:613-619.
Matagne, Lamotte-Brasseur, Dive, Knox, Frère (1993) Interactions between active-site serine β-lactamases and compounds bearing a methoxy side chain on the face of the β-lactam ring: Kinetic and molecular modeling studies. Biochem J 293:607-611.
Rahil, Pratt (1994) Characterization of covalently bound enzyme inhibitors as transition-state analogs by protein stability measurements Phosphonate monoester inhibitors of a β-lactamase. Biochemistry 33:116-125.
Delaire, Lenfant, Labia, Masson (1991) Site-directed mutagenesis on TEM-1 beta-lactamase. Role of Glu 166 in catalysis and substrate binding. Protein Eng 4:805-810.
Leung, Robinson, Aplin, Waley (1994) Site-directed mutagenesis of β-lactamase I: Role of Glu 166. Biochem J 299:671-678.
Escobar, Tan, Fink (1991) Site-directed mutagenesis of β-lactamase leading to accumulation of a catalytic intermediate. Biochemistry 30:10783-10787.
Strynadka, Adachi, Jensen, Johns, Sielecki, Betzel, Sutoh, James (1992) Molecular structure of the acyl-enzyme intermediate in β-lactam hydrolysis at 1.7 Å resolution. Nature 359:700-705.
Lobkovsky, Billings, Moews, Rahil, Pratt, Knox (1994) Crystallographic structure of a phosphonate derivative of the Enterobacter cloacae P99 cephalosporinase: Mechanistic interpretation of a β-lactamase transition state analog. Biochemistry 33:6762-6772.
Dubus, Normark, Kania, Page (1994) The role of tyrosine 150 in catalysis of β-lactam hydrolysis by AmpC β-lactamase from Escherichia coli investigated by site-directed mutagenesis. Biochemistry 33:8577-8586.
Monnaie, Dubus, Cooke, Marchand-Brynaert, Normark, Frère (1994) Role of residue Lys 315 in the mechanism of action of the Enterobacter cloacae 908R β-lactamase. Biochemistry 33:5193-5201.
Monnaie, Dubus, Frère (1994) The role of lysine-67 in class C β-lactamase is mainly electrostatic. Biochem J 302:1-4.
Galleni, Amicosante, Frère (1988) A survey of the kinetic parameters of class C β-lactamases. II. Cephalosporins and other β-lactam compounds. Biochem J 255:123-129.
Ledent, Raquet, Joris, Van Beeumen, Frere (1993) A comparative study of class D β-lactamases. Biochem J 292:555-562.
Pratt, Govardhan (1984) β-Lactamase-catalysed hydrolysis of acyclic depsipeptides and acyl transfer to specific amino acid acceptors. Proc Natl Acad Sci USA , 2nd edn; 81:1302-1306.
Adam, Damblon, Plaitin, Christiaens, Frère (1990) Chromogenic depsipeptide substrates for β-lactamases and penicillin-sensitive dd-peptidases. Biochem J 270:525-529.
Murphy, Pratt (1991) N-(Phenylacetyl)glycyl-D-aziridine-2-carboxylate, an acyclic amide substrate of β-lactamases. Importance of the shape of the substrate in β-lactamase evolution. Biochemistry 30:3640-3649.
Amicosante, Franceschini, Segatore, Oratore, Fattorini, Orefici, Van Beeumen, Frère (1990) Characterization of a β-lactamase produced in Mycobacterium fortuitum D316. Biochem J 271:729-734.
Delaire, Labia, Samama, Masson (1992) Site-directed mutagenesis at the active site of Escherichian coli TEM-1 β-lactamase. Suicide inhibitor-resistant mutants reveal the role of arginine 244 and methionine 69 in catalysis. J Biol Chem 267:20600-20606.
Imtiaz, Billings, Knox, Manavathu, Lerner, Mobashery (1993) Inactivation of class A β-lactamases by clavulanic acid: The role of arginine-244 in a proposed nonconcerted sequence of events. J Am Chem Soc 115:4435-4442.
Galleni, Fransceschini, Quinting, Fattorini, Orefici, Oratore, Frère, Amicosante (1994) Use of the chromosomal class A β-lactamase of Mycobacterium fortuitum to study potentially poor substrates and inhibitory β-lactam compounds. Antimicrob Agents Chemother 38:1608-1614.
