Frère, Jean-Marie ; Université de Liège - ULiège > Centre d'ingénierie des protéines
Joris, Bernard ; Université de Liège - ULiège > Département des sciences de la vie > Physiologie et génétique bactériennes - Centre d'ingénierie des protéines
Language :
English
Title :
Penicillin-sensitive enzymes in peptidoglycan biosynthesis
Ghuysen J.M., Frère Leyh-Bouille J.M., Coyette M., Dusart J.J., Nguyen-Distèche M. (1979) Use of model enzymes in the determination of the mode of action of penicillins and A'-cephalosporins. Annu. Rev. Biochem. 48:73.
Ghuysen J.M., Frère J., Leyh-Bouille M., Dideberg M., Lamotte-Brasseur O., Perkins J.H.R., De Coen J.L. (1981) Penicillins and Δ-cephalosporins as inhibitors and mechanism-based inactivators of D-alanyl-D-Ala peptidases chap. 3. Topics in Molecular Pharmacology, Eds. A.S.V. Burgen, G.C.K. Roberts., Elsevier/North-Holland; .
Waxman D.J., Strominger J.L. (1983) Penicillin-binding proteins and the mechanism of action of β-lactam antibiotics, Annu. Rev. Biochem. 52:825.
Frère J., Duez M., Dusart C., Coyette J., Leyh-Bouille J., Ghuysen M., Dideberg J.M.O., Knox J.R. (1980) Mode of action of β-lactam antibiotics at the molecular level chap. 12. Enzyme Inhibitors as Drugs, Ed. M. Sandler., Macmillan, New York; .
Penicillin fifty years after Fleming Phil. Trans. R. Soc. Lond. 1980, B289:167.
The Chemistry and Biology of β-Lactam Antibiotics , R.B. Morin, M. Gorman, Academic Press, New York; 1982, 1-3.
Hakenbeck R., Höltje J.V. The Target of Penicillin, Ed. H. Labischinski., W. De Gruyter, New York; 1983.
β-Lactam Antibiotics, Japan Scientific Societies Press, S. Mitsuhashi, Tokyo/Springer-Verlag, Berlin; 1981.
Recent Advances in the Chemistry of β-Lactam Antibiotics, Spec. Publ. No. 38, The Chemical Society, G.I. Gregory, Burlington House, London; 1980.
Ghuysen J.M. Antibiotics and peptidoglycan metabolism, in Topics in Antibiotic Chemistry , Ed. P.G. Sammes., Ellis Horwood, Chichester; 1980, 5:15.
Ghuysen J.M. The Bacterial DD-Carboxypeptidase-Transpeptidase System, University of Tokyo Press, Tokyo; 1977.
Park J.T., Strominger J.L. (1957) Mode of action of penicillin. Biochemical basis for the mechanism of action of penicillin and for its selective toxicity. Science 125:99.
Tomasz A. Murein hydrolases. Enzymes in search of a physiological function, in The Target of Penicillin , Eds. R. Hakenbeck, J.V. Höltje, H. Labischinski., W. de Gruyter, New York; 1983, 155.
Martin H.H., Gmeiner J. (1979) Modification of peptidoglycan structure by penicillin action on cell walls of. Proteus mirabilis, Eur. J. Biochem. 95:487.
Blundell J.K., Perkins H.R. (1981) Effects of β-lactam antibiotics on peptidoglycan synthesis in growing Neisseria gonorrhoeae, including changes in the degree of O-acetylation. J. Bacteriol. 147:633.
Lear A.L., Perkins H.R. (1983) Degrees of O-acetylation and cross-linking of the peptidoglycan of Neisseria gonorrhoeae during growth. J. Gen. Microbiol. 129:885.
Dougherty T.J. (1983) Peptidoglycan biosynthesis in Neisseria gonorrhoeae strains sensitive and intrinsically resistant to β-lactam antibiotics. J. Bacteriol. 153:429.
Gutmann L., Tomasz A. (1982) Penicillin-resistant and penicillin-tolerant mutants of group A Streptococci. Antimicrob. Agents Chemother. 22:128.
Shockman Daneo-Moore G.D., McDowell L.T.D., Wong W. The relationship between inhibition of cell wall synthesis and bacterial lethality, in The Chemistry and Biology of β-Lactam Antibiotics , Eds. R.B. Morin, M. Gorman., Academic Press, New York; 1982, 3:303.
Rolinson G.N. (1971) Bacterial resistance to penicillins and cephalosporins. Proc. R. Soc. Ser. B 179:403.
Ghuysen J.M., Shockman G.D. Biosynthesis of peptidoglycan, in Bacterial Membranes and Wall , Ed. L. Leive., Marcel Dekker, New York; 1973, 37.
Shockman G.D., Barrett J.F. (1983) Structure, function and assembly of cell walls of gram-positive bacteria. Annu. Rev. Microbiol. 37:501.
Tipper D.J., Wright A. The structure and biosynthesis of bacterial cell walls, in The Bacteria , Eds. J.R. Sokatch, L.N. Ornstein., Academic Press, New York; 1979, 7:291.
Mirelman D. Biosynthesis and assembly of cell wall peptidoglycan, in Bacterial Outer Membrane , Ed. M. Inouye., John Wiley & Sons, New York; 1980, 115.
Frère J.M. (1977) Mechanism of action of β-lactam antibiotics at the moleculer level. Biochem. Pharmacol. 26:2203.
Ghuysen J.M. (1968) Use of bacteriolytic enzymes in determination of wall structure and their role in cell metabolism. Bacteriol. Rev. 32:425.
Waxman D.J., Strominger J.L. (1982) β-Lactam antibiotic: biochemical mode of action. The Chemistry and Biology of β-Lactam Antibiotics , Ed. R.B. Morin., Academic Press, New York; 3:209.
Ward B.J., Perkins H.R. (1973) The direction of glycan synthesis in a bacterial peptidoglycan. Biochem. J. 135:721.
Ward B.J., Perkins H.R. (1974) Peptidoglycan biosynthesis by preparations from Bacillus licheniformis: crosslinking of newly synthesized chains to preformed cell wall. Biochem. J. 139:781.
Frère J., Ghuysen M., Zeiger J.M.A.R., Perkins H.R. (1976) The direction of peptide trimer synthesis from the donor-acceptor substrate N*-(acetyl)-N'-(glycyl)-L-lysyl-D-alanyl-D-alanine by the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R61. FEBS Lett. 63:112.
Oldmixon E.H., Dezélée P., Ziskin M.C., Shockman G.D. (1976) Monomer addition as a mechanism of forming peptide cross-links in the cell-wall peptidoglycan of Streptococcus faecalis ATCC 9790. Eur. J. Biochem. 68:271.
Martin H.H. (1964) Composition of the mucopolymer in cell walls of the unstable L-form of. Proteus mirabilis, J. Gen. Microbiol. 36:441.
Katz W., Martin H.H. (1970) Peptide crosslinkage in cell-wall murein of Proteus mirabilis and its penicillin-induced unstable L-form. Biochem. Biophys. Res. Commun. 39:744.
Wise E.M., Park J.T. (1965) Penicillin: its basic site of action as an inhibitor of a peptide cross-linking reaction in cell-wall mucopeptide synthesis. Proc. Natl. Acad. Sci. U.S.A. 54:75.
Tipper D.J., Strominger J.L. (1965) Mechanism of action of penicillins: a proposal based on their structural similarity to acyl-D-alanyl-D-alanine. Proc. Natl. Acad. Sci. U.S.A. 54:1133.
Izaki Matsuhashi K.M., Strominger J.L. (1966) Glycopeptide transpeptidase and D-alanine carboxypeptidase: penicillin-sensitive enzymatic reactions. Proc. Natl. Acad. Sci. U.S.A. 55:656.
Araki Shimada V.A.T., Ito E. (1966) Effect of penicillin on cell-wall mucopeptide synthesis in an Escherichia coli particulate system. Biochem. Biophys. Res. Commun. 23:518.
Mirelman Bracha D.R., Sharon N. (1974) Penicillin-induced secretion of a soluble, uncrosslinked peptidoglycan by Micrococcus luteus cells. Biochemistry 13:5045.
Tynecka Z., Ward B.J. (1975) Peptidoglycan synthesis in Bacillus licheniformis. The inhibition of crosslinking by benzylpenicillin and cephaloridine in vivo accompanied by the formation of soluble peptidoglycan. Biochem. J. 146:253.
Keglevic Lodesic D., Hadzija B., Tomasic O., Valinger J.Z., Pokorny M. (1974) Isolation and study of the composition of a peptidoglycan complex excreted by the biotin-requiring mutant of Brevibacterium divaricatum NRRL-2311 in the presence of penicillin. Eur. J. Biochem. 42:389.
Keglevic Lodesic D., Tomasic B., Valinger J.Z., Naumski R. (1979) Isolation procedure and properties of monomer unit from lysozyme digest of peptidoglycan complex excreted into the medium by penicillin-treated Brevibacterium divaricatum mutant. Biochim. Biophys. Acta 585:273.
Waxman Yu D.J.W., Strominger J.L. (1980) Linear, uncross-linked peptidoglycan secreted by penicillin-treated Bacillus subtilis. Isolation and characterization as a substrate for penicillin-sensitive D-alanine carboxypeptidases. J. Biol. Chem. 255:11577.
Bogdanovsky Bricas D.E., Dezélée P. (1969) Sur l'identité de la mucoendopeptidase et de la carboxypeptidase I d' Escherichia coli, enzymes hydrolysant des liaisons de configuration DD et inhibees par la penicilline. C.R. Acad. Sci. Paris Ser. D 269:390.
Coyette Perkins J., Polacheck H.R., Shockman I.G.D., Ghuysen J.M. (1974) Membrane-bound DD-carboxypeptidase and LD-transpeptidase of Streptococcus faecalis ATCC 9790. Eur. J. Biochem. 44:459.
Chapman S.J., Perkins H.R. (1983) Peptidoglycan-degrading enzymes in ether-treated cells of. Neisseria gonorrhoeae, J. Gen. Microbiol. 129:877.
Blumberg P.M., Strominger J.L. (1971) Inactivation of D-alanine carboxypeptidase by penicillins and cephalosporins is not lethal in. Bacillus subtilis, Proc. Natl. Acad. Sci. U.S.A. 68:2814.
Hammes W.P., Kandler O. (1976) Biosynthesis of peptidoglycan in Gaffkya homari. The incorporation of peptidoglycan into the cell wall and the direction of transpeptidation. Eur. J. Biochem. 70:97.
Hammes W.P. (1976) Biosynthesis of peptidoglycan in Gaffkya homari. The mode of action of penicillin G and mecillinam. Eur. J. Biochem. 70:107.
Ghuysen Leyh-Bouille J.M., Bonaly M., Nieto R., Perkins M., Schleifer H.R.K.H., Kandler O. (1970) Isolation of DD-carboxypeptidase from Streptomyces albus G culture filtrates. Biochemistry 9:2955.
Leyh-Bouille Coyette M., Ghuysen J., Idczak J.M., Perkins J.H.R., Nieto M. (1971) Penicillin-sensitive DD-carboxypeptidase from Streptomyces strain R61. Biochemistry 10:2163.
Leyh-Bouille Nakel M., Frère M., Johnson J.M., Ghuysen K., Nieto J.M.M., Perkins H.R. (1972) Penicillin-sensitive DD-carboxypeptidases from Streptomyces strains R39 and Kll. Biochemistry 11:1290.
Pollock Ghuysen J.J., Linder J.M., Salton R., Perkins M.R.J., Nieto H.R., Leyh-Bouille M.M., Frère J.M., Johnson K. (1972) Transpeptidase activity of Streptomyces D-alanyl-D-carboxypeptidases. Proc. Natl. Acad. Sci. U.S.A. 69:662.
Knox DeLucia J.R., Murthy M.L., Kelly N.S., Moews J.A.I.C., Frère J.M., Ghuysen J.M. (1979) Crystallographic data for a penicillin receptor: exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R61. J. Mol. Biol. 127:217.
Dideberg O., Frère J.M., Ghuysen J.M. (1979) Crystallographic data for the DD-carboxypeptidase-endopeptidase of low penicillin sensitivity excreted by Streptomyces albus G. J. Mol. Biol. 129:677.
Charlier P., Dideberg O., personal communication; 1983.
Joris VanBeeumen B., Casagrande J., Gerday F.C., Frère J.M., Ghuysen J.M. (1983) The complete amino acid sequence of the Zn-containing D-alanyl-D-alanine-cleaving carboxypeptidase of Streptomyces albus G. Eur. J. Biochem. 130:53.
Rasmussen J.R., Strominger J.L. (1978) Utilization of a depsipeptide substrate for trapping acylenzyme intermediates of penicillin-sensitive D-alanine carboxypeptidases. Proc. Natl. Acad. Sci. U.S.A. 75:84.
Ghuysen Bricas J.M., Lache E.M., Leyh-Bouille M. (1968) Structure of the cell walls of Micrococcus lysodeikticus. III. Isolation of a new peptide dimer, N°-[L-alanyl-γ-(α-D-glutamyl-glycine)]-L-lysyl-D-alanyl-N°-[L-alanyl-γ-(α-D-glutamyl-glycine)]-L-lysyl-D-alanine. Biochemistry 7:1450.
Frère J., Leyh-Bouille M., Ghuysen M., Nieto J.M.M., Perkins H.R. (1976) Exocellular DD-carboxypeptidases-transpeptidases from. Streptomyces, Methods Enzymol. 45:610.
De Coen Lamotte-Brasseur J.L., Ghuysen J.J.M., Frère J.M., Perkins H.R. (1981) Conformational analysis of peptide substrates and inhibitors of the Zn G and serine R61 D-alanyl-D-alanine peptidases. Eur. J. Biochem. 121:221.
Frère J., Ghuysen M., Perkins J.M.H.R., Nieto M. (1973) Molecular weight and amino acid composition of the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R61. Biochem. J. 135:463.
Frère J., Moreno M., Ghuysen R., Perkins J.M., Dierickx H.R.L., Delcambe L. (1974) Molecular weight, amino acid composition and physicochemical properties of the exocellular DD-carboxy-peptidase-transpeptidase of Streptomyces R39. Biochem. J. 143:233.
Perkins Nieto H.R., Frère M., Leyh-Bouille J.M.M., Ghuysen J.M. (1973) Streptomyces DD-carboxypeptidases as transpeptidases. The specificity for amino compounds acting as carboxyl acceptors. Biochem. J. 131:707.
Frère J., Ghuysen M., Perkins J.M.H.R., Nieto M. (1973) Kinetics of concomitant transfer and hydrolysis reactions catalysed by the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R61. Biochem. J. 135:483.
Ghuysen Leyh-Bouille J.M., Campbell M., Moreno J.N., Frère R., Duez J.M., Nieto C.M., Perkins H.R. (1973) Structure of the wall peptidoglycan of Streptomyces R39 and the specificity profile of its exocellular DD-carboxypeptidase-transpeptidase for peptide acceptors. Biochemistry 12:1243.
Leyh-Bouille Ghuysen M., Bonaly J.M., Nieto R., Perkins M., Schleifer H.R.K.H., Kandler O. (1970) Substrate requirements of the Streptomyces albus G DD-carboxypeptidase. Biochemistry 9:2961.
Ghuysen Reynolds J.M., Perkins P.E.I.R., Frère J.M., Moreno R. (1974) Effects of donor and acceptor peptides on concomitant hydrolysis and transfer reactions catalyzed by the exocellular DD-carboxypeptidase-transpeptidase from. Streptomyces , Biochemistry, 13, 2539; R39.
Zeiger A.R., Frère Ghuysen J.M.J.M., Perkins H.R. (1975) A donor-acceptor substrate of the exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R61. FEBS Lett. 52:221.
Frère J.M. (1973) Enzymic mechanisms involving concomitant transfer and hydrolysis reactions. Biochem. J. 135:469.
Yocum Amanuma R.R., O'Brien H., Waxman T.A.D.J., Strominger J.L. (1982) Penicillin is an active-site inhibitor for four genera of bacteria. J. Bacteriol. 149:1150.
Frère J.M., unpublished results; 1983.
Dusart Marquet J., Ghuysen A.J.M., Frère J.M., Leyh-Bouille R., Johnson M., Lucchi K., Perkins C.H.R., Nieto M. (1973) DD-carboxypeptidase-transpeptidase and killing site of β-lactam antibiotics in Streptomyces strains R39, R61 and K11. Antimicrob. Agents Chemother. 3:181.
Rogers H.J. (1967) The inhibition of mucopeptide synthesis by benzylpenicillin in relation to irreversible fixation of the antibiotic by staphylococci. Biochem. J. 103:90.
Blumberg P.M., Strominger J.L. (1974) Interaction of penicillin with the bacterial cell: penicillin-binding proteins and penicillin-sensitive enzymes. Bacteriol. Rev. 38:291.
Cooper P.D. (1956) Site of action of radiopenicillin. Bacteriol. Rev. 20:28.
Izaki K., Strominger J.L. (1968) Biosynthesis of the peptidoglycan of bacterial cell walls. XIV. Purification and properties of two D-alanine carboxypeptidases from. Escherichia coli, J. Biol. Chem. 243:3193.
Yocum Blumberg R.R.P.M., Strominger J.L. (1974) Purification and characterization of the thermophilic D-alanine carboxypeptidase from membranes of. Bacillus stearothermophilus, J. Biol. Chem. 249:4863.
Umbreit J.N., Strominger J.L. (1973) D-alanine carboxypeptidase from Bacillus subtilis membranes. II. Interaction with penicillins and cephalosporins. J. Biol. Chem. 248:6767.
Martin Maskos H.H.C., Burger R. (1975) D-Alanyl-D-alanine carboxypeptidase in the bacterial form and L-form of. Proteus mirabilis, Eur. J. Biochem. 55:465.
Martin Schilf H.H.W., Maskos C. (1976) Purification of the membrane-bound DD-carboxypeptidase of the unstable spheroplast L-form of Proteus mirabilis by affinity chromatography. Non-competitive inhibition of the enzyme by penicillins and low stability of the enzyme-inhibitor complex. Eur. J. Biochem. 71:585.
Barnett H.J. (1973) D-Alanine carboxypeptidases of Bacillus stearothermophilus: solubilisation of particulate enzymes and mechanism of action of penicillin. Biochim. Biophys. Acta 304:332.
Strominger Willoughby J.L., Kamiryo E., Blumberg T.P.M., Yocum R.R. (1974) Penicillin-sensitive enzymes and penicillin-binding components in bacterial cells, Ann. N.Y. Acad. Sci. 235:210.
Frère J., Leyh-Bouille M., Ghuysen M.J.M., Perkins H.R. (1974) Interaction between β-lactam antibiotics and exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R61. Eur. J. Biochem. 50:203.
Nieto Perkins M.H.R., Frère J.M., Ghuysen J.M. (1973) Fluorescence and circular dichroism studies on the Streptomyces R61 DD-carboxypeptidase-transpeptidase. Penicillin binding by the enzyme. Biochem. J. 135:493.
Frère J., Ghuysen M.J.M., Iwatsubo M. (1975) Kinetics of interaction between the exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R61 and β-lactam antibiotics. A choice of models. Eur. J. Biochem. 57:343.
Fuad N., Frère J., Ghuysen M., Duez J.M.C., Iwatsubo M. (1976) Mode of interaction between β-lactam antibiotics and the exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R39. Biochem. J. 155:623.
Frère J., Ghuysen M., Reynolds J.M., Moreno P.E.R., Perkins H.R. (1974) Binding of β-lactam antibiotics to the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R39. Biochem. J. 143:241.
Kelly J.A., Frère Klein J.M.D., Ghuysen J.M. (1981) Interaction between non-classical β-lactam compounds and the Zn2°-containing G and serine R61 and R39 D-alanyl-D-alanine peptidases. Biochem. J. 199:129.
Frère J., Kelly M., Klein J.A., Ghuysen D., Claes J.M.P., Vanderhaeghe H. (1982) Δ2- and Δ2-cephalosporins, penicillinate and 6-unsubstituted penems. Intrinsic reactivity and interaction with β-lactamases and D-alanyl-D-alanine-cleaving serine peptidases. Biochem. J. 203:223.
Frère J., Klein M., Kelly D.J.A., Ghuysen J.M. (1984) Interaction between monobactams and model D-alanyl-D-alanine-cleaving peptidases. FEMS Microbiol. Lett. 21:213.
Laurent Durant G., Frère F., Klein J.M.D., Ghuysen J.M. (1984) Des-, syn- and anti-oxyimino Δ3-cephalosporins. Intrinsic reactivity and reaction with RTEM-2 serine β-lactamase and D-alanyl-D-alanine-cleaving serine and Zn-containing peptidases. Biochem. J. 218:933.
Frère J., Ghuysen M.J.M., Perkins H.R. (1975) Interaction between the exocellular DD-carboxy-peptidase-transpeptidase from Streptomyces R61, substrate and β-lactam antibiotics. A choice of models. Eur. J. Biochem. 57:353.
Frère J., Leyh M.B., Renard A. (1983) Lineweaver-Burk, Hanes, Eadie-Hofstee and Dixon plots in non-steady-state situations. J. Theor. Biol 101:387.
Ghuysen Leyh-Bouille J.M., Frère M., Dusart J.M., Marquet J., Perkins A.H.R., Nieto M. (1974) The penicillin receptor in. Streptomyces, Ann. N.Y. Acad. Sci. 235:236.
Leyh-Bouille Ghuysen M., Nieto J.M., Perkins M., Schleifer H.R.K.H., Kandler O. (1970) On the Streptomyces albus G DD-carboxypeptidase mechanism of action of penicillin, vancomycin and ristocetin. Biochemistry 9:2971.
Dideberg Joris O., Frère B., Ghuysen J.M., Weber J.M., Robaye G., Delbrouck R.J.M., Roelandts I. (1980) The exocellular DD-carboxypeptidase of Streptomyces albus G: a metallo (Zn2°) enzyme. FEBS Lett. 117:215.
Frère J., Duez M., Ghuysen C.J.M., Vandekerkhove J. (1976) Occurrence of a serine residue in the penicillin-binding site of the exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R61. FEBS Lett. 70:257.
Frère J., Ghuysen M.J.M., De Graeve J. (1978) Fragmentation of penicillin catalysed by the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces strain R61. FEBS Lett. 88:147.
Degelaen Feeney J., Roberts J., Burgen G.C.K.A.S.V., Frère J.M., Ghuysen J.M. (1979) NMR evidence for the structure of the complex between penicillin and the DD-carboxypeptidase of Streptomyces R61. FEBS Lett. 98:53.
Duez C., Frère Ghuysen J.M., VanBeeumen J.M.J., Vandekerckhove J. (1981) Studies of the primary structures of the exocellular D-alanyl-D-alanine peptidases of Streptomyces strain R61 and Actinomadura strain R39. Biochim. Biophys. Acta 671:109.
Duez Joris C., Frère B., Ghuysen J.M.J.M., VanBeeumen J. (1981) The penicillin-binding site in the exocellular DD-carboxypeptidase-transpeptidase of Actinomadura R39. Biochem. J. 193:83.
Georgopapadakou Smith N.H.S.A., Cimarusti C.M. (1982) Interaction between monobactams and Streptomyces R61 DD-carboxypeptidase. Eur. J. Biochem. 124:507.
Georgopapadakou Liu N.H., Ryono F.Y., Neubeck D.E.R., Ondetti M.A. (1981) Chemical modifications of the active site of Streptomyces R61 DD-carboxypeptidase. Eur. J. Biochem. 115:53.
Frère J., Ghuysen M., Degelaen J.M., Loffet J.A., Perkins H.R. (1975) Fragmentation of benzylpenicillin after interaction with the exocellular DD-carboxypeptidase-transpeptidases of Streptomyces R61 and R39. Nature (London) 258:168.
Frère J., Ghuysen M., Vanderhaeghe J.M., Adriaens H., Degelaen P.J., De Graeve J. (1976) Fate of thiazolidine ring during fragmentation of penicillin by exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R61. Nature (London) 260:451.
Adriaens Meesschaert P., Frère B., Vanderhaeghe J.M., Degelaen H., Ghuysen J.J.M., Eyssen H. (1978) Stability of D-5,5-dimethyl-Δ2-thiazoline-4-carboxylic acid in relation to its possible occurrence as a degradation product of penicillin by the exocellular DD-carboxypeptidase-transpeptidase from Streptomyces R61 and the membrane-bound DD-carboxypeptidase from Bacillus stearothermophilus. J. Biol. Chem. 253:3660.
Marquet A., Frère Ghuysen J.M.J.M., Loffet A. (1979) Effects of nucleophiles on the breakdown of the benzylpenicilloyl-enzyme complex EI* formed between benzylpenicillin and the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces strain R61. Biochem. J. 177:909.
Knox Kelly J.R., Moews J.A.P.C., Murthy N.S. (1976) 5.5 Å Crystallographic structure of penicillin β-lactamase and radius of gyration in solution. J. Mol. Biol. 104:865.
Aschaffenburg Phillips R., Sulton D.C., Baldwyn B., Kiener G.P.A., Waley S.G. (1978) Preliminary crystallographic data for β-lactamase I from Bacillus cereus 569. J. Mol. Biol. 120:447.
Charlier Dideberg P., Frère O., Moews J.M.P.C., Knox J.R. (1983) Crystallographic data for the β-lactamase from Enterobacter cloacae P99. J. Mol. Biol. 171:237.
Kelly Moews J.A., Knox P.C.I.R., Frère J.M., Ghuysen J.M. (1982) Penicillin target enzyme and the antibiotic binding site. Science 218:479.
Kelly J.A. X-ray structure of a penicillin target enzyme, in The Target of Penicillin , W. De Gruyter, New York; 1983, 387.
Jacques P. Mèmoire de Licence, Université de Liège; 1983.
Waxman D.J., Strominger J.L. (1980) Sequence of active site peptides from the penicillin-sensitive D-alanine carboxypeptidase of Bacillus subtilis. Mechanism of penicillin action and sequence homology to β-lactamases. J. Biol. Chem. 255:3964.
Yocum Rasmussen R.R.J.R., Strominger J.L. (1980) The mechanism of action of penicillin. Penicillin acylates the active site of Bacillus stearothermophilus D-alanine carboxypeptidase. J. Biol. Chem. 255:3977.
Maruyama Yamamoto I.N., Maruyama A.T., Hirota Y. The fine architecture and function of the gene coding for PBP 3 of Escherichia coli, in The Target of Penicillin , W. De Gruyter, New York; 1983, 393.
Nakamura Maruyama M., Soma I.N., Kato M., Suzuki J.H., Hirota Y. (1983) On the process of cellular division in Escherichia colt nucleotide sequence of the gene for penicillin-binding protein 3. Mol. Gen. Genet. 191:1.
Broome-Smith J., Edelman A., Spratt B.G. Sequence of penicillin-binding protein 5 of Escherichia coli, in The Target of Penicillin , W. De Gruyter, New York; 1983, 403.
Ambler R.P. (1980) The structure of β-lactamases. Phil. Trans. R. Soc. Lond. B289:321.
Jaurin B., Grundström T. (1981) ampC Cephalosporinase of Escherichia coli K-12 has a different evolutionary origin from that of β-lactamases of the penicillinase type, Proc. Natl. Acad. Sci. U.S.A. 78:4897.
Leyh-Bouille Dusart M., Nguyen-Distèche J., Ghuysen M., Reynolds J.M.P.E., Perkins H.R. (1977) The peptidoglycan crosslinking enzyme system in Streptomyces strains R61, K15 and rimosus. Exocellular, lysozyme-releasable and membrane-bound enzymes. Eur. J. Biochem. 81:19.
Leyh-Bouille M., Nguyen-Distèche M., Ghuysen J.M. (1981) On the DD-carboxypeptidase enzyme system of Streptomyces strain K15. Eur. J. Biochem 115:579.
Frère J., Geurts M.F., Ghuysen J.M. (1978) The exocellular DD-carboxypeptidase-endopeptidase of Streptomyces albus G. Interaction with β-lactam antibiotics. Biochem. J. 175:801.
Duez C., Frère Klein J.M., Nöel D., Ghuysen M., Delcambe J.M.L., Dierickx L. (1981) The exocellular β-lactamase of Streptomyces albus G. Purification, properties and comparison with the exocellular DD-carboxypeptidase. Biochem. J. 193:75.
Duez C., Frère Geurts J.M., Ghuysen F., Dierickx J.M.L., Delcambe L. (1978) The exocellular DD-carboxypeptidase-endopeptidase from Streptomyces albus G. Purification and chemical properties. Biochem. J. 175:793.
Charlier P., Ph.D. thesis, University of Liège; 1983.
Dideberg Charlier O., Dupont P., Vermeire L.M., Frère J.M., Ghuysen J.M. (1980) The 4.5 Å resolution structure analysis of the exocellular DD-carboxypeptidase of. Streptomyces albus G. FEBS Lett. 117:212.
Dideberg Charlier O., Dive P., Joris G.B., Frère J.M., Ghuysen J.M. (1982) Structure of a Zn2°-containing D-analyl-D-alanine-cleaving carboxypeptidase at 2.5 Å resolution. Nature (London) 299:469.
Nieto Perkins M., Leyh-Bouille H.R.M., Frère J.M., Ghuysen J.M. (1973) Peptide inhibitors of Streptomyces DD-carboxypeptidases. Biochem. J. 131:163.
Labischinski Giesbrecht H., Fisher P., Barnickel E., Bradaczek G., Frère H., Houssier J.M., Charlier C., Dideberg P.O., Ghuysen J.M. (1984) Study of the Zn-containing DD-carboxypeptidase of Streptomyces albus G by small angle X-ray scattering in solution. Eur. J. Biochem. 138:83.
Hill Sammes H.A.O.P.G., Waley S.G. (1980) Active sites of β-lactamases from Bacillus cereus, Phil. Trans. R. Soc. Lond. B289:333.
Ambler R.P., personal communication; 1983.
Weaver Kester L.H.W.R., Matthews B.W. (1977) A crystallographic study of the complex of phosphoramidon with thermolysin. A model for the presumed catalytic transition state and for the binding of extended substrates. J. Mol. Biol. 114:119.
Argos Garavito P., Eventoff M., Rossmann W.M.G., Branden C.I. (1978) Similarities in active center geometries of zinc-containing enzymes, proteases and dehydrogenases. J. Mol. Biol. 126:141.
Lipscomb W.N. (1980) Carboxypeptidase A mechanisms. Proc. Natl. Acad. Sci. U.S.A. 77:3875.
Umbreit J.N., Strominger J.L. (1973) D-alanine carboxypeptidase from Bacillus subtilis membranes. I. Purification and characterization. J. Biol. Chem. 248:6759.
McArthur H.A.I., Reynolds P.E. (1980) Purification and properties of the D-alanyl-D-alanine carboxypeptidase of Bacillus coagulans NCIB 9365. Biochim. Biophys. Acta 612:107.
Shepherd Chase S.T.H.A., Reynolds P.E. (1977) The separation and properties of two penicillin-binding proteins from. Salmonella typhimurium, Eur. J. Biochem. 78:521.
Blumberg P.M., Strominger J.L. (1972) Isolation by covalent affinity chromatography of the penicillin-binding components from membranes of. Bacillus subtilis, Proc. Natl. Acad. Sci. U.S.A. 69:3751.
Spratt B.G., Pardee A.B. (1975) Penicillin-binding proteins and cell shape in. Escherichia coli. Nature (London) 254:516.
Bonner W.M., Laskey R.A. (1974) A film detection method for labelled proteins and nucleic acids in polyacrylamide gels. Eur. J. Biochem. 46:83.
Marquet Dusart A., Ghuysen J.J.M., Perkins H.R. (1974) Membrane-bound transpeptidase and penicillin binding sites in Streptomycesstrain R61. Eur. J. Biochem. 46:515.
Dusart Marquet J., Ghuysen A.J.M., Perkins H.R. (1975) The catalytic activity and penicillin sensitivity in the liquid and frozen states of membrane-bound and detergent-solubilised transpeptidase of Streptomyces R61. Eur. J. Biochem. 56:57.
Nguyen-Distèche M., Frère Dusart J.M., Leyh-Bouille J., Ghuysen M., Pollock J.M.J.J., Iacono V.J. (1977) The peptidoglycan cross-linking enzyme system in Streptomyces R61, K15 and rimosus. Immunological studies. Eur. J. Biochem. 81:29.
Dusart Leyh-Bouille J.M., Ghuysen J.M. (1977) The peptidoglycan cross-linking enzyme system in Streptomyces strains R61, K15 and rimosus. Kinetic coefficients involved in the interactions of the membrane-bound transpeptidase with peptide substrates and β-lactam antibiotics. Eur. J. Biochem. 81:33.
Dusart Reynolds J.P.E., Ghuysen J.M. (1981) Penicillin binding proteins and model transpeptidase activity of the plasma membranes of Streptomyces strains R61 and. rimosus, FEMS Microbiol. Lett. 12:299.
Nguyen-Distèche M., Leyh-Bouille M., Ghuysen J.M. (1982) Isolation of the membrane-bound 26,000-Mr penicillin-binding protein of Streptomyces strain K15 in the form of a sensitive D-alanyl-D-alanine-cleaving transpeptidase. Biochem. J. 207:109.
Pirlot S. Mèmoire de Licence, Université de Liège; 1983.
Veithem A. Mémoire de Licence, Université de Liège; 1983.
Leyh-Bouille M., Nguyen-Distèche M., personal communication; 1983.
Rousset A., Nguyen-Distèche Minck M.R., Ghuysen J.M. (1982) Penicillin-binding proteins and carboxypeptidase/transpeptidase activities in Proteus vulgaris P18 and its penicillin-induced stable L-forms. J. Bacteriol. 152:1042.
Schilf W., Frère P., Frère Martin J.M., Ghuysen H.H., Adriaens J.M.P., Meesschaert B. (1978) Interaction between penicillin and the DD-carboxypeptidase of the unstable L-form of Proteus mirabilis strain 19. Eur. J. Biochem. 85:325.
Schilf W., Martin H.H. (1980) Purification of two DO-carboxypeptidases/transpeptidases with different penicillin sensitivities from. Proteus mirabilis, Eur. J. Biochem. 105:361.
Izaki Matsuhashi K.M., Strominger J.L. (1968) Biosynthesis of the peptidoglycan of bacterial cell walls. XIII. Peptidoglycan transpeptidase and D-alanine carboxypeptidase: penicillin-sensitive enzymatic reaction in strains of. Escherichia coli, J. Biol. Chem. 243:3180.
Pollock J.J., Nguyen-Distèche Ghuysen M., Linder J.M.R., Salton M.R.J. (1974) The DD-carboxypeptidase-transpeptidase system in Escherichia coli mutant strain 44. Ann. N.Y. Acad. Sci. 235:225.
Pollock J.J., Nguyen-Distèche Ghuysen M., Coyette J.M., Under J., Salton R., Kim M.R.J., Perkins K.S.H.R., Reynolds P.E. (1974) Fractionation of the DD-carboxypeptidase-transpeptidase activities solubilized from membranes of Escherichia coli K12, strain 44. Eur. J. Biochem. 41:439.
Nguyen-Distèche Ghuysen M., Pollock J.M., Reynolds J.J., Perkins P.E., Coyette H.R.J., Salton M.R.J. (1974) Enzymes involved in wall peptide cross-linking in Escherichia coli K12, strain 44. Eur. J. Biochem. 41:447.
Nguyen-Distèche Pollock M., Ghuysen J.J., Puig J.M., Reynolds J., Perkins P.E., Coyette H.R.J., Salton M.R.J. (1974) Sensitivity to ampicillin and cephalothin of enzymes involved in wall peptide cross-linking in Escherichia coli K12, strain 44. Eur. J. Biochem. 41:457.
Wickus G.G., Strominger J.L. (1972) Penicillin-sensitive transpeptidation during peptidoglycan biosynthesis in cell-free preparations from Bacillus megaterium. I. Incorporation of free diaminopimelic acid into peptidoglycan. J. Biol., Chem. 247, 5297; .
Wickus G.G., Strominger J.L. (1972) Penicillin-sensitive transpeptidation during peptidoglycan biosynthesis in cell-free preparations from Bacillus megaterium. II. Effect of penicillin and cephalosporins on bacterial growth and in vivo transpeptidation. J. Biol. Chem. 247:5307.
Mirelman Bracha D.R., Sharon N. (1972) Role of penicillin-sensitive transpeptidation reaction in attachment of newly synthesized peptidoglycan to cell walls of. Micrococcus luteus, Proc. Natl. Acad. Sci. U.S.A. 69:3355.
Mirelman D., Sharon N. (1972) Biosynthesis of peptidoglycan by a cell-wall preparation of Staphylococcus aureus and its inhibition by penicillin. Biochem. Biophys. Res. Commun. 46:1909.
Linnett P.E., Strominger J.L. (1974) Biosynthesis of the crosslink of the γ-glutamyl glycine containing peptidoglycan of vegetative cells of. Sporosarcina ureae, J. Biol. Chem. 249:2497.
Linnett P.E., Strominger J.L. (1974) Amidation and crosslinking of the enzymatically synthesized peptidoglycan of. Bacillus stearothermophilus, J. Biol. Chem. 249:2489.
Coyette Ghuysen J.J.M., Fontana R. (1980) The penicillin-binding proteins in Streptococcus faecalis ATCC 9790. Eur. J. Biochem. 110:445.
Coyette Ghuysen J.J.M., Fontana R. (1978) Solubilization and isolation of the membrane-bound DD-carboxypeptidase of Streptococcus faecalis ATCC 9790. Properties of the purified enzyme. Eur. J. Biochem. 88:297.
Coyette Ghuysen J.J.M., Perkins H.R. (1977) The exchange reaction of peptides R-D-alanyl-D-alanine with D[14C] alanine to R-D-alanyl-D-[14C] alanine and D-alanine, catalysed by the membranes of Streptococcus faecalis ATCC 9790. Eur. J. Biochem. 75:225.
Coyette Ghuysen J., Binot J.M., Adriaens F., Meesschaert P.B., Vanderhaeghe H. (1977) Interactions between β-lactam antibiotics and isolated membranes of Streptococcus faecalis ATCC 9790. Eur. J. Biochem. 75:231.
Kozarich J.W., Strominger J.L. (1978) A membrane enzyme from Staphylococcus aureus which catalyzes transpeptidase, carboxypeptidase, and penicillinase activities. J. Biol. Chem. 253:1272.
Blumberg P.M., Strominger J.L. (1972) Five penicillin-binding components occur in Bacillus subtilis membranes. J. Biol. Chem. 247:8107.
Waxman D.J., Strominger J.L. (1979) Cephalosporin-sensitive penicillin-binding proteins of Staphylococcus aureus and Bacillus subtilis active in the conversion of [14C] penicillin G to [14C] phenylacetylglycine. J. Biol. Chem. 254:12056.
Hayes Curtis M.V., Wyke N.A.C.A.W., Ward J.B. (1981) Decreased affinity of a penicillin-binding protein for β-lactam antibiotics in a clinical isolate of Staphylococcus aureus resistant to methicillin. FEMS Microbiol. Lett. 10:119.
Brown D.F.J., Reynolds P.E. (1980) Intrinsic resistance to β-lactam antibiotics in. Staphylococcus aureus, FEBS Lett. 122:275.
Curtis Hayes N.A.C., Wyke M.V.A.W., Ward J.B. (1980) A mutant of Staphylococcus aureus H lacking penicillin-binding protein 4 and transpeptidase activity. In vitro, FEMS Microbiol. Lett. 9:263.
Wyke Ward A.W., Hayes J.B.M.V., Curtis N.A.C. (1981) A role in vivo for penicillin-binding protein-4 of. Staphylococcus aureus, Eur. J. Biochem. 119:389.
Mirelman D. Assembly of wall peptidoglycan polymers, in β-Lactam Antibiotics , Academic Press, New York; 1981, 67.
Lawrence P.J., Strominger J.L. (1970) Biosynthesis of the peptidoglycan of bacterial cell walls. XV. The binding of radioactive penicillin to the particulate enzyme preparation of Bacillus subtilis and its reversal with hydroxylamine or thiols. J. Biol. Chem. 245:3653.
Lawrence P.J., Strominger J.L. (1970) Biosynthesis of the peptidoglycan of bacterial cell walls. XVI. The reversible fixation of radioactive penicillin G to the D-alanine carboxypeptidase of. Bacillus subtilis, J. Biol. Chem. 245:3660.
Reynolds P.E. Peptidoglycan synthesis in bacilli. I. Effect of temperature on the in vitro system from Bacillus megaterium , Bacillus stearothermophilus, Biochim. Biophys., Acta; 1971, 237:239.
Reynolds P.E., Barnett H.J. (1974) Transpeptidases and DD-carboxypeptidases in bacilli. Ann. N.Y. Acad. Sci. 235:269.
Blumberg Yocum P.M., Willoughby R.R.E., Strominger J.L. (1974) Binding of [14C]penicillin G to the membrane-bound and the purified D-alanine carboxypeptidases from Bacillus stearothermophilus and Bacillus subtilis and its release. J. Biol. Chem. 249:6828.
Nishino Kozarich T.J.W., Strominger J.L. (1977) Kinetic evidence for an acyl-enzyme intermediate in D-alanine carboxypeptidases of Bacillus subtilis and. Bacillus stearothermophilus, J. Biol. Chem. 252:2934.
Storm Blumberg D.R.P.M., Strominger J.L. (1974) Inhibition of the Bacillus subtilis membrane-bound D-alanine carboxypeptidase by 6-aminopenicillanic acid covalently coupled to sepharose. J. Bact. 117:783.
Sharpe Blumberg A.P.M., Strominger J.L. (1974) D-alanine carboxypeptidase and cell wall cross-linking in. Bacillus subtilis, J. Bact. 117:926.
Hammarström S., Strominger J.L. (1975) Degradation of penicillin G to phenylacetylglycine by D-alanine carboxypeptidase from. Bacillus stearothermophilus, Proc. Natl. Acad. Sci. U.S.A. 72:3463.
Hammarström S., Strominger J.L. (1976) Formation of 5,5-dimethyl-Δ2-thiazoline-1-carboxylic acid during cleavage of penicillin G by D-alanine carboxypeptidase from Bacillus stearothermophilus. J. Biol. Chem. 251:7947.
Kozarich Nishino J.W., Willoughby T.E., Strominger J.L. (1977) Hydroxylaminolysis of penicillin binding components is enzymatically catalyzed. J. Biol. Chem. 252:7525.
Georgopapadakou N.H., Hammarström S., Strominger J.L. (1977) Isolation of the penicillin-binding peptide from D-alanine carboxypeptidase of. Bacillus subtilis, Proc. Natl. Acad. Sci. U.S.A. 74:1009.
Yocum Waxman R.R., Rasmussen D.J.J.R., Strominger J.L. (1979) Mechanism of penicillin action: penicillin and substrate bind covalently to the same active site serine in two bacterial D-alanine carboxypeptidases. Proc. Natl. Acad. Sci. U.S.A. 76:2730.
Waxman D.J., Strominger J.L. (1979) Cleavage of a COOH-terminal hydrophobic region from D-alanine carboxypeptidase, a penicillin-sensitive bacterial membrane enzyme. Characterization of active, water-soluble fragments. J. Biol. Chem. 254:4863.
Waxman D.J., Strominger J.L. (1981) Limited proteolysis of the penicillin-sensitive D-alanine carboxypeptidase purified from Bacillus subtilis membranes. Active, water-soluble fragments generated by cleavage of a COOH-terminal membrane anchor. J. Biol. Chem. 256:2059.
Waxman D.J., Strominger J.L. (1981) Primary structure of the COOH-terminal membranous segment of a penicillin-sensitive enzyme purified from two. Bacilli, J. Biol. Chem. 256:2067.
Chase Shepherd H.A.S.T., Reynolds P.E. (1977) Studies on the penicillin-binding components of. Bacillus megaterium, FEBS Lett. 76:199.
Chase H.A. (1980) Purification of four penicillin-binding proteins from. Bacillus megaterium, J. Gen. Microbiol. 117:211.
Diaz-Maurino T., Nieto M., Perkins H.R. (1974) Membrane-bound DD-carboxypeptidases from Bacillus megaterium KM. General properties, substrate specificity and sensitivity to penicillins, cephalosporins and peptide inhibitors of the activity at pH 5. Biochem. J. 143:391.
Marquet Nieto A.M., Diaz-Maurino T. (1976) Membrane-bound DD-carboxypeptidase and transpeptidase activities from Bacillus megaterium KM at pH 7. Eur. J. Biochem. 68:581.
Chase Reynolds H.A.P.E., Ward J.B. (1978) Purification and characterization of the penicillin-binding protein that is the lethal target of penicillin in Bacillus megaterium and. Bacillus licheniformis, Eur. J. Biochem. 88:275.
Guinand Michel M.G., Tipper D.J. (1974) Appearance of a γ-D-glutamyl-(L)meso-diaminopime-late peptidoglycan hydrolase during sporulation in. Bacillus sphaericus, J. Bacteriol. 120:173.
Tamura Imae T.Y., Strominger J.L. (1976) Purification to homogeneity and properties of two D-alanine carboxypeptidases I from. Escherichia coli, J. Biol. Chem. 251:414.
Spratt B.G., Strominger J.L. (1976) Identification of the major penicillin-binding proteins of Escherichia coli as a D-alanine carboxypeptidase I.A. J. Bacteriol. 127:660.
Amanuma H., Strominger J.L. (1980) Purification and properties of penicillin-binding proteins 5 and 6 from Escherichia coli membranes. J. Biol. Chem. 255:11173.
Matsuhashi Ishino M., Tamaki F., Nakajima-Iijima S., Tomioka S., Nakagawa S., Hirata J., Spratt A., Tsuruoka B.G., Inouye T.S., Yamada Y. Mechanism of action of β-lactam antibiotics. Inhibition of peptidoglycan transpeptidases and novel mechanisms of action., Trends in Antibiotic Research, Japan Antibiotics Research Association, 99; .
Curtis S.J., Strominger J.L. (1978) Effects of sulfhydryl reagents on the binding and release of penicillin G by D-alanine carboxypeptidase IA of. Escherichia coli, J. Biol. Chem. 253:2584.
Spratt B.G. (1977) Properties of the penicillin-binding proteins of Escherichia coli K12. Eur. J. Biochem. 72:341.
Matsuhashi Takagaki M., Maruyama Y., Tamaki I.N., Nishimura S., Suzuki Y., Ogino H.U., Hirota Y. (1977) Mutants of Escherichia coli lacking in highly penicillin-sensitive D-alanine carboxypeptidase activity. Proc. Natl. Acad. Sci. U.S.A. 74:2976.
Matsuhashi Maruyama M., Takagaki I.N., Tamaki Y., Nishimura S.Y., Hirota Y. (1978) Isolation of a mutant of Escherichia coli lacking penicillin-sensitive D-alanine carboxypeptidase I.A. Proc. Natl. Acad. Sci. U.S.A. 75:2631.
Spratt B.G. (1980) Deletion of the penicillin-binding protein 5 gene of. Escherichia coli, J. Bacteriol. 144:1190.
Broome-Smith J.K., Spatt B.G. (1982) Deletion of the penicillin-binding protein 6 gene of. Escherichia coli, J. Bacteriol. 152:904.
Waxman Amanuma D.J.H., Strominger J.L. (1982) Amino acid sequence homologies between Escherichia coli penicillin-binding protein 5 and class A β-lactamases. FEBS Lett. 139:159.
Iwaya M., Strominger J.L. (1977) Simultaneous deletion of D-alanine carboxypeptidase IB-C and penicillin-binding component IV in a mutant of Escherichia coli K12. Proc. Natl. Acad. Sci. U.S.A. 74:2980.
Tomioka S., Matsuhashi M. (1978) Purification of penicillin-insensitive DD-endopeptidase, a new cell-wall peptidoglycan-hydrolysing enzyme in Escherichia coli, and its inhibition by deoxyribonucleic acids. Biochem. Biophys. Res. Commun. 84:978.
Matsuhashi Tamaki M., Curtis S.S.J., Strominger J.L. (1979) Mutational evidence for identity of penicillin-binding protein 5 in Escherichia coli with the major D-alanine carboxypeptidase IA activity. J. Bacteriol. 137:644.
Broome-Smith J., Spratt B.G., personal communication; 1983.
Nishimura Suzuki Y., Hirota H.Y., Park J.T. (1980) A mutant of Escherichia coli defective in penicillin-binding protein 5 and lacking D-alanine carboxypeptidase. J. Bacteriol. 143:531.
Markiewicz Broome-Smith Z., Schwarz J.K.U., Spratt B.G. (1982) Spherical Escherichia coli due to elevated levels of D-alanine carboxypeptidase. Nature (London) 297:702.
Hammes W.P., Seidel H. (1978) The activities in vitro of DD-carboxypeptidase and LD-carboxypeptidase of Gaffkya homariduring biosynthesis of peptidoglycan. Eur. J. Biochem. 84:141.
Hammes W.P., Seidel H. (1978) The LD-carboxypeptidase activity in Gaffkya homari. The target of the action of certain β-lactam antibiotics on the formation of wall-bound peptidoglycan. Eur. J. Biochem. 91:509.
Kim H.S., Campbell B.J. (1982) β-lactamase activity of renal dipeptidase against N-formimidoylthienamycin. Biochem. Biophys. Res. Commun. 108:1638.
Labia Kazmierczak R., Guionie A.M., Masson J.M. (1980) Some bacterial proteins with affinity for cefotaxime. J. Antimicrob. Chemother. 6:19.
Corran P.H., Waley S.G. (1975) The reaction of penicillin with proteins. Biochem. J. 149:357.
Reynolds P.E., Chase H. β-lactam binding proteins: identification as lethal targets and probes of β-lactam accessibility, in β-Lactam Antibiotics , Academic Press, New York; 1981, 153.
Reynolds P.E., personal communication; 1983.
Joris B., Ph.D. thesis, University of Liege; 1983.
Stoker Pratt N.G.J.M., Spratt B.G. (1983) Identification of the rodA gene product of. Escherichia coli, J. Bacteriol. 155:854.
Tamaki Nakajima S.S., Matsuhashi M. (1977) Thermosensitive mutation in Escherichia coli simultaneously causing defects in penicillin-binding protein-1Bs and in enzyme activity for peptidoglycan synthesis. In vitro, Proc. Natl. Acad. Sci. U.S.A. 74:5472.
Spratt Jobanputra B.G.V., Schwarz U. (1977) Mutants of Escherichia coli which lack a component of penicillin-binding protein 1 are viable. FEBS Lett. 79:374.
Curtis S.J., Strominger J.L. (1981) Purification of penicillin-binding protein 2 of. Escherichia coli, J. Bacteriol. 145:398.
Spratt B.G. (1975) Distinct penicillin binding proteins involved in the division, elongation, and shape of Escherichia coli K12. Proc. Natl. Acad. Sci. U.S.A. 72:2999.
Suzuki Nishimura H.Y., Hirota Y. (1978) On the process of cellular division in Escherichia coli: a series of mutants of E. coli altered in the penicillin-binding proteins. Proc. Natl. Acad. Sci. U.S.A. 75:664.
Matsuhashi Ishino M., Nakagawa F., Mitsui J., Nakajima-Iijima K., Tamaki S.S., Hashizuma T. Enzymatic activities of penicillin-binding proteins of E. coli and their sensitivities to β-lactam antibiotics, in β-Lactam Antibiotics , Academic Press, New York; 1981, 169.
Tomioka Ishino S., Tamaki F.S., Matsuhashi M. (1982) Formation of hyper-crosslinked peptidoglycan with multiple crosslinkages by a penicillin-binding protein, 1A, of. Escherichia coli, Biochem. Biophys. Res. Commun. 106:1175.
Suzuki VanHeijenoort H., Tamura Y., Mizoguchi T., Hirota J.Y., VanHeijenoort J. (1980) In vitro peptidoglycan polymerization catalyzed by penicillin binding protein 1b of Escherichia coli K12. FEBS Lett. 110:245.
Ishino Mitsui F., Tamaki K.S., Matsuhashi M. (1980) Dual enzyme activities of cell wall peptidoglycan synthesis, peptidoglycan transglycosylase and penicillin-sensitive transpeptidase, in purified preparations of Escherichia coli penicillin-binding protein 1A. Biochem. Biophys. Res. Commun. 97:287.
Tarawa Suzuki T., Nishimura H., Mizoguchi Y.J., Hirota Y. (1980) On the process of cellular division in Escherichia coli: isolation and characterization of penicillin-binding proteins la, lb, and 3. Proc. Natl. Acad. Sci. U.S.A. 77:4499.
Ishino F., Matsuhashi M. (1981) Peptidoglycan synthetic enzyme activities of highly purified penicillin-binding protein 3 in Escherichia coli: a septum-forming reaction sequence. Biochem. Biophys. Res. Commun. 101:905.
Nakagawa J., Matsuhashi M. (1982) Molecular divergence of a major peptidoglycan synthetase with transglycosylase-transpeptidase activities in Escherichia coli penicillin-binding protein 1 Bs. Biochem. Biophys. Res. Commun. 105:1546.
Ishino Tamaki F., Spratt S.B.G., Matsuhashi M. (1982) A mecillinam-sensitive peptidoglycan crosslinking reaction in. Escherichia coli, Biochem. Biophys. Res. Commun. 109:689.
Stoker Broome-Smith N.G., Edelman J.K.A., Spratt B.G. (1983) Organization and subcloning of the dacA-rodA-pbpA cluster of cell shape genes in. Escherichia coli, J. Bacteriol. 155:847.
Croft L.R. Handbook of Protein Sequences, Joynson-Bruvvers, Oxford; 1973.
Kleppe G., Strominger J.L. (1979) Studies of the high molecular weight penicillin-binding proteins of. Bacillus subtilis, J. Biol. Chem. 254:4856.
Chase H.A., Reynolds P.E. (1981) The cell-wall as a permeability barrier to β-lactam antibiotics in. Bacillus megaterium, FEMS Microbiol. Lett. 10:285.
Waxman Lindgren D.J.D.M., Strominger J.L. (1981) High-molecular-weight penicillin-binding proteins from membranes of bacilli. J. Bacteriol. 148:950.
Rodriguez-Tebar A., Rojo F., Vasquez D. (1982) Interaction of β-lactam antibiotics with penicillin-binding proteins from. Bacillus megaterium, Eur. J. Biochem. 126:161.
Buchanan C.E., Strominger J.L. (1976) Altered penicillin-binding components in penicillin-resistant mutants of. Bacillus subtilis, Proc. Natl. Acad. Sci. U.S.A. 73:1816.
Reynolds Shepherd P.E.S.T., Chase H.A. (1978) Identification of the binding protein which may be the target of penicillin action in. Bacillus megaterium. Nature (London) 271:568.
Taku Stuckey A.M., Fan D.P. (1982) Purification of the peptidoglycan transglycosylase of Bacillus megaterium. J. Biol. Chem. 257:5018.
Jackson G.E.D., Strominger J.L. (1984) Synthesis of peptidoglycan by high molecular weight penicillin-binding proteins of Bacillus subtilis and. Bacillus stearothermophilus, J. Biol. Chem. 259:1483.
Curtis N.A., Hayes M.V. (1981) A mutant of Staphylococcus aureus H deficient in PBP1 is viable. FEMS Microbiol. Lett. 10:227.
Wyke Ward A.W.J.B., Hayes M.V. Penicillin-sensitive enzymes in Staphylococcus aureus, in The Target of Penicillin , W. De Gruyter, New York; 1983, 543.
Wyke Ward A.W.J.B., Hayes M.V. (1982) Synthesis of peptidoglycan in vivo in methicillin-resistant. Staphylococcus aureus, Eur. J. Biochem. 127:553.
Wilkinson B.J., Nadakavukaren M.J. (1983) Methicillin-resistant septal peptidoglycan synthesis in a methicillin-resistant Staphylococcus aureus strain. Antimicrob. Agents Chemother. 23:610.
Fontana Canepari R., Satta P.G., Coyette J. (1980) Identification of the lethal target of benzyl-penicillin in Streptococcus faecalis by in vivo penicillin binding studies. Nature (London) 287:70.
Fontana Canepari R., Satta P.G., Coyette J. (1983) Streptococcus faecium ATCC 9790 penicillin-binding proteins and penicillin sensitivity are heavily influenced by growth conditions: proposal for an indirect mechanism of growth inhibition by β-lactams. J. Bacteriol 154:916.
Coyette J., SomzéBriquet A., Ghuysen J.J.J.M., Fontana R. Function of penicillin-binding protein 3 in Streptococcus faecium, in The Target of Penicillin , W. De Gruyter, New York; 1983, 523.
Fontana Canepari R.P., Satta G. The role of a protein that binds penicillin with slow kinetics in physiology and response to penicillin of Streptococcus faecium ATCC 9790 The Target of Penicillin , W. De Gruyter, New York; 1983, 531.
Satta Canepari G.P., Fontana R. A novel hypothesis to explain regulation of the murein sacculus shape, in The Target of Penicillin , W. De Gruyter, New York; 1983, 135.
Sykes R.B., Bush K. Physiology, biochemistry, and inactivation of β-lactamases, in The Chemistry and Biology of β-Lactam Antibiotics , Academic Press, New York; 1982, 3:155.
Hamilton-Miller J.M.T., Smith J.T. β-Lactamases, Academic Press, London; 1979.
Hill Sammes H.A.O.P.G., Waley S.G. (1980) Active sites of β-lactamases from. Bacillus cereus, Phil. Trans. R. Soc. Lond. B289:333.
Pollock M.R. (1971) The function and evolution of penicillinase. Proc. R. Soc. Lond. B 179:385.
Saz A.K., Lowery D.L. Do β-lactamases have a biological function?, in β-Lactamases , Academic Press, London; 1979, 465.
Saz A.K. (1970) An introspective view of penicillinase. J. Cell. Physiol. 76:397.
Richmond M.H., Sykes R.B. (1973) The β-lactamases of gram-negative bacteria and their possible physiological role. Adv. Microb. Physiol. 9:31.
Meadway R.J. (1969) The amino acid sequence of penicillinase from Bacillus licheniformis. Biochem. J. 115:12.
Ambler R.P. (1975) The amino acid sequence of Staphylococcus aureus penicillinase. Biochem. J. 151:197.
Thatcher D.B. (1975) The partial amino-acid sequence of the exocellular β-lactamase I of Bacillus cereus 569/H. Biochem. J. 137:313.
Ambler R.P., Scott G.K. (1978) Partial amino acid sequence of penicillinase coded by Escherichia coli plasmid R6K. Proc. Natl. Acad. Sci. U.S.A. 75:3732.
Sutcliffe J.G. (1978) Nucleotide sequence of the ampicillin resistance gene of Escherichia coli plasmid pBR 322. Proc. Natl. Acad. Sci. U.S.A. 75:3737.
Saino Kobayashi Y., Inoue F.M., Mitsuhashi S. (1982) Purification and properties of inducible penicillin β-lactamase isolated from. Pseudomonas maltophilia, Antimicrob. Agents Chemother. 22:564.
Knox Kelly J.R., Moews J.A.P.C., DeLucia M.L. RTEM β-lactamase: secondary structure prediction and X-ray analysis at 4 A resolution in β-Lactamases , Academic Press, London; 1979, 127.
Brown Butterworth A.G., Cole D., Hanscomb M., Hood G.J.D., Reading C. (1976) Naturally-occurring β-lactamase inhibitors with antibacterial activity. J. Antibiot. 29:668.
Maeda Takahashi K., Sezaki S., Iinuma M., Naganawa K., Kondo H., Ohno S.M., Umezawa H. (1977) Isolation and structure of a β-lactamase inhibitor from. Streptomyces, J. Antibiot. 30:770.
Brown Corbett A.G., Eglington D.F.A.J., Howarth T.T. (1977) Structure of olivanic acid derivatives MM4550and MM13902. J. Chem. Soc. Chem. Commun. 523.
Fukagawa Okamura Y., Shibamoto K.N., Ishikura T. PS-series β-lactam antibiotics, in β-Lactam Antibiotics , Ed. S. Mitsuhashi., Japan Scientific Societies Press, Tokyo; 1981, 158.
Pratt R.F., Loosemore M.J. (1978) 6-β-bromopenicillanic acid, a potent β-lactamase inhibitor. Proc. Natl. Acad. Sci. U.S.A. 75:4145.
English Retsema A.R., Girard J.A., Lynch A.E.J.E., Barth W.E. (1978) CP45899, a β-lactamase inactivator which extends the antibacterial spectrum of β-lactams. Antimicrob. Agents Chemother. 14:414.
Fisher Charnas J., Bradley R.L.S.M., Knowles J.R. (1981) Inactivation of the RTEM β-lactamase from Escherichia coli. Interaction of penam sulfones with enzyme. Biochemistry 20:2726.
Knott-Hunziker Waley V., Orlek S.G.B.S., Sammes P.G. (1979) Penicillinase active sites: labeling of serine-44 in β-lactamase I by 6β-bromopenicillanic acid. FEBS Lett. 99:59.
Cartwright S.J., Coulson A.F.W. (1980) Active site of staphylococcal β-lactamase. Phil. Trans. R. Soc. Lond. B289:370.
Cartwright S.J., Fink A.L. (1982) Isolation of a covalent intermediate in β-lactamase I catalysis. FEBS Lett. 137:186.
Anderson E.G., Pratt R.F. (1981) Pre-steady state β-lactamase kinetics. Observation of a covalent intermediate during turnover of a fluorescent cephalosporin by the β-lactamase of Staphylococcus aureus PC1. J. Biol. Chem. 256:11401.
Knott-Hunziker Petursson V., Jayatilake S., Waley G.S., Jaurin S.G.B., Grundström T. (1982) Active sites of β-lactamases. The chromosomal β-lactamases of Pseudomonas aeruginosa and. Escherichia coli, Biochem. J. 201:621.
Joris Dusart B., Frère J., VanBeeumen J.M., Emanuel J., Petursson E.L., Gagnon S.J., Waley S.G. (1984) The active site of the P99 β-lactamase from. Enterobacter cloacae. Biochem. J. 223:271.
Sigal Harwood I.S.B.G., Arentzen R. (1982) Thiol-β-lactamase: replacement of the active-site serine of RTEM β-lactamase by a cysteine residue. Proc. Natl. Acad. Sci. U.S.A. 79:7157.
Fisher Belasco J., Khosla J.G.S., Knowles J.R. (1980) β-lactamase proceeds via an acyl-enzyme intermediate. Interaction of the Escherichia coli RTEM enzyme with cefoxitin. Biochemistry 19:2895.
Citri Samuni N.A., Zyk N. (1976) Acquisition of substrate-specific parameters during the catalytic reaction of penicillinase. Proc. Natl. Acad. Sci. U.S.A. 73:1048.
Kiener Knott-Hunziker P.A., Petursson V.S., Waley S.G. (1980) Mechanism of substrate-induced inactivation of β-lactamase I. Eur. J. Biochem. 109:575.
Frère J.M. (1981) Interaction between serine β-lactamases and class A substrates: a kinetic analysis and a reaction pathway hypothesis. Biochem. Pharmacol. 30:549.
Anderson E.G., Pratt R.F. (1983) Pre-steady stage β-lactamase kinetics: the trapping of a covalent intermediate and the interpretation of pH-rate profiles. J. Biol. Chem. 258:13120.
Loosemore Cohen M.J.S.A., Pratt R.F. (1980) Inactivation of Bacillus cereus β-lactamase I by 6β-bromopenicillanic acid: kinetics. Biochemistry 19:3990.
Frère J., Dormans M., Duyckaerts C.C., De Graeve J. (1982) Interaction of β-iodopenicillanate with the β-lactamases of Streptomyces albus G and Actuiomadura R39. Biochem. J. 207:437.
Fisher Charnas J.R.L., Knowles J.R. (1978) Kinetic studies on the inactivation of Escherichia coli RTEM β-lactamase by clavulanic acid. Biochemistry 17:2180.
Frère J., Dormans M., Lenzini C.V.M., Duyckaerts C. (1982) Interaction of clavulanate with the β-lactamases of Streptomyces albus G and Actinomadura R39. Biochem. J. 207:429.
Charnas R.L., Knowles J.R. (1981) Inactivation of RTEM β-lactamase from Escherichia coli by clavulanic acid and 9-deoxyclavulanic acid. Biochemistry 20:3214.
Knott-Hunziker Orlek V., Sammes B.S.P.G., Waley S.G. (1980) Kinetics of inactivation of β-lactamase I by 6β-bromopenicillanic acid. Biochem. J. 187:797.
Waley S.G., personal communication; 1983.
Moews Knox P.C., Waxman J.R.D.J., Strominger J.L. (1981) Secondary structure relations between β-lactamases and penicillin-sensitive D-alanine-carboxypeptidases. Int. J. Peptide Protein 17:211.
Kelly J.A., Frère Duez J.M.C., Ghuysen J.M. (1981) Interactions between non-classical β-lactam compounds and the β-lactamases of Actinomadura R39 and Streptomyces albus G. Biochem. J. 199:137.
Duez C., Frère Ghuysen J.M., VanBeeumen J.M., Delcambe J.L., Dierickx L. (1982) Purification and properties of the exocellular β-lactamase of Actinomadura strain R39. Biochim. Biophys. Acta 700:24.
Pratt R.F., Govardhan C.P. (1984) β-lactamase catalysed hydrolysis of acyclic depsipeptides and acyl transfer to specific amino acid acceptors. Proc. Natl. Acad. Sci. U.S.A. 81:1302.
Sykes Cimarusti R.B., Bonner C.M., Bush D.P., Floyd K., Georgopapadakou D.M., Koster N.H., Liu W.H., Parker W.C., Principe W.L., Rathnum P.A., Slusarchyk M.L., Trejo W.A.W.H., Wells J.S. (1981) Monocyclic β-lactam antibiotics produced by bacteria. Nature (London) 291:489.
Georgopapadakou Smith N.H.S.A., Sykes R.B. (1982) Mode of action of azthreonam. Antimicrob. Agents Chemother. 21:950.
Lee B. (1971) Conformation of penicillin as a transition-state analog of the substrate of peptidoglycan transpeptidase. J. Mol. Biol. 61:463.
Rando R.R. (1975) On the mechanism of action of antibiotics which act as irreversible enzyme inhibitors. Biochem. Pharmacol 24:1153.
Lamotte-Brasseur J., Dive G., Ghuysen J.M. (1984) On the structural analogy between D-alanyl-D-alanine terminated peptides and β-lactam antibiotics. Eur. J. Med. Chem. 19:319.