Penicillin target. Penicillin target enzyme and the antibiotic binding site. X-ray structure of streptococcus pneumoniae pbp2x, a primary ....

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Involvement of a change in penicillin target and peptidoglycan ...

Penicillin target. Oglycan structure in low-level resistance to beta-lactam antibiotics in Neisseria gonorrhoeae.Journal List > Antimicrob Agents Chemother > v.28(1); Jul 1985" style="vertical-align:middle; margin-right:3pt">Summary Selected References Page Browse PDF (969K) Contents Archive Journal Homepage Related material:PubMed recordPubMed related artsPubMed LinkOutPubChem CompoundPubChem SubstanceTaxonomyTaxonomy treePubMed articles by: Dougherty, T. Antimicrob Agents Chemother. 1985 July; 28(1): 90–95. Copyright noticeInvolvement of a change in penicillin target and peptidoglycan structure in low-level resistance to beta-lactam antibiotics in Neisseria gonorrhoeae.T J Dougherty This article has been cited by other articles in PMC.AbstractA penicillin-susceptible gonococcus and its low-level resistant penA transformant were examined with regard to their penicillin-binding proteins (PBPs) and their peptidoglycan structures. Treatment of the susceptible strain with its MIC of penicillin ( penicillin target
 

Structural determinants required to target penicillin-binding ...

0.01 microgram ml) led to significant binding to PBPs 2 and 3 and a substantial decrease in the O-acetyl modification on the peptidoglycan. Peptidoglycan synthesis gradually ceased over an extended time. When the penA strain was treated with the same concentration of penicillin, only binding to PBP 3 was observed and there was no O-acetylation decrease, with continued peptidoglycan synthesis. This suggested that PBP 2 was the primary target in penicillin-susceptible gonococci and that this protein participated in the O-acetylation of peptidoglycan. Penicillin concentrations representing the MIC for the penA transformant (0.06 microgram ml) caused significant binding to PBPs 1, 2, and 3 in the susceptible strain and PBPs 1 and 3 in the penA strain. In both strains the rate of peptidoglycan synthesis and the cross-linkage of the peptidoglycan made declined sharply, suggesting that significant inhibition of PBP 1 interfered with transpeptidation. A model for low-level resistance is propos penicillin target


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penicillin target Ash;641. PubMed Dougherty TJ. Peptidoglycan biosynthesis in Neisseria gonorrhoeae strains sensitive and intrinsically resistant to beta-lactam antibiotics. J Bacteriol. 1983 Jan;153(1):429–435. PubMed Dougherty TJ penicillin target, Koller AE penicillin target, Tomasz A. Penicillin-binding proteins of penicillin-susceptible and intrinsically resistant Neisseria gonorrhoeae. Antimicrob Agents Chemother. 1980 Nov;18(5):730–737. PubMed Dougherty TJ penicillin target, Koller AE penicillin target, Tomasz A. Competition of beta-lactam antibiotics for the penicillin-binding proteins of Neisseria gonorrhoeae. Antimicrob Agents Chemother. 1981 Jul;20(1):109–114. PubMed Goodell EW penicillin target, Fazio M penicillin target, Tomasz A. Effect of benzylpeni penicillin target.

penicillin target Cillin on the synthesis and structure of the cell envelope of Neisseria gonorrhoeae. Antimicrob Agents Chemother. 1978 Mar;13(3):514–526. PubMed Lear AL penicillin target, Perkins HR. Degrees of O-acetylation and cross-linking of the peptidoglycan of Neisseria gonorrhoeae during growth. J Gen Microbiol. 1983 Mar;129(3):885–888. PubMed Maier TW penicillin target, Zubrzycki L penicillin target, Coyle MB penicillin target, Chila M penicillin target, Warner P. Genetic analysis of drug resistance in Neisseria gonorrhoeae: production of increased resistance by the combination of two antibiotic resistance loci. J Bacteriol. 1975 Nov;124(2):834–842. PubMed Martin HH penicillin target, Gmeiner J. Modification of peptidoglycan structure by penicillin action in cell walls of Proteus mirabilis. Eur J Biochem. 1979 Apr;95(3):487–495. PubMed Sarubbi FA Jr penicillin target, Sparling PF penicillin target, Blackman E penicillin target, Lewis E. Loss of low-level antibiotic resistance in Neisseria gonorrhoeae due to env mutations. J Bacteriol. 1975 Nov;124(2):750–756. PubMed Sinha RK penicillin target, Rosenthal RS. Release of soluble peptidoglycan from growing conococci: demonstration of anhydro-muramyl-containing fragments. Infect Immun. 1980 Sep;29(3):914–925. PubMed Sparling PF penicillin target, Sarubbi FA Jr penicillin target, Blackman E. Inheritance of low-level resistance to penicillin penicillin target, tetracycline penicillin target, and chloramphenicol in Neisseria gonorrhoeae. J Bacteriol. 1975 Nov;124(2):740–749. PubMed S.

penicillin target in cell walls of Proteus mirabilis. Eur J Biochem. 1979 Apr;95(3):487–495. PubMed Sarubbi FA Jr penicillin target, Sparling PF penicillin target, Blackman E penicillin target, Lewis E. Loss of low-level antibiotic resistance in Neisseria gonorrhoeae due to env mutations. J Bacteriol. 1975 Nov;124(2):750–756. PubMed Sinha RK penicillin target, Rosenthal RS. Release of soluble peptidoglycan from growing conococci: demonstration of anhydro-muramyl-containing fragments. Infect Immun. 1980 Sep;29(3):914–925. PubMed Sparling PF penicillin target, Sarubbi FA Jr penicillin target, Blackman E. Inheritance of low-level resistance to penicillin penicillin target, tetracycline penicillin target, and chloramphenicol in Neisseria gonorrhoeae. J Bacteriol. 1975 Nov;124(2):740–749. PubMed Sp.

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D.J. & Strominger, J.L. Penicillin-binding proteins and the mechanism of action of -lactam antibiotics. Annu. Rev. Biochem. 52, 825& 8722;865 (1983). Article PubMed ISI ChemPort Matsuhashi, M. in New Comprehensive Biochemistry. Bacterial Cell Wall Vol. 27, (eds J.-M. Ghuysen & R. Hakenbeck) 55& 8722;71 (Elsevier Science Publishers, Amsterdam 1994). ChemPort Spratt, B.G. Resistance to antibiotics mediated by target alterations. Science 264, 388& 8722;393 (1994). PubMed ISI ChemPort Laible, G., Spratt, B.G. & Hakenbeck, R. Interspecies recombinational events during the evolution of altered PBP 2x genes in penicillin-resistant clinical isolates of Streptococcus pneumoniae. Mol. Microbiol. 5, 1993& 8722;2002 (1991). PubMed ISI ChemPort Laible, G. & Hakenbeck, R. Penicillin-binding proteins in -lactam-resistant laboratory mutants of Streptococcus pneumoniae. Mol. Microbiol. 1, 355& 8722;363 (1987). PubMed ISI ChemPort Charlier, P. et al. Crystallization of a genetically engineered water-soluble primary penicillin target enzyme. The high molecular mass PBP2x of Streptococcus pneumoniae. J. Mol. Biol. 232, 1007& 8722;1009 (1993). Article PubMed ISI ChemPort Lobkovsky, E. et al. Evolution of an enzyme activity: Crystallographic structure at 2- Å resolution of cephalosporinase from the ampCgene of Enterobacter cloacae P99 and comparison with a class A penicillinase. Proc. Natl. Acad. Sci. USA 90, 11257& 8722;11261 (1993). PubMed ChemPort Kelly, J.A. & Kuzin, A.P. The refined Crystallographic structure of a DD-peptidase penicillin-target enzyme at 1.6 &Arin

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