Mode of interaction between β-lactam antibiotics and the exocellular DD-carboxypeptidase–transpeptidase from Streptomyces R39. [PDF]
Biochemical Journal, 1976 The exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R39 is inhibited by beta-lactam antibiotics according to the same general scheme of reaction as the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R61. However, the values for the kinetic constants involved in the reaction are very different for the two enzymes and ...
Fuad, Noha +4 more
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Inhibition of Streptococcus pneumoniae Penicillin-Binding Protein 2x and Actinomadura R39 DD-Peptidase Activities by Ceftaroline [PDF]
Antimicrobial Agents and Chemotherapy, 2013 ABSTRACT Although the rate of acylation of a penicillin-resistant form of Streptococcus pneumoniae penicillin-binding protein 2x (PBP2x) by ceftaroline is 80-fold lower than that of its penicillin-sensitive counterpart, it remains sufficiently high ( k 2
Zervosen, Astrid +2 more
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Cloning and amplified expression in Streptomyces lividans of the gene encoding the extracellular β-lactamase of Actinomadura R39 [PDF]
Biochemical Journal, 1989 By using the promoter-probe plasmid pIJ424, genomic DNA fragments of Actinomadura R39 were shown to have promoter activity in Streptomyces lividans. The same 100-200-copy-number plasmid was used to clone in S. lividans TK24, the gene that encodes the Actinomadura R39 beta-lactamase. Gene cloning resulted in an amplified expression of the beta-lactamase
Fraipont, Claudine +6 more
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Studies on the primary structures of the exocellular d-alanyl-d-alanine peptidases of Streptomyces strain R61 and Actinomadura strain R39 [PDF]
Biochimica et Biophysica Acta (BBA) - Protein Structure, 1981 The Mr 37 000 D-alanyl-D-alanine peptidase excreted by Streptomyces R61 and the Mr 53 000 D-alanyl-D-alanine peptidase excreted by Actinomadura R39 are both characterized by a very uneven distribution of the basic (Arg + Lys) amino acid residues. Trypsin degradation of the heat-denatured enzymes generates (1) thirteen soluble peptides which contain ...
Duez, Colette +4 more
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Interactions between non-classical β-lactam compounds and the β-lactamases of Actinomadura R39 and Streptomyces albus G [PDF]
Biochemical Journal, 1981 6-Aminopenicillanic acid, 7-aminocephalosporanic acid, mecillinam and quinacillin have varying substrate activities for both the R39 beta-lactamase (excreted by Actinomadura R39) and the G beta-lactamase (excreted by Streptomyces albus G). Cefoxitin and quinacillin sulphone are not recognized by the G beta-lactamase and are weak inactivators of the R39
Kelly, Judith +3 more
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Inhibition of
Biochemistry, 2013 Inhibitors of bacterial DD-peptidases represent potential antibiotics. In the search for alternatives to β-lactams, we have investigated a series of compounds designed to generate transition state analogue structures upon reaction with DD-peptidases. The compounds contain a combination of a peptidoglycan-mimetic specificity handle and a warhead capable
Dzhekieva, Liudmila +7 more
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Primary and predicted secondary structure of the Actinomadura R39 extracellular
Biochemical Journal, 1992 As derived from gene cloning and sequencing, the 489-amino-acid DD-peptidase/penicillin-binding protein (PBP) produced by Actinomadura R39 has a primary structure very similar to that of the Escherichia coli PBP4 [Mottl, Terpstra & Keck (1991) FEMS Microbiol. Lett. 78, 213-220]. Hydrophobic-cluster analysis of the two proteins shows that, providing
Granier, Benoît +8 more
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Antimicrobial Agents and Chemotherapy, 1973 Additional evidence is given that in Streptomyces strains R39, R61, and K11 the same enzyme performs dd -carboxypeptidase and transpeptidase activities and that this enzyme is the killing site of β-lactam antibiotics. With strain R61, it was found that the exocellular enzyme has a sensitivity
Dusart, Jean +9 more
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Synthesis and Evaluation of 3-(Dihydroxyboryl)benzoic Acids as
Journal of Medicinal Chemistry, 2009 Penicillin binding proteins (PBPs) catalyze steps in the biosynthesis of bacterial cell walls and are the targets for the beta-lactam antibiotics. Non-beta-lactam based antibiotics that target PBPs are of interest because bacteria have evolved resistance to the beta-lactam antibiotics.
Inglis, Steven R. +7 more
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The effect of induced molting on the testicular physiological remodeling in no-semen roosters [PDF]
BMC GenomicsBackground The fertility of roosters significantly impacts the economic outcome of the poultry industry. However, it is common for some roosters to fail to produce semen during production, and the underlying reasons remain largely unclear.
Wanying Xie +8 more
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