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
openaire +4 more sources
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
openaire +5 more sources
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
openaire +5 more sources
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
core +7 more sources
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
openaire +4 more sources
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
openaire +5 more sources
Applied and Environmental Microbiology, 1997 Monospecific polyclonal antisera raised against Rhizobium leguminosarum bv. trifolii R39, a bacterium which was isolated originally from red clover nodules, were used to study the colonization of roots of leguminous and nonleguminous plants (Pisum sativum, Lupinus albus, Triticúm aestivum, and Zea mays) after inoculation.
M, Schloter +6 more
openaire +3 more sources
Biochemistry, 2010 The Actinomadura R39 DD-peptidase is a bacterial low molecular weight class C penicillin-binding protein. It has previously been shown to catalyze hydrolysis and aminolysis of small D-alanyl-D-alanine terminating peptides, especially those with a side chain that mimics the amino terminus of the stem peptide precursor to the bacterial cell wall.
Dzhekieva, Liudmila +5 more
openaire +3 more sources
Fragmentation of benzylpenicillin after interaction with the exocellular DD-carboxypeptidase-transpeptidases of Streptomyces R61 and R39 [PDF]
Nature, 1975 THE killing target of penicillin in bacteria is a membrane-bound transpeptidase which catalyses peptide cross linking during wall peptidoglycan synthesis1,2. Streptomyces R61 and R39 excrete during growth DD-carboxypeptidase-transpeptidase enzymes3,4 which seem to be soluble forms of the corresponding membrane-bound transpeptidases5.
Frère, Jean-Marie +4 more
openaire +3 more sources