Nucleotide sequence of the gene encoding the active-site serine β-lactamase from Actinomadura R39 [PDF]
FEMS Microbiology Letters, 1989 The gene encoding the extracellular, active-site serine beta-lactamase of Actinomadura R39, previously cloned into Streptomyces lividans, has the information for the synthesis of a 304 amino acid protein, the amino terminal region of which has the characteristic features of a signal peptide.
S. Houba +6 more
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Molecular weight, amino acid composition and physicochemical properties of the exocellular DD-carboxypeptidase-transpeptidase of Streptomyces R39. [PDF]
Biochemical Journal, 1974 The exocellular dd-carboxypeptidase–transpeptidase from Streptomyces R39 was purified to protein homogeneity and in milligram amounts. The isolated enzyme consisted of one polypeptide chain of molecular weight about 53300. Its amino acid composition and several physicochemical properties were determined and compared with those of the exo-cellular dd ...
J. Frère, R. Moreno, J. Ghuysen
semanticscholar +3 more sources
dd-Carboxypeptidase-Transpeptidase and Killing Site of β-Lactam Antibiotics in Streptomyces Strains R39, R61, and K11 [PDF]
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
J. Dusart +9 more
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Interaction of beta-iodopenicillanate with the beta-lactamases of Streptomyces albus G and Actinomadura R39. [PDF]
Biochemical Journal, 1982 The beta-lactamases of Streptomyces albus G and Actinomadura R39 are inactivated by beta-iodopenicillanate. However, in contrast with the beta-lactamase I from Bacillus cereus, they also efficiently catalyse the hydrolysis of the inactivator; with the S. albus G enzyme, kcat.
J. Frère +3 more
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The penicillin-binding site in the exocellular DD-carboxypeptidase-transpeptidase of Actinomadura R39. [PDF]
Biochemical Journal, 1981 Heat denaturation and Pronase degradation of the complex previously formed between benzylpenicillin and the exocellular DD-carboxypeptidase-transpeptidase of Actinomadura R39 yields a heptapeptide H-Leu-Pro-Ala-Ser-Asn-Gly-Val-OH, where the benzylpenicilloyl group is ester-linked to the serine residue.
C. Duez +4 more
semanticscholar +4 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
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Binding of antiphospholipid antibodies to discontinuous epitopes on domain I of human beta(2)-glycoprotein I: mutation studies including residues R39 to R43. [PDF]
Arthritis & Rheumatism, 2007 AbstractObjectivePathogenic antiphospholipid antibodies (aPL) bind the self antigen N‐terminal domain (domain I) of β2‐glycoprotein I (β2GPI), with residues G40–R43 being important. However, peptides homologous to other regions of domain I have also been shown to bind aPL.
Y. Ioannou +5 more
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Purification and properties of the exocellular β-lactamase of a Actinomadura strain R39 [PDF]
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1982 The exocellular beta-lactamase (penicillin amido-beta-lactamhydrolase, EC 3.5.2.6) of Actinomadura R39 consists of one single polypeptide chain of molecular weight about 15 200. It exhibits a highly asymmetrical shape, has a low isoelectric point (at pH 5.0) and contains about 9.3% (w/w) of a polydeoxyribonucleotide with which it forms a rather stable ...
C. Duez +5 more
semanticscholar +3 more sources
Structure of the wall peptidoglycan of Streptomyces R39 and the specificity profile of its exocellular DD-carboxypeptidase--transpeptidase for peptide acceptors. [PDF]
Biochemistry, 1973 Benzylpenicillin and cephaloridine reacted with the exocellular dd-carboxypeptidase–transpeptidase from Streptomyces R39 to form equimolar and inactive antibiotic–enzyme complexes. At saturation, the molar ratio of chromogenic cephalosporin 87-312 to enzyme was 1.3:1, but this discrepancy might be due to a lack of accuracy in the measurement of the ...
J. Ghuysen +7 more
semanticscholar +4 more sources
The Baraitser-Winter Cerebrofrontofacial Syndrome Recurrent R196H Variant in Cytoplasmic β-Actin Impairs Its Cellular Polymerization and Stability. [PDF]
FASEB JBWCFF, a severe disease with neurological symptoms, is caused by mutations in the cytoskeletal actin genes. Patient‐derived fibroblasts carrying the R196H β‐actin mutation were compared to wild type cells. The mutant cells displayed slower proliferation and migration and a lower F‐actin content, which correlated with reduced cell stiffness ...
Gráczer É +12 more
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