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M L Capmau

Publications and source records attributed to M L Capmau.

23 records · Page 2Linked to original sources

2"-O-phosphorylation of gentamicin components by a Staphylococcus aureus strain carrying a plasmid.

A wild-type strain of Staphylococcus aureus that inactivates the 4,6-glycosidically linked deoxystreptamine aminoglycoside antibiotics by a plasmid-mediated process was found to harbor two enzymes: an acetyltransferase of the AAC(6') type and a new phosphotranferase specific to the gentamicin components. The target of this last enzyme is the 2''-hydroxyl function of these antibiotics, since one inactivated compound is 2''-(O)-phosphorylsisomicin.

Acetyltransferases↗

Plasmid-mediated pristinamycin resistance. PAC IIA: a new enzyme which modifies pristinamycin IIA.

A wild strain of Staphylococcus aureus which inactivates a wide variety of antibiotics has been found to inactivate pristinamycin IIA, an antistaphylococcal antibiotic. This phenomenon has been demonstrated to be plasmid mediated. The plasmid directs the biosynthesis of an acetyltransferase which is able to O-acetylate the drug. We propose to call the new enzyme PAC (IIA): Pristinamycin acetyltransferase.

Acetyltransferases↗

[Analysis of biospecific complexes by electrophoresis: antibiotics specific to bacterial ribosomes].

Electrophoresis is a widespread method in biochemistry. Apparently it has never been used in the study of interactions found in enzyme-substrates or drug-receptor complexes. The aim of this Note is to describe some possibilities given by this simple technique especially in the case of interactions found between some antibiotics and the bacterial ribosome. Chloramphenicol, pristinamycin are located in 50 S subunit whereas dihydrostreptomycin is found in 30 S particle (fig). Such results have been previously obtained by other methods. The distribution of the gentamicin and kanamycin components is quite different. This suggests that the mechanism of action of these molecules may be different from that of streptomycin group antibiotics.

Anti-Bacterial Agents↗

New plasmid-mediated nucleotidylation of aminoglycoside antibiotics in Staphlococcus aureus.

A wild-type strain of Staphylococcus aureus, which inactivates a wide variety of aminoglycosides (except the gentamicin components), has been found to harbor a plasmid (RAp01) that mediates the biosynthesis of a nucleotidyltransferase. This enzyme modifies the 4'-hydroxy function of these antibiotics. The plasmid has been studied, the enzyme responsible for this resistance pattern has been isolated by affinity chromatography, and its kinetics and physicochemistry have been characterized. The target of this enzyme has also been located by demonstrating the structure of one inactivated compound, 4'-(O)-adenylyltobramycin.

Aminoglycosides↗