Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UMLS:C0348321 (Haemophilus)
 15,372 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Plasmid mediated phosphorylating activities have been found in Haemophilus sp. strains resistant to some aminoglycoside antibiotics. The enzymes responsible for this phenomenon have been purified and studied. They belong to the group of aminoglycoside phosphotransferases which are able to phosphorylate these antibiotics on the 3'- or 5"-hydroxyl group. The first enzyme studied is closely related to APH(3')I whereas the second one is different from the former on the basis of substrate specificities and physicochemical properties. We propose to call this second enzyme APH(3')Ib as compared to APH(3')I which will be called APH(3')Ia.
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PMID:[Plasmidic resistance of "Haemophilus sp." to aminoglycoside antibiotics: isolation and study of a new phosphotransferase (author's transl)]. 19 1

From September 1, 1990 to December 31, 1993 a total of 425 Haemophilus influenzae strains from clinical specimens were isolated in the Microbiology Laboratory of the Zaragoza University Hospital. Of these strains, 16 (33.33%) were resistant to kanamycin, neomycin, paromomycin, lividomycin and streptomycin. Demonstration of APH (3')-I activity by the phosphocellulose paper binding assay, based on the incorporation of radiolabel into lividomycin was sixfold greater than into butirosin. Two DNA probes were prepared to screen for the genes encoding APH(3') activity in kanamycin-resistant H. influenzae. Homology was observed between the aphA1 DNA probe and total cellular DNA from all 16 APH(3')-I producers. On the other hand, streptomycin-resistance was not through metabolic modification of the antibiotic.
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PMID:Aminoglycoside resistance in Haemophilus influenzae. 766 27