Literature DB >> 3447876

Stability of dactimicin to aminoglycoside-modifying enzymes.

R Gomez-Lus1, M A Marco, M L Gomez-Lus.   

Abstract

Dactimicin was active against strains expressing the activities of aminoglycoside acetylating enzymes [AAC(3)-II, III, IV and V, AAC(2'), AAC(6')-I and II], aminoglycoside-nucleotidylating enzymes [ANT(2"), AAD(3")] and aminoglycoside-phosphorylating enzymes [APH(3')-I-II and III], with the exception of AAC(3)-I and one staphylococcal AAC(6')-IV. Apparently this is the first report of one 6'-N-acetylating enzyme which modifies and inactivates dactimicin. The authors' data suggest that the differences in the behaviour of dactimicin, gentamicin and amikacin against the aminoglycoside-resistant strains tested were mainly due to the production of aminoglycoside-modifying enzymes. If the results are summarized, it may be concluded that dactamicin is the most stable to the majority of aminoglycoside-modifying enzymes demonstrated [APH(3'), APH(2"), APH(3"), ANT(2"), AAD(3"), AAC(2') and AAC(6')], with the exception of AAC(3)-I and staphylococcal AAC(6')-IV.

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Year:  1987        PMID: 3447876

Source DB:  PubMed          Journal:  Drugs Exp Clin Res        ISSN: 0378-6501


  1 in total

1.  In vitro activity of dactimicin, a novel pseudodisaccharide aminoglycoside, compared with activities of other aminoglycosides.

Authors:  J W Gu; H C Neu
Journal:  Antimicrob Agents Chemother       Date:  1989-11       Impact factor: 5.191

  1 in total

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