STABILITY OF DACTIMICIN TO AMINOGLYCOSIDE-MODIFYING ENZYMES

  • 1 January 1987
    • journal article
    • research article
    • Vol. 13  (12) , 731-735
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)-1 and staphylocccal AAC(6'')-IV.