Purification and characterization of an aminoglycoside inactivating enzyme from Staphylococcus epidermidis FK109 that nucleotidylates the 4'- and 4"-hydroxyl groups of the aminoglycoside antibiotics.

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Abstract
The resistance to aminoglycoside antibiotics in S. epidermidis FK109, is mediated by an enzyme that catalyzes transfer of the nucleotide monophosphate moiety from the nucleotide triphosphates to the 4''-hydroxyl group or the 4"-hydroxyl group, that is in the equatorial plane of the aminoglycoside molecule. The enzyme, modifying the 2 sites, appears as a single and homogeneous entity in affinity chromatography, in chromatography on DEAE-Sepharose Cl-6B, in isoelectric focusing and in gel-filtration. It requires divalent cations, notably Mg++, and dithiothreitol for optimal adenylylation. It has a MW of 46,770 and an isoelectric point of 5.0. The ability of the enzyme modify the 2 hydroxyl groups of aminoglycoside molecules, enables it to have a spectrum of substrates that surpasses, in range, the substrate spectrum of all the aminoglycoside-modifying enzymes which were previously characterized.

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