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Tobramycin adenylyltransferase: a new aminoglycoside-inactivating enzyme from staphylococcus epidermidis


Santanam, P; Kayser, F H (1976). Tobramycin adenylyltransferase: a new aminoglycoside-inactivating enzyme from staphylococcus epidermidis. Journal of Infectious Diseases, 134(Supplement):S33-S39.

Abstract

Certain strains of Staphylococcus epidermidis resistant to the aminoglycoside antibiotics were shown to contain an enzyme that inactivates the kanamycins, neomycins, butirosins, paromomycin, gentamicin A, amikacin, and tobramycin by adenylylation. Tobramycin adenylyltransferase, as this enzyme is called, was found to be optimally active at pH 5.5. With paromomycin or neomycin Band C as substrates, however, two pH values (5.5 and 9.0) for optimal activity were observed. The enzyme requires Mg+ + for activity and is stabilized significantly by dithiothreitol. It is probable that the 4′-hydroxyl group of ring I of the antibiotics is adenylylated. Those aminoglycosides that are not substrates for the enzyme lack a hydroxyl group in the corresponding position

Abstract

Certain strains of Staphylococcus epidermidis resistant to the aminoglycoside antibiotics were shown to contain an enzyme that inactivates the kanamycins, neomycins, butirosins, paromomycin, gentamicin A, amikacin, and tobramycin by adenylylation. Tobramycin adenylyltransferase, as this enzyme is called, was found to be optimally active at pH 5.5. With paromomycin or neomycin Band C as substrates, however, two pH values (5.5 and 9.0) for optimal activity were observed. The enzyme requires Mg+ + for activity and is stabilized significantly by dithiothreitol. It is probable that the 4′-hydroxyl group of ring I of the antibiotics is adenylylated. Those aminoglycosides that are not substrates for the enzyme lack a hydroxyl group in the corresponding position

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Item Type:Journal Article, refereed, original work
Communities & Collections:National licences > 142-005
Dewey Decimal Classification:570 Life sciences; biology
610 Medicine & health
Language:English
Date:1 August 1976
Deposited On:23 Oct 2018 17:18
Last Modified:24 Nov 2018 02:56
Publisher:Oxford University Press
ISSN:0022-1899
OA Status:Green
Free access at:Publisher DOI. An embargo period may apply.
Publisher DOI:https://doi.org/10.1093/infdis/134.supplement_1.s33
Related URLs:https://www.swissbib.ch/Search/Results?lookfor=nationallicenceoxford101093infdis134Supplement_1S33 (Library Catalogue)
PubMed ID:972283

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