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Altered Substrate Specificities by Substitutions at Tyr 218 in Bacterial Aminoglycoside 3'- Phosphotransferase – II
Date
1992-06-01
Author
Kocabıyık, Semra
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Mutant aminoglycoside 3'-phosphotransferase II enzymes were produced in which Tyr218 was changed to serine, aspartic acid, or phenylalanine. In each case the mutation resulted in increased bacterial susceptibility to neomycin and kanamycin, while simultaneously increasing the Km values for these substrates. For the Ser and Asp mutants, bacterial resistance to amikacin increased, with a concomitant increase in affinity for this drug. Initial velocity studies indicated that the wild-type and mutant enzymes all followed Michaelis-Menten kinetics. Although these mutagenic substitutions changed the substrate specificity of these enzymes they did not alter the enzyme affinity for Mg(2+)-ATP.
URI
https://hdl.handle.net/11511/71172
Journal
FEMS Microbiol. Lett
DOI
https://doi.org/10.1016/0378-1097(92)90529-w
Collections
Department of Biology, Article
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S. Kocabıyık, “Altered Substrate Specificities by Substitutions at Tyr 218 in Bacterial Aminoglycoside 3′- Phosphotransferase – II,”
FEMS Microbiol. Lett
, pp. 199–202, 1992, Accessed: 00, 2021. [Online]. Available: https://hdl.handle.net/11511/71172.