Kinetic mechanism of enterococcal aminoglycoside phosphotransferase 2″-Ib
Biochemistry, ISSN: 0006-2960, Vol: 46, Issue: 18, Page: 5570-5578
2007
- 23Citations
- 17Captures
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Metrics Details
- Citations23
- Citation Indexes23
- 23
- CrossRef19
- Captures17
- Readers17
- 17
Article Description
The major mechanism of resistance to aminoglycosides in clinical bacterial isolates is the covalent modification of these antibiotics by enzymes produced by the bacteria. Aminoglycoside 2″-Ib phosphotransferase [APH(2″)-Ib] produces resistance to several clinically important aminoglycosides in both Gram-positive and Gram-negative bacteria. Nuclear magnetic resonance analysis of the product of kanamycin A phosphorylation revealed that modification occurs at the 2″-hydroxyl of the aminoglycoside. APH(2″)-Ib phosphorylates 4,6-disubstituted aminoglycosides with kK values of 10 -10 M s, while 4,5-disubstituted antibiotics are not substrates for the enzyme. Initial velocity studies demonstrate that APH(2″)-Ib operates by a sequential mechanism. Product and dead-end inhibition patterns indicate that binding of aminoglycoside antibiotic and ATP occurs in a random manner. These data, together with the results of solvent isotope and viscosity effect studies, demonstrate that APH(2″)-Ib follows the random Bi-Bi kinetic mechanism and substrate binding and/or product release could limit the rate of reaction. © 2007 American Chemical Society.
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