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Comparison Of Activation Enthalpies For Aminoglycoside Modification Reactions, Brittany Sterling Soto
Comparison Of Activation Enthalpies For Aminoglycoside Modification Reactions, Brittany Sterling Soto
Masters Theses
At highly elevated temperatures, many biological reactions can proceed spontaneously from the ground state to the transition state. However, due to the long half-life of these reactions, catalysts are required to catalyze these reactions at modern day temperatures by lowering the activation energy. Wolfenden et al. has previously shown that catalysts enhance the rate of the reaction by reducing the enthalpy of activation. Therefore, the activation energies have been determined for three aminoglycoside modifying enzymes, APH(3’)-IIIa, AAC(3)-IIIb, and AAC(3)-VIa, to determine whether these three enzymes distinguish between the two classes of aminoglycoside antibiotics by reducing the enthalpy of activation during …
Examining The Functional Consequences Of The Flexibility Of Aminoglycoside Phosphotransferase (3’)-Iiia, Katelyn Dawn Rosendall
Examining The Functional Consequences Of The Flexibility Of Aminoglycoside Phosphotransferase (3’)-Iiia, Katelyn Dawn Rosendall
Masters Theses
The use of aminoglycoside antibiotics began in 1940 with the discovery of streptomycin. The overuse and misuse of antibiotics has resulted in prevalent cases of antibiotic resistance. The most common source of aminoglycoside resistance is the presence of enzymes that covalently modify the antibiotics at specific locations. One such enzyme, APH(3′)-IIIa [the aminoglycoside phosphotransferase three prime three a] conveys resistance by transferring the γ-phosphate [gamma phosphate] from ATP [adenosine triphosphate] onto the 3′ [three prime] carbon of the aminoglycoside antibiotic sugar ring. APH(3′)-IIIa has been shown to be flexible in solution and this flexibility is proposed to be responsible for …