Masters Theses
Date of Award
12-2014
Degree Type
Thesis
Degree Name
Master of Science
Major
Biochemistry and Cellular and Molecular Biology
Major Professor
Engin H. Serpersu
Committee Members
Gladys Alexandre, Hong Guo
Abstract
Aminoglycosides have proven very useful in the treatment of infections; lately their effectiveness has been greatly reduced due to increasing resistance. Among many known mechanisms of resistance to aminoglycosides, enzymatic modification is the most prevailing. More than 14 aminoglycoside -N3-acetyltransferases- a class of aminoglycoside modifying enzymes, are known today. This study focuses on a pair of acetyl transferases: The aminoglycoside-N3- acetyltransferase IIIb (AAC-IIIb) and the aminoglycoside-N3- acetyltransferase IIa (AAC-IIa). AAC-IIa and AAC-IIIb are very similar in their amino acid sequence and structure – yet they have a strong difference in their substrate selectivity, kinetic and thermodynamic properties. This work represents a comparative study of these two enzymes in an effort to determine thermodynamic basis of the differential substrate profiles of AAC-IIa to AAC-IIIb.
Recommended Citation
Raval, Sherin R., "A step towards understanding of the molecular basis of ligand promiscuity in the aminoglycoside modifying enzymes. " Master's Thesis, University of Tennessee, 2014.
https://trace.tennessee.edu/utk_gradthes/3173