Engin Serpersu, Ph.D.

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Research Statement

The major project studied in our laboratory involves structural and functional studies of enzymes that modify antibiotics and render them useless against infectious diseases. We use several different enzymes that catalyze different chemical modification reactions of aminoglycoside antibiotics. Current studies are concentrated on the determination of  thermodynamic properties of various enzyme–antibiotic complexes and their solution structures using NMR, EPR spectroscopy, computer modeling, isothermal and differential scanning calorimetry and other biophysical and biochemical techniques. These studies are aimed to understand dynamic and structural features of enzyme–antibiotic complexes and to determine basic principles of macromolecule–ligand interactions.

Selected Publications

Wright, E. and Serpersu, E. H. (2011) Effects of Proton Linkage on Thermodynamic Properties of Enzyme–Antibiotic Complexes of the Aminoglycoside Nucleotidyltransferase(2″)-Ia.  J. Thermodyn. and Catal.  “in press”.

Wieninger, S. A, Serpersu, E. H. and Ullmann, G. M. (2011) ATP Binding Enables Broad Antibiotic Selectivity of Aminoglycoside Phosphotransferase(3′)-IIIa– An Elastic Network Analysis. J. Mol. Biol.409,450-465.

Serpersu, E. H., Özen, C., Norris, A. L. Steren, C. and Whittemore, N. (2010) Backbone Resonance Assignments of a Promiscuous Aminoglycoside Antibiotic Resistance Enzyme; the Aminoglycoside Phosphotransferase(3′)-IIIa. Biomol. NMR Assign. 4, 9-12.

Norris, A. L. and Serpersu, E. H. (2010) Coenzyme A Interactions with the Aminoglycoside Acetyltransferase (3)-IIIb and the Thermodynamics of a Ternary System. Biochemistry 49,4036–4042.

Norris, A. L., Özen, C., and Serpersu, E. H. (2010) Thermodynamics and Kinetics of Antibiotic Association with the Aminoglycoside Acetyltransferase (3)-IIIb: A Resistance Causing Enzyme. Biochemistry 49, 4027-4035.

Norris, A. L. and Serpersu, E. H. (2010) Coenzyme A Interactions with the Aminoglycoside Acetyltransferase (3)-IIIb and the Thermodynamics of a Ternary System. Biochemistry 49, 4036–4042.

Norris, A. D. and Serpersu, E. H. (2009) NMR Detected Hydrogen-Deuterium Exchange Reveals Differential Dynamics of Antibiotic and Nucleotide Bound Aminoglycoside Phosphotransferase 3′-IIIa. J. Am. Chem. Soc. 131, 8587-8594.

Wu, Lingzhi and Serpersu, E. H. (2009) Deciphering Interactions of the Aminoglycoside Phosphotransferase(3′)-IIIa with its Ligands. Biopolymers 91, 801-809.

 

Contact Information

Office:
Room F-431A
Walters Life Sciences
Phone: (865) 974-2668

Lab:
Room D-417
Walters Life Sciences
Phone: (865) 974-2530

Email: serpersu@utk.edu