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Welcome!» Faculty and Research» Engin Serpersu


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

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., 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.

Özen, C. and Serpersu EH (in press) Thermodynamics of aminoglycoside binding to aminoglycoside-3′-phosphotransferase IIIa studied by isothermal titration calorimetry. Biochemistry.

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.

Özen, C., Norris, A. L., Land, M., Tjioe, E., and Serpersu, E. H. (2008) Detection of Specific Solvent Rearrangement Regions of an Enzyme: NMR and ITC Studies with Aminoglycoside Phosphotransferase(3′)-IIIa. Biochemistry, 47, 40-49.

Serpersu, E., H., Özen, C., and Wright, E. (2008) Studies of enzymes that cause resistance to aminoglycoside antibiotics. Methods in Molecular Medicine ( New Antibiotic Targets) 142, 261-271.

Özen, C., Malek, J. M., and Serpersu, E. H. (2006). Dissection of Aminoglycoside-Enzyme Interactions: A Calorimetric and NMR Study of Noemycin B Binding to the Aminoglycoside Phosphotransferase(3')-IIIa. J. Am. Chem. Soc. 128, 15248-15254.

Serpersu, E., H., Özen, C., and Wright, E. (2006) Thermodynamic Studies of Aminoglycoside Antibiotic-Enzyme Interactions. Turkish J. Biochem. 31, 79-85.

Wright, E. and Serpersu, E. H. (2006) Molecular Determinants of Affinity for Aminoglycoside Binding to the Aminoglycoside Nucleotidyltransferase(2″)-Ia. Biochemistry 45, 10243-10250.

Wright E and Serpersu EH (2004) Isolation of Aminoglycoside Nucleotidyltransferase (2″)-Ia from Inclusion Bodies as Active, Monomeric Enzyme. Protein Express. Purif. 35: 373-380.

Owston AM and Serpersu EH (2002) Cloning, overexpression and purification of aminoglycoside antibiotic 3-acetyltransferase-IIIb: Conformational studies with bound substrates. Biochemistry  41: 10764-10770.

Ekman DR, DiGiammarino EL, Wright E, Witter ED and Serpersu EH (2001) Cloning overexpression and purification of aminoglycoside antibiotic nucleotidyl transferase (2")-Ia: Conformational Studies with bound substrates.  Biochemistry 40: 7017-7024.

Cox JR, Ekman DR,  DiGiammarino EL,  Akal-Strader A and  Serpersu E H (2000) Aminoglycoside Antibiotics Bound to Aminoglycoside-Detoxifying Enzymes and RNA Adopt Similar Conformations. Cell Biochem. & Biophys. 33: 297-308.

Serpersu  EH, Cox JR,  DiGiammarino EL, Mohler ML, Ekman DR, Akal-Strader A and Owston M (2000) Conformations of Antibiotics in  Active Sites of  Aminoglycoside-Detoxifying Enzymes. Cell Biochem. & Biophys. 33: 309-321.

DiGiammarino EL, Draker K, Wright GD and Serpersu EH (1998) Solution Studies of Isepamicin and conformational comparisons between isepamicin and butirosin A when bound to an aminoglycoside 6N-N-acetyltransferase determined by NMR spectroscopy. Biochemistry 37: 3638-3644.

Mohler LM, Cox JR and Serpersu EH (1998) Aminoglycoside phosphotransferase(3N)-IIIa (APH(3N)-IIIa)-bound conformation of the aminoglycoside lividomycin A characterized by NMR. Carbohydr. Lett.  3: 17-24.

Cox JR and Serpersu EH (1997) Biologically important conformations of aminoglycoside antibiotics bound to an aminoglycoside 3N-phosphotransferase as determined by transferred nuclear Overhauser effect spectroscopy. Biochemistry 36: 2353-2359.

Pappu KM, Kunnumal B and Serpersu EH (1997) A new metal binding site for yeast phosphoglycerate kinase as determined by the use of metal-ATP analog. Biophys. J. 2: 928-935.

Cox JR, McKay GA, Wright GD and Serpersu EH (1996) Arrangement of substrates at the active site of an aminoglycoside antibiotic 3N-phosphotransferase (APH(3N)-IIIa) as determined by NMR. J. Am. Chem. Soc. 118:1295-1301.

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., 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 Thermodynamics of a Ternary System. Biochemistry. 49, 4036-4042.

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Engin Serpersu, Ph.D.

 

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: eserpersu@utk.edu