Patrick Hanna, PhD

Morse-Alumni Distinguished Teaching Professor of Medicinal Chemistry and Professor Emeritus, Department of Medicinal Chemistry

Patrick Hanna

Contact Info

Office Phone 612-625-4152

Fax 612-626-3114

Office Address:
8-170 Weaver-Densford Hall

Mailing Address:
University of Minnesota
College of Pharmacy
Department of Medicinal Chemistry
8-101 Weaver-Densford Hall
308 Harvard St. SE
Minneapolis, MN 55455

Morse-Alumni Distinguished Teaching Professor of Medicinal Chemistry and Professor Emeritus, Department of Medicinal Chemistry

Professor, Department of Pharmacology

PhD, University of Kansas, 1969

Bachelor of Creighton University, 1963


Many chemicals that cause cancer or produce other undesirable effects do so only after they are converted (bioactivated) in the body to carcinogenic or toxic metabolites. The primary emphasis of my laboratory is on the chemical and biochemical aspects of bioactivation reactions catalyzed by N-acetyltransferases. These investigations involve application of the techniques of organic chemistry, protein chemistry, enzymology and molecular biology.

N-acetyltransferases play a central role in the metabolic detoxification and bioactivation of a diverse group of drugs, carcinogens and environmentally important chemicals. Acetylation is a major metabolic pathway for hydrazines, hydrazides and arylamines. N-acetyltransferases also catalyze the conversion of carcinogenic arylhydroxylamines (ARNHOH) and arylhydroxamic acids (ArNOHCOCH3) to reactive metabolites that form covalent adducts with proteins and nucleic acids. One objective is to gain insight into differences in the substrate specificities and active site topologies of acetyltransferase isozymes by identifying critical peptide and amino acid residues and elucidating their contributions to substrate binding and catalysis. A second major objective is to identify and characterize the arylamine-protein adducts formed as a result of acetyltransferase-catalyzed bioactivation of carcinogens. The results of the research will provide a basis for understanding the functions and catalytic mechanisms of the acetyltransferases and will contribute to definitive characterization of the chemical mechanisms through which the bioactivated carcinogens form adducts with their macromolecular targets.



  • F. Liu, N. Zhang, X. Zhou, P.E. Hanna, C.R. Wagner, D.M. Koepp and K.J. Walters. Arylamine N- Acetyltransferase Aggregation and Constituitive Ubiquitylation. J. Mol. Biol. 361, 482-492 (2006).
  • N. Zhang, L. Liu, F. Liu, C.R. Wagner, P.E. Hanna and K.J. Walters. NMR-based Model Reveals the Structural Determinants of Mammalian Arylamine N-Acetyltransferase Substrate Specificity. J. Mol. Biol. 363, 188-200 (2006).
  • L. Liu, A VonVett, N. Zhang, K.J. Walters, C.R. Wagner and P.E. Hanna. Arylamine N-Acetyltransferases: Characterization of the Substrate Specificities and Molecular Interactions of Environmental Arylamines with Human NAT1 and NAT2. Chem. Res. Toxicol. 20 , 1300-1308 (2007).
  • R.F. Minchin, P.E. Hanna, J-M. Dupret, C.R. Wagner, F. Rodrigues-Lima and N.J. Butcher. Arylamine N-Acetyltransferase I. Intl. J. Biochem. Cell Biol., 39, 1999-2005 (2007).L. Liu, C. R. Wagner, and P. E. Hanna. Human Arylamine N-Acetyltransferase 1: In Vitro and Intracellular Inactivation by Nitrosoarene Metabolites of Toxic and Carcinogenic Arylamines. Chem. Res. Toxicol. 21, 2005-2016 (2008).
  • X. Zhou, N. Zhang, L. Liu, K.J. Walters, P.E. Hanna and C.R. Wagner. Probing the Catalytic Potential of the Hamster Arylamine N-Acetyltransferase 2 Catalytic Triad by Site-Directed Mutagenesis of the Proximal Conserved Residue, Tyrosine 190. FEBS J. 276, 6928-6941 (2009).
  • L. Liu, C.R. Wagner and P.E. Hanna. Isoform-Selective Inactivation of Human Arylamine N-Acetyltransferases by Reactive Metabolites of Environmental Arylamines. Chem. Res. Toxicol. 22, 1962-1974 (2009).