People & Research

Minae Mure

Associate Professor

Minae Mure photo

1251 Wescoe Hall Drive
Malott Hall, Room 6079
University of Kansas
Lawrence, KS 66045

Phone: (785) 864-2901

Fax: (785) 864-5396


Academic Degrees

  • Ph.D., 1990, Osaka University
  • M.S., 1988, Osaka University
  • B.S., 1985, Osaka University
  • Visiting Postdoctoral Scholar, 1990-1994, University of California, Berkeley
  • Research Associate Specialist, 2002-2004, University of California, Berkeley


  • NSF CAREER MCB-0747377 ”Mechanistic studies of tyrosine derived cofactors”

Areas of Specialization

Bioanalytical and Bioinorganic Chemistry

Research Interests

Understanding the chemistry and biological functions of enzymes.

Quinones are highly reactive in solution and are used as catalysts and electron-transfer mediators. However, this reactivity also means that some are very toxic. Nature has found ways to control and take advantage of the chemical potential of quinones by encapsulating them inside of proteins to provide the optimal environment for catalysis. There is a family of enzymes that contain quinones as their organic cofactors that catalyze the oxidation of biogenic amines, alcohols and sugars. These enzymes are called quinoproteins and they are ubiquitous. Humans have at least two types of quinoproteins that are crucial for cellular integrity and development, biological signal transduction, neurotransmitter metabolism, and connective tissue formation. Aberrant expression levels of these proteins are linked to health problems and diseases such as cancer, fibrosis and diabetes. We are interested in understanding the mechanism of these enzymes at the chemistry/biology interface. A combination of techniques (organic synthesis, biochemistry, spectroscopy, electrochemistry, molecular cell biology, developmental biology) will be applied. An understanding the mechanism will lead to the development of specific inhibitors that will have a high chance of producing therapeutic agents.

Selected publications

  1. “A General Protease Digestion Procedure for Optimal Protein Sequence Coverage and PTM Analysis of Recombinant Glycoproteins: Application to the Characterization of hLOXL2 Glycosylation” Rebecchi, K.R., Go, E. P., Xu, L., Woodin, C. L., Mure, M., and Desaire, H. Anal. Chem. 83(22), 8484-8491 (2011)
  2. "Kinetic and Structural Analysis of Substrate Specificity in Two Copper Amine Oxidases from Hansenula polymorpha" Chang, C. M., Klema, V. J., Johnson, B. J., Mure, M., Klinman, J. P., and Wilmot, C. M. Biochemistry, 49, 2540-2550 (2010)
  3. "Crystal Structure of Histamine Dehydrogenase from Nocardioides simplex" Reed, T., Lushington, G. H., Xia, Y., Hirakawa, H., Travis, D. M., Mure, M., Scott, E. E., and Limburg, J. J. Biol. Chem. 285(33) 25782-25791 (2010)
  4. “Chapter 3. Cofactors: Copper and TPQ” Mure, M. in “Copper amine oxidases: structures, catalytic mechanisms, and role in pathophysiology” edited by Floris, G. Mondovi B. CRC Press, Boca Raton, FL (2009)
  5. “Expression, Purification, Crystallization and Preliminary X-ray Studies of Histamine Dehydroganase from Nocardioides simplex” Reed, TM. Hirakawa, H. Mure, M. Scott, EE. and Limburg, J. Acta Crystallogr. Sect. F. Struct. Biol. Cryst. Commun. 64, 785-787 (2008)
    "Hydrazines and Amphetamine Binding to Amine Oxidase: Old Drugs with New Prospects" Knowles, P., Kurtis, C., Murray, J., Saysell, C., Tambyrajah, W. Wilmot, C., McPherson, M., Phillips, S., Dooley, D., Brown, D., Rogers, M. and Mure, M. J. Neural. Trans. 114, 743-746 (2007)
  6. "Trapping a Dopaquinone Intermediate in the TPQ Cofactor Biogenesis in a Copper-Containing Amine Oxidase from Arthrobacter globiformis" Moore, R. H., Spies, M. A., Culpepper, M.B., Murakawa, T., Hirota, S. Okajima, T., Tanizawa, K. and Mure, M. J. Am. Chem. Soc. 129, 11524-11534 (2007)
  7. "Active Site Rearrangement of the 2-Hydrazinopyridine Adduct in E. coli Amine Oxidase to an Azo Cu(II) Chelate form: A Key Role for Y369 in Controlling the Mobility of the TPQ-2HP Adduct ", Mure, M., Kurtis, C. R., Brown, D. E., Rogers, M., Wilmot, C. M., Parsons, M., Phillips, S. E. V., McPherson, M. J., Knowles, P. F. and Dooley, D. M. Biochemistry 44, 1583-1594 (2005)
  8. "Role of the Interactions between the Active Site Base and the Substrate Schiff Base in Amine Oxidase Catalysis.  Evidence from Structural and Spectroscopic Studies of the 2-Hydrazinopyridine Adduct of E. coli Amine Oxidase."  Mure, M., Brown, D. E., Saysell, C., Kurtis, C. R., Rogers, M., Wilmot, C. M., Phillips, S. E. V., McPherson, M. J., Knowles, P. F. and Dooley, D. M. Biochemistry 44, 1568-1582 (2005)

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