The University of Arizona

Vahe Bandarian

Assistant Professor of Biochemistry & Molecular Biophysics
Ph.D., University of Wisconsin, Madison

Biosynthesis of secondary metabolites; mechanistic enzymology.

Research Interests

We will utilize tools of chemistry and of biology to elucidate the biosynthetic pathways by which deazapurine-containing metabolites are produced. Deazapurines are widely distributed in nature and play diverse biological functions, such as cofactors in redox reactions and antimicrobial agents. The goals of the research in my laboratory will be to identify the enzymes that catalyze individual steps in the biosynthetic pathways leading to the deazapurine-containing metabolites and to probe the catalytic mechanisms of these enzymes.

Select Publications

Any link on the below references will take you off of the BMCB site and to an abstract of that particular paper.

Poyner, R.R., M.A. Anderson, V. Bandarian, W.W. Cleland, and G.H. Reed. 2006. Probing nitrogen-sensitive steps in the free-radical-mediated deamination of amino alcohols by ethanolamine ammonia-lyase. Journal of the American Chemical Society 128: 7120-7121.

Bandarian, V., and R.G. Matthews. 2004. Measurement of energetics of conformational change in the cobalamin-dependent methionine synthase. Methods in Enzymology 380: 152-169..

Bandarian, V., M.L. Ludwig, and R.G. Matthews. 2003. Factors modulating conformational equilibria in large modular proteins: A case study with cobalamin-dependent methionine synthase Proceedings of the National Academy of Sciences U.S.A. 100: 8156-8163.

Bandarian, V., and G.H. Reed. 2002. Analysis of electron paramagnetic resonance spectrum of a radical intermediate in the coenzyme B(12)-dependent ethanolamine ammonia-lyase catalyzed reaction of S-2-aminopropanol. Biochemistry 41: 8580-8588.

Bandarian, V., K.A. Pattridge, B.W. Lennon, D.P. Huddler, R.G. Matthews, and M.L. Ludwig. 2002. Domain alternation in B(12)-dependent methionine synthase to the activation conformation. Nature Structural Biology 9: 53-56.

Bandarian, V., and R.G. Matthews. 2001. Quantitation of rate enhancements attained by the binding of cobalamin to methionine synthase. Biochemistry 40: 5056-5064.

Miller, J., V. Bandarian, G.H. Reed, and P.A. Frey. 2001. Inhibition of lysine 2,3-aminomutase by the alternative substrate 4-thialysine and characterization of the 4-thialysyl radical intermediate. Archives of Biochemistry and Biophysics 387: 281-287.

LoBrutto, R., V. Bandarian, O.T. Magnusson, X. Chen, V.L. Schramm, and G.H. Reed. 2001. 5'-Deoxyadenosine contacts the substrate radical intermediate in the active site of ethanolamine ammonia-lyase:2H and 13C electron nuclear double resonance studies. Biochemistry 40: 9-14.

Chang, C-W.T., D.A. Johnson, V. Bandarian, H. Zhou, R. LoBrutto, G.H. Reed, and H.-W. Liu. 2000. Characterization of a unique coenzyme B6 radical in the ascarylose biosynthetic pathway. Journal of the American Chemical Society 122: 4239-4240.

Abend, A., V. Bandarian, G.H. Reed, and P.A. Frey. 2000. Identification of cis-ethanesemidione as the organic radical derived from glycolaldehyde in the suicide inactivation of dioldehydrase and of ethanolamine ammonia-lyase. Biochemistry 39: 6250-6257.

Wu, W., S. Booker, K.W. Lieder, V. Bandarian, G.H. Reed, and P.A. Frey. 2000. Lysine 2,3-aminomutase and trans-4,5-dehydrolysine: Characterization of an allylic analogue of a substrate-based radical in the catalytic mechanism. Biochemistry 39: 9561-9570.

Bandarian, V., and G.H. Reed. 2000. Isotope effects in the transient phases of the reaction catalyzed by ethanolamine ammonia-lyase: determination of the number of exchangeable hydrogens in the enzyme-cofactor complex. Biochemistry 39: 12069-12075.

Bandarian, V., and G.H. Reed. 1999. In Vitamin B12 (R. Banerjee, Ed.) John Wiley & Sons, Inc., New York.

Contact Information

    Mailing:
    Vahe Bandarian, Assistant Professor
    Department of Biochemistry & Molecular Biophysics
    University of Arizona
    Biological Sciences West 537A
    P.O. Box 210088
    Tucson, AZ 85721-0088

    Web Site: Home Page

    Telephone:
    520-626-0389 (Office)

    Fax:
    520-626-9204

    Email:
    vahe@email.arizona.edu

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