Vahe Bandarian
Assistant Professor of Biochemistry and Molecular Biophysics
Ph.D. 1998, 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.

Recent publications

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

Bandarian, V. and Reed, G. H. (2000) Kinetic isotope effects in the transient phases of the reaction catalyzed by ethanolamine ammonia-lyase, Biochemistry 39, 12069-12075.

Wu, W., Booker, S., Lieder, K. W., Bandarian, V., Reed, G. H. (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.

Abend, A., Bandarian, V., Reed, G. H., and Frey, P. A (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.

Chang, C-w. T., Johnson, D. A., Bandarian, V., Zhou, H., LoBrutto, R., Reed, G. H., and Liu, H.-w. (2000) Characterization of a unique coenzyme B₆ radical in the ascarylose biosynthetic pathway, J. Amer. Chem. Soc. 122, 4239-4240.

LoBrutto, R., Bandarian, V., Magnusson, O. Th., Chen, X., Schramm, V. L., and Reed, G. H. (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.

Miller, J., Bandarian, V., Reed, G. H., and Frey, P. A. (2001) Inhibition of lysine 2,3-aminomutase by the alternative substrate 4-thialysine and characterization of the 4-thialysyl radical intermediate, Arch. Biochem. Biophys. 387, 281-287.

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

Bandarian, V., Pattridge, K. A., Lennon, B. W., Huddler, D. P., Matthews, R. G., and Ludwig, M. L. (2002) Domain alternation in B₁₂-dependent methionine synthase: Switching to the activation conformation. Nature Struct. Biol. 9, 53-56.

Bandarian, V. and Reed, G. H. (2002) Analysis of electron paramagnetic resonance spectrum of a radical intermediate in the coenzyme B₁₂-dependent ethanolamine ammonia-lyase reaction with S-propanolamine, Biochemistry 41, 8580-8588.

Bandarian, V., Ludwig, M. L., and Matthews, R. G. (2003) Factors modulating conformational equilibria in large modular proteins: A case study with cobalamin-dependent methionine synthase, Proc. Natl. Acad. Sci. USA 100, 8156-8163.

Bandarian, V. and Matthews, R. G. (2003) Measurement of energetics of conformational change in the cobalamin-dependent methionine synthase in Methods in Enzymology, 151-170.

Matthews, R. G., Smith, A. E., Zhou, Z. H. S., Taurog, R. E., Bandarian, V., Evans, J. C., Ludwig, M. L. (2003) Cobalamin-dependent and cobalamin-indepenent methionine synthases: Are there two solutions to the same chemical problem? Helv. Chim. Acta 86, 3939-3954.

Contact Information

Mailing:
Dr. Vahe Bandarian, Assistant Professor
Department of Biochemistry & Molecular Biophysics
University of Arizona
1041 E. Lowell Street
Biosciences West 537A
Tucson AZ 85721-0088

Telephone: 520-626-0389
Fax: 520-626-9204

vahe@email.arizona.edu

Biological Sciences West
1041 East Lowell Street
P.O. Box 210088 · Tucson, AZ 85721-0088
Tel: (520) 621-5110
FAX (520) 626-9204

Life Sciences South
1007 East Lowell Street
P.O. Box 210106 · Tucson, AZ 85721-0106
FAX (520) 621-3709