Georgia Institute of TechnologyChemistry & Biochemistry
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Sheldon W. May

Sheldon W. May

Regents' Professor; Associate Director, Georgia Tech Institute for Bioengineering and Biosciences (IB2); Director, Georgia Tech Bioscience Center


Office: IBB 3307

Phone: 404-894-4052

Fax: 404-894-7452

E-mail Sheldon W. May

 

B.S., Roosevelt University, 1966; Ph.D., The University of Chicago, 1970

Research Interests

Professor May is interested in rational, molecularly based approaches to problems in neurochemistry, in the development of novel enzyme effectors such as suicide substrates and transition state analogs, and in basic mechanistic studies on enzymes involved in the biosynthesis, metabolism, interconversion and regulation of neurotransmitters, neuroregulators and biologically active neuropeptides and peptide hormones. Both chemical and physical techniques are being used to investigate the structure and reactivity of these enzymes, and detailed stereochemical and structural studies on substrates, products, and inhibitors are being pursued. In addition, pharmacological techniques are being utilized in order to evaluate the action of novel enzyme effectors on cardiovascular and neurological functions. Dr. May's group has established a special cell culture laboratory which is used extensively in their neurochemical work.

In 1990, Professor May's group discovered a new enzyme, which has been named Peptidylamidoglycolate Lyase (PGL). This enzyme has been officially recognized by the Enzyme Nomenclature Commission of the International Union of Biochemistry, who have assigned to it the E.C. number 4.3.2.5. PGL, which carries out the final post-translational modification step (C-terminal amidation) essential to the biological activity of most peptide hormones, is being extensively investigated in Dr. May's lab.

Another area of activity is biotechnology, with particular emphasis on the production of "designer' biopolymers and on enzyme technology. Efforts are being directed toward the enzymatic and microbial production of new biopolymers with desirable properties, and toward the application of enzymes and microbial preparations to carry out chemical conversions that are difficult to accomplish in a synthetic sense. These studies in enzyme technology involve work with both soluble and immobilized enzyme systems as well as unusual aspects of fermentation technology such as hydrocarbon fermentation and continuous culture.

Representative Publications

"Iso-coenzyme A," K. L. Burns, L. T. Gelbaum, M. C. Sullards, D. E. Bostwick, S. W. May, J. Biol. Chem., 2005, 280 (17), 16550-16558.

"Reversal of the transformed phenotype and inhibition of peptidylglycine alpha-monooxygenase in Ras-transformed cells by 4-phenyl-3-butenoic acid," J. A. Sunman, M. S. Foster, S. L. Folse, S. W. May, D. F. Matesic, Molec. Carcinog., 2004, 41 (4), 231-246.

"Analysis of organoselenium compounds in human urine using active carbon and chemically modified silica sol-gel surface-assisted laser desorption/ionization high-resolution time-of-flight mass spectrometry," T. T. Hoang, Y. F. Chen, S. W. May, R. F. Browner, Anal. Chem., 2004, 76 (7), 2062-2070.

"Selenium redox cycling in the protective effects of organoselenides against oxidant-induced DNA damage," V. De Silva, M. M. Woznichak, K. L. Burns, K. B. Grant, S. W. May, J. Am. Chem. Soc., 2004, 126 (8), 2409-2413.

"Catalysis, stereochemistry, and inhibition of ureidoglycolate lyase," J. K. McIninch, J. D. McIninch, S. W. May, J. Biol. Chem., 2003, 278, 50091-50100.

"Separation methods applicable to the evaluation of enzyme-inhibitor and enzyme-substrate interactions," K. L. Burns, S. W. May, J. Chromotogr., 2003, B 797, 175-190.

"Developments with the oscillating capillary nebulizer - effects of spray chamber design, droplet size and turbulence on analytical signals and analyte transport efficiency of selected biochemically important organoselenium compounds," T. T. Hoang, S. W. May, R. F. Browner, J. Anal. At. Spectrom., 2002, 17, DOI: 10.1039/b204625n.

"High-performance liquid chromatographic enantiomeric separation of an enzyme inhibitor which possesses both a chiral center and tautomeric moieties," J. Feng, S. W. May, J. Chromatogr. A, 2001, 905, 103-109.

"Reaction of phenylaminoethyl selenides with peroxynitrite and hydrogen peroxide," M. M. Woznichak, J. D. Overcast, K. Robertson, H. M. Neumann, S. W. May, Archives Biochemistry & Biophysics, 2000, 379, 314-320.

"Vascular and endothelial actions of inhibitors of substance P amidation," G. A. Abou-Mohamed, J. Huang, C. D. Oldham, T. A. Taylor, L. Jin, R. B. Caldwell, S. W. May, R. W. Caldwell, J. Cardiovascular Pharmacology, 2000, 35, 871-880.

"Kinetic and stereochemical studies on novel inactivators of carboxyl-terminal amidation," J. Feng, J. Shi, S. R. Sirimanne, C. E. Mounier-Lee, S. W. May, Biochemical J., 2000, 350, 521-530.

"The Ninth European Congress on Biotechnology; an introduction," S. W. May, Enzyme & Microbial Technology, 2000, 27, 733.

"Liquid chromatography/electrospray mass spectrometry of organoselenium compunds with postcolumn crown ether complexation," W. Z. Shou, M. W. Woznichak, S. W. May, R. F. Browner, Anal. Chem., 2000, 72, 3266-3271.