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My research interests focus on the enzyme Aldehyde Dehydrogenase (ALDH). ALDHs catalyze the oxidation of aldehydes to their corresponding carboxylic acids coupled with reduction of NAD or NADP to NADH or NADPH, respectively. ALDHs occur throughout all phyla of life. Many disparate aldehydes are ubiquitous in nature and most are toxic at low levels because of their chemical reactivity. Thus, levels of metabolic-intermediate and environmental aldehydes must be carefully regulated. For this, most well studied organisms are known to have several distinct ALDHs which take part in a variety of physiological roles. which is central to the detoxification of alcohol, xenobiotics and several chemotherapeutic agents in the human body. Through analysis of a large protein sequence alignment (145 sequences) by this investigator, a large number of important conserved amino acid residues were identified in the ALDH extended family. In collaboration with the University of Pittsburgh, the activity of these residues is being explored via site-directed mutagenesis of the rat class 3 ALDH, providing students with skills in molecular biology, protein biochemistry and enzyme kinetics.
Another area of research interest is the growing field of bioinformatics. Modern sequence databases possess a large amount of untapped information. Student research projects involve performing multiple protein sequence alignments of certain proteins and/or protein families. From these alignments and comparisons to known tertiary structures, the identities and potential functions of conserved residues will be proposed. Also the evolutionary relationships between proteins from distinct species will be evaluated.
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