Date: 2009. 6. 11, 5:00 PM Place: Mogam Hall, Bldg 500 - Abstract - Transaminase plays a vital role in aminoacid metabolism in a cell, where the transfer of aminogroup of amino donors to keto group of amino acceptors occurs frequently. Its features such as several superfamilies, broad substrate specificity, high reaction rate, no need of external cofactors except pyridoxal phosphate and wide applicability in the preparation of enantiomerically pure natural and non-natural aminoacids, amino alcohols and amines, etc. make it very attractive biocatalyst for industrial preparation. As demand for enantiomerically pure compounds, especially with amino functional group, from chemical and pharmaceutical industries is still in its infancy, transaminase coupled with other enzymes can be widely used to prepare a variety of such chemicals. This talk will introduce some of such examples to produce chiral compounds and non-natural amino acids using aminotransferase and other coupled enzymes. In addition, since microbial genome data are being accumulated very rapidly, proper usage of such immense data information gives new dimensions in finding new transaminases for new desirable substrates and reactions. We will discuss how such transaminases can be efficiently screened by using subprofile analysis, homology modeling, and 3-D protein-ligand docking, and the selected enzymes can be used for the production of chiral amines, non-natural amino acids and amino alcohols by enzyme reaction engineering.