원문정보
초록
영어
ω-Transaminase has a great potential in pharmaceutical industry due to its ability to synthesize chiral amines and amino acids that are used as intermediate for chiral drugs. However size constraints in the active site pocket of ω-transaminase limits production of various enantiopure amino acids. To overcome this stringency of substrate specificity, protein engineering was applied. From the docking model, a single point mutations were introduced to the active site residue to expand the small pocket. The resulting mutants showed enhanced activity toward keto acids, amino acids, and amines carrying bulky substituents. This work was supported by the Advanced Biomass R&D Center (ABC- 2010-0029737) and the Basic Science Research Program (2010-0024448) through the National Research Foundation of Korea funded by the Ministry of Education, Science and Technology.