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Hyungdon YUN 한국생물공학회 2021 한국생물공학회 학술대회 Vol.2021 No.10
Optically pure unnatural amino acids including beta- and gamma- amino acids are crucial active intermediates frequently used in the industrial synthesis of a range of chemicals and pharmaceuticals. Over time, numerous biocatalytic routes catalyzed by lipase, amidases, acylases, nitrilases, hydantoinases, ammonia lyases, aldolases, and amino acid dehydrogenase have been developed to access to chiral beta- and g- amino acids. Each enzyme catalyzed reaction has its advantages and limitations. The development of an efficient biocatalytic process for chiral unnatural amino acids remains a challenging task. The toolbox of transaminase (TA) is rapidly expanding, since they possess many benefits over other enzymes including broad substrate specificity, high enantioselectivity and no requirement for cofactor regeneration. beta-TA can reversibly transfer amino group from beta- and gamma-amino acids as well as amines onto amine acceptor such as pyruvate. To the best of our knowledge naturally occurring (R)-beta-TAs reactive for various beta - and gamma-amino acids has not yet been discovered, despite many (S)-beta-TAs have been reported. Therefore, creating (R)-beta-TA with broad substrate specificity and high catalytic efficiency is desperately needed for the synthesis of chiral beta- and gamma- amino acids. we have successfully created an (R)- beta-TA, not yet found in nature through the hybridizing of DATA and (R)-ATA created from DATA, and subsequent ISM-based directed evolution of the hybrid.