Earticle

초록

영어

ω-Aminotransferase (ωAT) is an interesting biocatalyst for the preparation of chiral amines which are widely used as building blocks for pharmaceuticals, agrochemicals and fine chemicals. With the assumption that substrate and sequence spaces are in the process of co-evolution, we explored sequences space to screen the enzymes showing activity to new target compounds. 527 bacterial genome sequences were analyzed by the profiles of subgroups in aminotransferase group II including ornithine aminotransferase (orAT), acetylornithine aminotransferase (aoAT), ω-aminotransferase (ωAT), γ-aminobutyrate aminotransferase (GABAAT) and 7,8-diaminopelargonate aminotransferase (DAPAAT). We selected the sequences having a Z-score of 0~1.8 to guarantee the ωAT reaction and to avoid the typical ωAT sequences. Among the selected sequences, we filtered out the sequences having very low Z-scores for the rest of four subgroups in aminotransferase group II to consider the diversity. For the selected sequences, we performed protein-ligand docking simulations to predict the docking pose of amino acceptor. Throughout all the analysis procedures, several candidate aminotransferase sequences for the asymmetric synthesis of chiral amines were obtained. An efficient procedure for virtual screening of novel enzymes was demonstrated.

저자

• Joo-Hyun SEO [ School of Chemical and Biological Engineering, Seoul National University ]
• Hyung-Yeon PARK [ Department of Chemistry, Inha University ]
• Juhan KIM [ Cooperative Institute for Research in Environmental Sciences, University of Colorado ]
• Bon-Su LEE [ Department of Chemistry, Inha University ]
• Byung-Gee KIM [ School of Chemical and Biological Engineering, Seoul National University ]

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간행물

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• 간행물명

  한국생물공학회 학술대회

• 간기

  반년간

• 수록기간

  1985~2013

• 십진분류

  KDC 476 DDC 576