E-resources
Peer reviewed
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Hwang, B.Y. (Seoul National University, Seoul, Republic of Korea); Ko, S.H. (Seoul National University, Seoul, Republic of Korea); Park, H.Y. (Inha University, Incheon, Republic of Korea); Seo, J.H. (Seoul National University, Seoul, Republic of Korea); Lee, B.S. (Inha University, Incheon, Republic of Korea); Kim, B.G. (Seoul National University, Seoul, Republic of Korea), E-mail: byungkim@snu.ac.kr
Journal of microbiology and biotechnology, 01/2008, Volume: 18, Issue: 1Journal Article
A putative ω-aminotransferase gene, cc3143 (aptA), from Caulobacter crescentus was screened by bioinformatical tools and overexpressed in E. coli, and the substrate specificity of the ω-aminotransferase was investigated. AptA showed high activity for short-chain β-amino acids. It showed the highest activity for 3-amino-n-butyric acid. It showed higher activity toward aromatic amines than aliphatic amines. The 3D model of the ω-aminotransferase was constructed by homology modeling using a dialkylglycine decarboxylase (PDB ID: 1DGE) as a template. Then, the ω-aminotransferase was rationally redesigned to increase the activity for 3-amino-3-phenylpropionic acid. The mutants N285A and V227G increased the relative activity for 3-amino-3-phenylpropionic acid to 3-amino-n-butyric acid by 11-fold and 3-fold, respectively, over that of wild type.
