Crystallization and preliminary X-ray crystallographic studies of beta-transaminase from Mesorhizobium sp strain LUK
- Crystallization and preliminary X-ray crystallographic studies of beta-transaminase from Mesorhizobium sp strain LUK
- 박현호; 김보경[김보경]; 박옥경[박옥경]; 배주영[배주영]; 장태호[장태호]; 윤종환[윤종환]; 도경훈[도경훈]; 김병기[김병기]; 윤형돈
- AMINO ACIDS; PYRUVATE TRANSAMINASE; CRYSTAL-STRUCTURE; AMINOTRANSFERASES; INHIBITOR; PEPTIDES; CLONING
- Issue Date
- ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS, v.67, pp.231 - 233
- beta-Transaminase (beta-TA) catalyzes the transamination reaction between beta-aminocarboxylic acids and keto acids. This enzyme is a particularly suitable candidate for use as a biocatalyst for the asymmetric synthesis of enantio-chemically pure beta-amino acids for pharmaceutical purposes. The beta-TA from Mesorhizobium sp. strain LUK (beta-TAMs) belongs to a novel class in that it shows beta-transaminase activity with a broad and unique substrate specificity. In this study, beta-TAMs was overexpressed in Escherichia coli with an engineered C-terminal His tag. beta-TAMs was then purified to homogeneity and crystallized at 293 K. X-ray diffraction data were collected to a resolution of 2.5 angstrom from a crystal that belonged to the orthorhombic space group C222(1), with unit-cell parameters a = 90.91, b = 192.17, c = 52.75 angstrom.
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