Crystallization and preliminary X-ray crystallographic studies of omega-transaminase from Vibrio fluvialis JS17
- Crystallization and preliminary X-ray crystallographic studies of omega-transaminase from Vibrio fluvialis JS17
- 박현호; 장태호; 김보경; 박옥경; 배주영; 김병기[김병기]; 윤형돈
- CRYSTAL-STRUCTURE; PYRUVATE AMINOTRANSFERASE; AMINO ACID; KINETIC RESOLUTION; ASPARTATE-AMINOTRANSFERASE; SUBSTRATE-SPECIFICITY; DIRECTED EVOLUTION; ESCHERICHIA-COLI; INHIBITION; MODE
- Issue Date
- ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS, v.66, pp.923 - 925
- Omega-transaminase (omega-TA) catalyzes the transfer of an amino group from a non-alpha-position amino acid or an amine compound with no carboxylic group to an amino acceptor. omega-TA from Vibrio fluvialis JS17 (omega-TAVf) is a novel amine:pyruvate transaminase that is capable of stereoselective transamination of aryl chiral amines. In this study, omega-TAVf was overexpressed in Escherichia coli with engineered C-terminal His tags. omega-TAVf was then purified to homogeneity and crystallized at 292 K. X-ray diffraction data were collected to a resolution of 2.5 A from a crystal belonging to the orthorhombic space group P2(1)2(1)2(1), with unit-cell parameters a = 78.43, b = 95.95, c = 122.89 A.
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