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B6db references: 20693669

type Journal Article
authors Jang TH, Kim B, Park OK, Bae JY, Kim BG, Yun H, Park HH.
title Crystallization and preliminary X-ray crystallographic studies of ω-transaminase from Vibrio fluvialis JS17
journal Acta Crystallogr Sect F Struct Biol Cryst Commun
Activity amine.transaminase
Family amine.transaminase
sel unselected
ui 20693669
year (2010)
volume 66
number 8
pages 923-5
keywords Biocatalysis; Chiral aminodiols; omega-Transaminase; alpha-Methylbenzylamine; Asymmetric synthesis
abstract Omega-transaminase (ω-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. ω-TA from Vibrio fluvialis JS17 (ω-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. ω-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.
last changed 2011/04/14 10:16

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