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