|
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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