Crystallization and preliminary X-ray crystallographic studies of ω-transaminase from Vibrio fluvialis JS17.
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.
Jang
Tae-ho
TH
School of Biotechnology and Graduate School of Biochemistry at Yeungnam University, Gyeongsan, Republic of Korea.
Kim
Bokyung
B
Park
Ok Kyoung
OK
Bae
Ju Young
JY
Kim
Byung-Gee
BG
Yun
Hyungdon
H
Park
Hyun Ho
HH
D003460:Crystallization; D018360:Crystallography, X-Ray; D000637:Transaminases / Q000737:chemistry*; D014733:Vibrio / Q000201:enzymology*
D000637:Transaminases