Jang Tae-ho, Kim Bokyung, Park Ok Kyoung, Bae Ju Young, Kim Byung-Gee, Yun Hyungdon, Park Hyun Ho
School of Biotechnology and Graduate School of Biochemistry at Yeungnam University, Gyeongsan, Republic of Korea.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Aug 1;66(Pt 8):923-5. doi: 10.1107/S1744309110021573. Epub 2010 Jul 29.
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.
ω-转氨酶(ω-TA)催化将氨基从非α位氨基酸或无羧基的胺化合物转移至氨基受体。河流弧菌JS17的ω-TA(ω-TAVf)是一种新型胺:丙酮酸转氨酶,能够对芳基手性胺进行立体选择性转氨作用。在本研究中,ω-TAVf在带有工程化C端组氨酸标签的大肠杆菌中过表达。然后将ω-TAVf纯化至同质,并在292 K下结晶。从属于正交空间群P2(1)2(1)2(1)、晶胞参数a=78.43、b=95.95、c=122.89 Å的晶体收集到分辨率为2.5 Å的X射线衍射数据。