Kim Bokyung, Park Ok Kyeung, Bae Ju Young, Jang Tae-ho, Yoon Jong Hwan, Do Kyoung Hun, Kim Byung-Gee, Yun Hyungdon, Park Hyun Ho
School of Biotechnology, Yeungnam University, Gyeongsan, Republic of Korea.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Feb 1;67(Pt 2):231-3. doi: 10.1107/S1744309110050876. Epub 2011 Jan 22.
β-Transaminase (β-TA) catalyzes the transamination reaction between β-aminocarboxylic acids and keto acids. This enzyme is a particularly suitable candidate for use as a biocatalyst for the asymmetric synthesis of enantiochemically pure β-amino acids for pharmaceutical purposes. The β-TA from Mesorhizobium sp. strain LUK (β-TAMs) belongs to a novel class in that it shows β-transaminase activity with a broad and unique substrate specificity. In this study, β-TAMs was overexpressed in Escherichia coli with an engineered C-terminal His tag. β-TAMs was then purified to homogeneity and crystallized at 293 K. X-ray diffraction data were collected to a resolution of 2.5 Å from a crystal that belonged to the orthorhombic space group C222(1), with unit-cell parameters a = 90.91, b = 192.17, c = 52.75 Å.
β-转氨酶（β-TA）催化β-氨基羧酸与酮酸之间的转氨反应。这种酶是用作生物催化剂以不对称合成用于制药目的的对映体纯β-氨基酸的特别合适的候选物。来自中生根瘤菌属菌株LUK的β-TA（β-TAMs）属于一个新类别，因为它表现出具有广泛且独特底物特异性的β-转氨酶活性。在本研究中，β-TAMs在带有工程化C末端His标签的大肠杆菌中过表达。然后将β-TAMs纯化至同质，并在293K下结晶。从属于正交空间群C222(1)、晶胞参数a = 90.91、b = 192.17、c = 52.75 Å的晶体收集了分辨率为2.5 Å的X射线衍射数据。
