Crystallization and preliminary X-ray crystallographic studies of β-transaminase from Mesorhizobium sp strain LUK

被引：4

作者：

Kim, Bokyung ^{[1
]}

Park, Ok Kyeung ^{[2
]}

Bae, Ju Young ^{[2
]}

Jang, Tae-ho ^{[2
]}

Yoon, Jong Hwan ^{[1
]}

Do, Kyoung Hun ^{[1
]}

Kim, Byung-Gee ^{[3
,4
]}

Yun, Hyungdon ^{[1
]}

Park, Hyun Ho ^{[1
,2
]}

机构：

[1] Yeungnam Univ, Sch Biotechnol, Gyongsan, South Korea

[2] Yeungnam Univ, Grad Sch Biochem, Gyongsan, South Korea

[3] Seoul Natl Univ, Inst Mol Biol & Genet, Seoul 151742, South Korea

[4] Seoul Natl Univ, Sch Chem & Biol Engn, Seoul 151742, South Korea

来源：

ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY COMMUNICATIONS | 2011年 / 67卷

关键词：

AMINO ACIDS; PYRUVATE TRANSAMINASE; CRYSTAL-STRUCTURE; AMINOTRANSFERASES; INHIBITOR; PEPTIDES; CLONING;

D O I：

10.1107/S1744309110050876

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

beta-Transaminase (beta-TA) catalyzes the transamination reaction between beta-aminocarboxylic acids and keto acids. This enzyme is a particularly suitable candidate for use as a biocatalyst for the asymmetric synthesis of enantio-chemically pure beta-amino acids for pharmaceutical purposes. The beta-TA from Mesorhizobium sp. strain LUK (beta-TAMs) belongs to a novel class in that it shows beta-transaminase activity with a broad and unique substrate specificity. In this study, beta-TAMs was overexpressed in Escherichia coli with an engineered C-terminal His tag. beta-TAMs was then purified to homogeneity and crystallized at 293 K. X-ray diffraction data were collected to a resolution of 2.5 angstrom 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 angstrom.

引用

页码：231 / 233

页数：3

共 23 条

[1] Crystallography & NMR system:: A new software suite for macromolecular structure determination [J].