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

Title
Crystallization and preliminary X-ray crystallographic studies of beta-transaminase from Mesorhizobium sp strain LUK
Author(s)
박현호김보경[김보경]박옥경[박옥경]배주영[배주영]장태호[장태호]윤종환[윤종환]도경훈[도경훈]김병기[김병기]윤형돈
Keywords
AMINO ACIDS; PYRUVATE TRANSAMINASE; CRYSTAL-STRUCTURE; AMINOTRANSFERASES; INHIBITOR; PEPTIDES; CLONING
Issue Date
201101
Publisher
WILEY-BLACKWELL
Citation
ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS, v.67, pp.231 - 233
Abstract
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.
URI
http://hdl.handle.net/YU.REPOSITORY/25753http://dx.doi.org/10.1107/S1744309110050876
ISSN
1744-3091
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이과대학 > 화학생화학부 > Articles
생명공학부 > 생명공학부 > Articles
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