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

ABSTRACT: ?-Transaminase (?-TA) catalyzes the transamination reaction between ?-aminocarboxylic acids and keto acids. This enzyme is a particularly suitable candidate for use as a biocatalyst for the asymmetric synthesis of enantiochemically pure ?-amino acids for pharmaceutical purposes. The ?-TA from Mesorhizobium sp. strain LUK (?-TAMs) belongs to a novel class in that it shows ?-transaminase activity with a broad and unique substrate specificity. In this study, ?-TAMs was overexpressed in Escherichia coli with an engineered C-terminal His tag. ?-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.

SUBMITTER: Kim B 

PROVIDER: S-EPMC3034615 | biostudies-literature | 2011 Feb

REPOSITORIES: biostudies-literature

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

Kim Bokyung B   Park Ok Kyeung OK   Bae Ju Young JY   Jang Tae-ho TH   Yoon Jong Hwan JH   Do Kyoung Hun KH   Kim Byung-Gee BG   Yun Hyungdon H   Park Hyun Ho HH  

Acta crystallographica. Section F, Structural biology and crystallization communications 20110122 Pt 2

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  ...[more]

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