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Crystallization and preliminary X-ray crystallographic studies of ?-transaminase from Vibrio fluvialis JS17.

ABSTRACT: Omega-transaminase (?-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. ?-TA from Vibrio fluvialis JS17 (?-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. ?-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.

SUBMITTER: Jang TH

PROVIDER: S-EPMC2917292 | biostudies-literature | 2010 Aug

REPOSITORIES: biostudies-literature

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Crystallization and preliminary X-ray crystallographic studies of ω-transaminase from Vibrio fluvialis JS17.

Jang Tae-ho TH Kim Bokyung B Park Ok Kyoung OK Bae Ju Young JY Kim Byung-Gee BG Yun Hyungdon H Park Hyun Ho HH

Acta crystallographica. Section F, Structural biology and crystallization communications 20100729 Pt 8

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 d ...[more]

PMID: 20693669

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