Biochemical properties and crystal structure of a β-phenylalanine aminotransferase from Variovorax paradoxus.

@article{Crismaru2013BiochemicalPA,
  title={Biochemical properties and crystal structure of a β-phenylalanine aminotransferase from Variovorax paradoxus.},
  author={Ciprian G. Crismaru and Gjalt G. Wybenga and Wiktor Szymański and Hein J. Wijma and Bian Wu and Sebastian Bartsch and Stefaan de Wildeman and Gerrit J Poelarends and Ben L Feringa and Bauke W Dijkstra and Dick B. Janssen},
  journal={Applied and environmental microbiology},
  year={2013},
  volume={79 1},
  pages={185-95}
}
By selective enrichment, we isolated a bacterium that can use β-phenylalanine as a sole nitrogen source. It was identified by 16S rRNA gene sequencing as a strain of Variovorax paradoxus. Enzyme assays revealed an aminotransferase activity. Partial genome sequencing and screening of a cosmid DNA library resulted in the identification of a 1,302-bp aminotransferase gene, which encodes a 46,416-Da protein. The gene was cloned and overexpressed in Escherichia coli. The recombinant enzyme was… CONTINUE READING

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