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• Cloning, expression, and biochemical characterization of a coldactive GDSL-esterase of a Pseudomonas sp. S9 isolated from Spitsbergen island soil

  Publikacja

  • M. Wicka-Grochocka
  • M. Wanarska
  • E. Krajewska
  • A. Pawlak-Szukalska
  • J. Kur
  • H. Cieśliński

  - Acta Biochimica Polonica - Rok 2016

  An estS9 gene, encoding an esterase of the psychrotolerant bacterium Pseudomonas sp. S9 was cloned and sequenced. The deduced sequence revealed a protein of 636 amino acid residues with a molecular mass of 69 kDa.Further amino acid sequence analysis revealed that the EstS9 enzyme contained a G-D-S-L motif centered at a catalytic serine, an N-terminal catalytic domain and a C-terminal autotransporter domain. Two recombinant E. coli...

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