Structure and activity of the cold-active and anion-activated carboxyl esterase OLEI01171 from the oil-degrading marine bacterium Oleispira antarctica.

@article{Lemak2012StructureAA,
  title={Structure and activity of the cold-active and anion-activated carboxyl esterase OLEI01171 from the oil-degrading marine bacterium Oleispira antarctica.},
  author={S. Lemak and A. Tchigvintsev and Pierre Petit and Robert L Flick and A. Singer and G. Brown and E. Evdokimova and O. Egorova and C. Gonzalez and T. Chernikova and M. Yakimov and M. Kube and R. Reinhardt and P. Golyshin and A. Savchenko and A. Yakunin},
  journal={The Biochemical journal},
  year={2012},
  volume={445 2},
  pages={
          193-203
        }
}
  • S. Lemak, A. Tchigvintsev, +13 authors A. Yakunin
  • Published 2012
  • Chemistry, Medicine
  • The Biochemical journal
  • The uncharacterized α/β-hydrolase protein OLEI01171 from the psychrophilic marine bacterium Oleispira antarctica belongs to the PF00756 family of putative esterases, which also includes human esterase D. In the present paper we show that purified recombinant OLEI01171 exhibits high esterase activity against the model esterase substrate α-naphthyl acetate at 5-30°C with maximal activity at 15-20°C. The esterase activity of OLEI01171 was stimulated 3-8-fold by the addition of chloride or several… CONTINUE READING
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