Contribution of cutinase serine 42 side chain to the stabilization of the oxyanion transition state.

@article{Nicolas1996ContributionOC,
  title={Contribution of cutinase serine 42 side chain to the stabilization of the oxyanion transition state.},
  author={Alain Nicolas and Maarten R. Egmond and Cornelis T Verrips and Jacob de Vlieg and Sonia Longhi and Christian Cambillau and Chrislaine Martinez},
  journal={Biochemistry},
  year={1996},
  volume={35 2},
  pages={398-410}
}
Cutinase from the fungus Fusarium solani pisi is a lipolytic enzyme able to hydrolyze both aggregated and soluble substrates. It therefore provides a powerful tool for probing the mechanisms underlying lipid hydrolysis. Lipolytic enzymes have a catalytic machinery similar to those present in serine proteinases. It is characterized by the triad Ser, His, and Asp (Glu) residues, by an oxyanion binding site that stabilizes the transition state via hydrogen bonds with two main chain amide groups… CONTINUE READING

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