Mutations in the "lid" region affect chain length specificity and thermostability of a Pseudomonas fragi lipase.

@article{Santarossa2005MutationsIT,
  title={Mutations in the "lid" region affect chain length specificity and thermostability of a Pseudomonas fragi lipase.},
  author={Gianluca Santarossa and Pietro Gatti Lafranconi and Claudia Alquati and Luca Degioia and Lilia Alberghina and Piercarlo Fantucci and Marina Lotti},
  journal={FEBS letters},
  year={2005},
  volume={579 11},
  pages={2383-6}
}
The cold-adapted Pseudomonas fragi lipase (PFL) displays highest activity on short-chain triglyceride substrates and is rapidly inactivated at moderate temperature. Sequence and structure comparison with homologous lipases endowed with different substrate specificity and stability, pointed to three polar residues in the lid region, that were replaced with the amino acids conserved at equivalent positions in the reference lipases. Substitutions at residues T137 and T138 modified the lipase chain… CONTINUE READING

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