Send to

Choose Destination
FEBS Lett. 2005 Apr 25;579(11):2383-6.

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

Author information

Dipartimento di Biotecnologie e Bioscienze, Università degli Studi di Milano-Bicocca, Italy.


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-length preference profile, increasing the relative activity towards C8 substrates. Moreover, mutations conferred to PFL higher temperature stability. On the other hand, replacement of the serine at position 141 by glycine destabilized the protein.

[Indexed for MEDLINE]
Free full text

Supplemental Content

Full text links

Icon for Wiley
Loading ...
Support Center