期刊
FEBS LETTERS
卷 579, 期 11, 页码 2383-2386出版社
WILEY
DOI: 10.1016/j.febslet.2005.03.037
关键词
lipase; chain length selectivity; thermo stability; Pseudomonas fragi
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. (c) 2005 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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