Saturation mutagenesis in selected amino acids to shift Pseudomonas sp. acidic lipase Lip I.3 substrate specificity and activity.

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Abstract

Several Pseudomonas sp. CR611 Lip I.3 mutants with overall increased activity and a shift towards longer chain substrates were constructed. Substitution of residues Y29 and W310 by smaller amino acids provided increased activity on C18-substrates. Residues G152 and S154, modified to study their influence on interfacial activation, displayed a five and eleven fold increased activity.

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Journal

Journal ID (iso-abbrev): Chem. Commun. (Camb.)

Title: Chemical communications (Cambridge, England)

ISSN (Electronic): 1364-548X

ISSN (Print): 1359-7345

Publication date (Electronic): Jan 25 2015

Volume: 51

Issue: 7

Affiliations

[1 ] Bioscience Department, Facultad de Química, Universidad de la República (UdelaR), Montevideo, Uruguay. ppanizza@fq.edu.uy.

Article

DOI: 10.1039/c4cc08477b

PubMed ID: 25482450

SO-VID: 64f5ab48-a449-463d-9b27-546791894458

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