title: Saturation mutagenesis in selected amino acids to shift Pseudomonas sp. acidic lipase Lip I.3 substrate specificity and activity.
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.
authors.affiliation: Bioscience Department, Facultad de Química, Universidad de la República (UdelaR), Montevideo, Uruguay. ppanizza@fq.edu.uy.
authors.forename: Paola
authors.initials: P
authors.lastname: Panizza
authors.forename: Silvia
authors.initials: S
authors.lastname: Cesarini
authors.forename: Pilar
authors.initials: P
authors.lastname: Diaz
authors.forename: Sonia
authors.initials: S
authors.lastname: Rodríguez Giordano
mesh_terms: D008049:Lipase / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D008958:Models, Molecular; D016296:Mutagenesis; D009154:Mutation; D011487:Protein Conformation; D011549:Pseudomonas / Q000201:enzymology*; D013379:Substrate Specificity
chemical_list: D008049:Lipase