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

Chem Commun (Camb). 2015 Jan 25;51(7):1330-3. doi: 10.1039/c4cc08477b.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Lipase / chemistry*
  • Lipase / genetics
  • Lipase / metabolism*
  • Models, Molecular
  • Mutagenesis*
  • Mutation
  • Protein Conformation
  • Pseudomonas / enzymology*
  • Substrate Specificity

Substances

  • Lipase