title: Rational engineering of Candida antarctica lipase B for selective monoacylation of diols.
abstract: The enzyme Candida antarctica lipase B was subjected to site directed mutagenesis suggested by molecular modelling. The selectivity for the enzyme increased towards a range of diols over their corresponding monoesters as an effect of the mutations.
authors.affiliation: School of Biotechnology, Department of Biochemistry, Royal Institute of Technology (KTH), AlbaNova, SE-106 91 Stockholm, Sweden.
authors.forename: Anders
authors.initials: A
authors.lastname: Hamberg
authors.forename: Steffen
authors.initials: S
authors.lastname: Maurer
authors.forename: Karl
authors.initials: K
authors.lastname: Hult
mesh_terms: D000215:Acylation; D002072:Butylene Glycols / Q000378:metabolism*; D002175:Candida / Q000737:chemistry / Q000201:enzymology* / Q000235:genetics / Q000378:metabolism; D019855:Ethylene Glycol / Q000378:metabolism*; D005656:Fungal Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D008049:Lipase / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D056004:Molecular Dynamics Simulation; D016297:Mutagenesis, Site-Directed; D013379:Substrate Specificity
chemical_list: D002072:Butylene Glycols; D005656:Fungal Proteins; C039681:1,4-butanediol; D008049:Lipase; C431349:lipase B, Candida antarctica; D019855:Ethylene Glycol