title: Computationally designed variants of Escherichia coli chorismate mutase show altered catalytic activity.
abstract: Computational protein design methods were used to predict five variants of monofunctional Escherichia coli chorismate mutase expected to maintain catalytic activity. The variants were tested experimentally and three active site mutants exhibited catalytic activity similar to or greater than the wild-type enzyme. One mutant, Ala32Ser, showed increased catalytic efficiency.
authors.affiliation: Biochemistry and Molecular Biophysics Option, Howard Hughes Medical Institute, Pasadena, CA 91125, USA.
authors.forename: Jonathan Kyle
authors.initials: JK
authors.lastname: Lassila
authors.forename: Jennifer R
authors.initials: JR
authors.lastname: Keeffe
authors.forename: Peter
authors.initials: P
authors.lastname: Oelschlaeger
authors.forename: Stephen L
authors.initials: SL
authors.lastname: Mayo
mesh_terms: D000409:Alanine / Q000235:genetics; D019943:Amino Acid Substitution / Q000235:genetics; D002384:Catalysis; D020134:Catalytic Domain; D002826:Chorismate Mutase / Q000235:genetics* / Q000378:metabolism*; D019295:Computational Biology; D004926:Escherichia coli / Q000201:enzymology*; D009154:Mutation; D015202:Protein Engineering; D012694:Serine / Q000235:genetics
chemical_list: D012694:Serine; D002826:Chorismate Mutase; D000409:Alanine