Computationally designed variants of Escherichia coli chorismate mutase show altered catalytic activity.
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.
Lassila
Jonathan Kyle
JK
Biochemistry and Molecular Biophysics Option, Howard Hughes Medical Institute, Pasadena, CA 91125, USA.
Keeffe
Jennifer R
JR
Oelschlaeger
Peter
P
Mayo
Stephen L
SL
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
D012694:Serine; D002826:Chorismate Mutase; D000409:Alanine