Computationally designed variants of Escherichia coli chorismate mutase show altered catalytic activity

Lassila, Jonathan Kyle
Keeffe, Jennifer R.
Oelschlaeger, Peter
Mayo, Stephen L.

¹Biochemistry and Molecular Biophysics Option, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA
²Division of Biology, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA
³Division of Chemistry and Chemical Engineering, Howard Hughes Medical Institute, California Institute of Technology, Pasadena, CA 91125, USA

⁴To whom correspondence should be addressed. E-mail: [email protected]

Received March 2, 2005; accepted March 4, 2005

Edited by Don Hilvert

Protein Engineering, Design and Selection 18(4):p 161-163, April 2005.

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.