In this postdoctoral research project I propose to engineer new enzymes from a different and so far unexplored angle, namely to use a monomeric mutant enzyme with a molten globule structure as a scaffold. We believe the plasticity of a molten globule may improve the odds of designing new functional properties. Combinatorial protein chemistry techniques followed by rounds of selection together with extensive kinetic and structural studies of mutant chorismate mutases (CM) as a model will be our strategy. The project will focus on:
1) improving the CM activity;
2) changing the substrate specificity of the protein to catalyse the prephenate - and gt;phenyl-pyruvate reaction;
3) combining the two catalytic properties to create a bi-functional enzyme.
Call for proposal
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