Abstract
Promiscuity, the ability of an enzyme to catalyze diverse activities using the same active site, sets up the stage for the evolution of complex organisms through gene duplication and specialization. The detection of promiscuous motifs is crucial to understand the physiological relevance of a protein, or for any endeavor that intends to rationally modify these latent capabilities to design new proteins under laboratory conditions. We have established a methodology for identifying catalytic residues based on spatial and electrostatic congruence with known active site configurations. Here, we discuss insights gained in several initiatives using our method on different enzymes.
Highlights
Promiscuity, the ability of an enzyme to catalyze diverse activities using the same active site, sets up the stage for the evolution of complex organisms through gene duplication and specialization
Compound promiscuity plays a major role in drug discovery, and in the therapeutic efficacy of drugs[9]
The sequence-to-structure-to-function paradigm facilitates the functional characterization of new proteins by applying a ‘guilt by association’ logic, and has essentially revolutionized the field by its easy to use model[15]
Summary
2. Bone R, Silen JL, Agard DA: Structural plasticity broadens the specificity of an engineered protease. 3. Yoshikuni Y, Ferrin TE, Keasling JD: Designed divergent evolution of enzyme function. 4. Khersonsky O, Tawfik DS: Enzyme promiscuity: a mechanistic and evolutionary perspective.
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