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Structure function relationships underlying laccases properties are very limited that makes these enzymes interesting for protein engineering approaches.
The high plasticity of the active-site cavity of cytochromes P450, permitting reactivity toward a vast array of compounds, makes these enzymes attractive targets for biotechnological application.
BVMO reactions are often difficult, if not impossible to achieve by chemical approaches and this makes these enzymes thus highly desired candidates for industrial applications.
The ability of P450s to introduce oxygen atoms at specific positions on complex molecules makes these enzymes particularly valuable for applications in synthetic biology.
This makes these enzymes particularly interesting targets for in-silico inhibition prediction.
The complete utilization of biomass (both cellulose and hemicellulose) to obtain bulk chemicals (biofuels) and XOS makes these enzymes very interesting from industrial perspective.
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It costs energy to make these enzymes.
Aberrant HDAC activity is associated with cancer, making these enzymes important targets for drug design.
Few healthy cells make these enzymes, so they are a reliable marker of tumours.To make use of the MMPs Dr Tsien attaches his fluorescent dye, along with some positive charges, to one side of a small hairpin-shaped protein molecule.
Aspartic proteases are already the targets of some clinically useful drugs (e.g. chemotherapy of HIV infection) and a variety of factors make these enzymes appealing to those seeking novel antiparasite therapies.
On the other hand, all enzymes are sensitive to pH changes, but extremely high or low pH values can make these enzymes lose their sensitivity [30, 31].
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