Enzyme protein, redesigned

Redesign of Ca fMg Specificity. Proteins in the calmodulin superfamily (including troponin C, parvalbumin (PV) and oncomodulin (OM)) share similar overall structure and yet have different selectivity for Ca and Mg see Calcium-binding Proteins, Cation-activated Enzymes). For example, PV and OM have four helix-tum-helix domains, two of which contain mixed Ca /Mg sites and two Ca -specific sites. The mixed Ca /Mg sites have been converted to Ca -specific sites by replacing amino acids with the corresponding residues in the Ca -specific site. " ... 

Our results demonstrate that protein engineering is a powerful means to understand structure-function relations in proteins, and that engineering secondary structures to produce enzymes with novel properties is feasible. Lessons leaned from our studies should be applicable to the redesign and optimization of functions in other enzymes. 

The different but complementary strategies for redesigning natural enzyme can be approached from the perspective of how rational the strategy could be. Thus, the existing biocatalyst can be fine-tuned by rational design, being information intensive and computer assisted. In other words, the more rational the desired approach, the more knowledge is necessary to exactly interplay protein sequence and function. 

Protein engineering is of very wide interest, offering the potential to provide new or better enzymes. As we begin to understand the process of molecular recognition and catalysis in flavocytochrome 2 in more detail, we should increase the scope for rational redesign of this enzyme. 

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