why protein is Polar and enzyme non polar
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I am comparing the active/catalytic site of two proteins A and B, both belonging to the same family. Both bind to a divalent cation but have entirely different and nearly opposite functions. While the core catalytic site residues remain the same, the residue present in close proximity (within 8A) show differences in the number of polar residues. Protein A seems to have only 3 while B appears to 6-7 (nearly double). This would probably have an impact on the overall surface charge of the catalytic site. However, would it alter the functioning of both the proteins
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polar is protein
enzyme is non polar
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