Critical amino acids responsible for converting specificities of proteins and for enhancing enzyme evolution are located around β-turn potentials: Data-based prediction

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Abstract
Various reports have described that amino acid substitutions can alter substrate, positional, inhibitory, and target gene specificities of proteins. By using the method of Chou and Fasman, the present work predicts that critical amino acids for converting these specificities are located around β-turns. Residues responsible for the alterations of substrate specificities of trypsin,l-lactate dehydrogenase, aspartate aminotransferase, β-lactamase, and cytochrome P-450 are found to exist within regions predicted as β-turns. The ratios of hydroxylation and oxygenation positions of substrates by cytochrome P-450 and lipoxygenase, respectively, are varied by changes of the protein structures, probably around turn conformations. Inhibitory specificities of bovine pancreatic trypsin inhibitor and α1-antitrypsin and target gene specificity of glucocorticoid receptor are converted by changing turn structures. Occurrence of β-turn probabilities can be predicted around the amino acid alteration positions of an evolutionally antecedent protein of a nylon degradation enzyme. These findings will have relevance to work on protein engineering and enzyme evolution.