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Amino acid sequence alignment of bacterial and mammalian pancreatic serine proteases based on topological equivalences

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Comparative analysis identifies structural similarities in serine proteases, highlighting evolutionary adaptations.

The study aims to compare the three-dimensional structures of bacterial and mammalian pancreatic serine proteases to understand their evolutionary relationships.
Compared alpha-carbon positions of bacterial serine proteases (SGPA, SGPB, alpha-lytic) with pancreatic enzymes (alpha-chymotrypsin, elastase).
Established a sequence alignment based on topological equivalences and structural homology.
Analyzed the effects of zymogen function on architectural changes between bacterial and pancreatic enzymes.
Approximately 60% of the alpha-carbon positions in bacterial serine proteases are topologically equivalent to those in pancreatic enzymes (55-64%).
Bacterial serine proteases show about 84% topological equivalence among themselves.
Significant architectural alterations were found in pancreatic enzymes, including N-terminal loop insertions of 9 and 12 residues affecting their structure.

James et al. (1978) studied this question.

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