Evidence for an Extended Active Center in Elastase

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Abstract
Large increases in the esterase, amidase, and peptidase activities of elastase are observed on increasing the length of peptide substrates. The results suggest that at least five contiguous peptide units of the substrate (four N-terminal and one C-terminal to the scissile bond) can interact concurrently with the enzyme. When analyzed in terms of an acyl-enzyme mechanism, the increased effectiveness of the enzyme with larger substrates appears mainly in the acylation reaction and, to a lesser extent, in the binding and deacylation steps.