Prodomain mutations at the subtilisin interface: correlation of binding energy and the rate of catalyzed folding

The binding of the prodomain to native subtilisin accelerates folding, indicating that the subtilisin intermediate has structural characteristics of the native form. The catalytic activity is unaffected by binding of native subtilisin. The binding site of the prodomain is different from its site on the native protein. An analysis of mutations in the C-terminal region of the prodomain reveals that the binding site is in 100-144 amino acid sequence of subtilisin. The amino acids probably have a native-like fold in the intermediate which is stabilized by the prodomain.