The reactive of Streptomyces subtilisin inhibitor (SSI) was investigated by chymotryptic cleavage of the reactive site peptide bond and its resynthesis by inhibitor-subtilisin complex formation. The results show that the reactive site peptide bond of the inhibitor is Met(73)-Val(74) and that subtilisin specifically cleaved the Leu(6)-Tyr(7) bond of SSI upon complex formation.
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