The reactive site of Streptomyces subtilisin inhibitor.
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.
D000596:Amino Acids / Q000032:analysis; D001426:Bacterial Proteins / Q000378:metabolism*; D055598:Chemical Phenomena; D002621:Chemistry; D002850:Chromatography, Gel; D002918:Chymotrypsin; D010446:Peptide Fragments; D011480:Protease Inhibitors; D013302:Streptomyces / Q000378:metabolism*; D013381:Subtilisins / Q000037:antagonists & inhibitors* / Q000378:metabolism
D000596:Amino Acids; D001426:Bacterial Proteins; D010446:Peptide Fragments; D011480:Protease Inhibitors; C018150:subtilisin inhibitor protein, Streptomyces; D013381:Subtilisins; D002918:Chymotrypsin