Question: where does cleavage of the peptide bond by chymotrypsin occur
[{'answer': 'digestive systems', 'provenance': [{'wikipedia_id': '7060', 'title': 'Chymotrypsin', 'start_paragraph_id': 6, 'start_character': 80, 'end_paragraph_id': 6, 'end_character': 97, 'bleu_score': 1.0, 'section': 'Section::::Mechanism of action and kinetics.\n'}]}, {'answer': 'where the side - chain of the amino acid N - terminal to the scissile amide bond ( the P position ) is a large hydrophobic amino acid ( tyrosine , tryptophan , and phenylalanine )'}, {'answer': 'positions 14 - 15 , 146 - 147 and 148 - 149'}, {'provenance': [{'wikipedia_id': '7060', 'title': 'Chymotrypsin', 'start_paragraph_id': 1, 'start_character': 0, 'end_paragraph_id': 1, 'end_character': 1042, 'bleu_score': 0.914842803924624, 'meta': {'yes_no_answer': 'NONE', 'annotation_id': 9896526504257587108}, 'section': 'Section::::Abstract.'}]}, {'provenance': [{'wikipedia_id': '7060', 'title': 'Chymotrypsin', 'start_paragraph_id': 0, 'start_character': 0, 'end_paragraph_id': 0, 'end_character': 0, 'bleu_score': 1.0, 'meta': {'yes_no_answer': 'NONE', 'annotation_id': 9896526504257587108}, 'section': 'Section::::Abstract.'}]}, {'provenance': [{'wikipedia_id': '7060', 'title': 'Chymotrypsin', 'start_paragraph_id': 6, 'start_character': 0, 'end_paragraph_id': 6, 'end_character': 641, 'bleu_score': 0.9368861528651171, 'meta': {'yes_no_answer': 'NONE', 'annotation_id': 9896526504257587108}, 'section': 'Section::::Mechanism of action and kinetics.\n'}]}, {'provenance': [{'wikipedia_id': '7060', 'title': 'Chymotrypsin', 'start_paragraph_id': 4, 'start_character': 0, 'end_paragraph_id': 4, 'end_character': 684, 'bleu_score': 0.979896933041101, 'meta': {'yes_no_answer': 'NONE', 'annotation_id': 9896526504257587108}, 'section': 'Section::::Activation.\n'}]}, {'provenance': [{'wikipedia_id': '7060', 'title': 'Chymotrypsin', 'section': 'Section::::Mechanism of action and kinetics.\n', 'start_paragraph_id': 6, 'end_paragraph_id': 6, 'meta': {'evidence_span': ['chymotrypsin is a proteolytic enzyme (serine protease) acting in the digestive systems of many organism', '"In vivo", chymotrypsin is a proteolytic enzyme (serine protease) acting in the digestive systems of many organisms. It facilitates the cleavage of peptide bonds by a hydrolysis reaction, which despite being thermodynamically favorable, occurs extremely slowly in the absence of a catalyst. The main substrates of chymotrypsin are peptide bonds in which the amino acid N-terminal to the bond is a tryptophan, tyrosine, phenylalanine, or leucine. Like many proteases, chymotrypsin also hydrolyses amide bonds "in vitro", a virtue that enabled the use of substrate analogs such as N-acetyl-L-phenylalanine p-nitrophenyl amide for enzyme assays.', '"In vivo", chymotrypsin is a proteolytic enzyme (serine protease) acting in the digestive systems of many organisms. It facilitates the cleavage of peptide bonds by a hydrolysis reaction, which despite being thermodynamically favorable, occurs extremely slowly in the absence of a catalyst.']}}]}, {'provenance': [{'wikipedia_id': '74729', 'title': 'Chymotrypsinogen', 'section': 'Section::::Abstract.', 'start_paragraph_id': 1, 'end_paragraph_id': 1, 'meta': {'evidence_span': ['It is synthesized in the acinar cells of the pancreas and stored inside membrane-bounded granules at the apex of the acinar cell.', 'Chymotrypsinogen is an inactive precursor (zymogen) of chymotrypsin, a digestive enzyme which breaks proteins down into smaller peptides. Chymotrypsinogen is a single polypeptide chain consisting of 245 amino acid residues. It is synthesized in the acinar cells of the pancreas and stored inside membrane-bounded granules at the apex of the acinar cell. Release of the granules from the cell is stimulated by either a hormonal signal or a nerve impulse, and the granules spill into a duct leading into the duodenum.']}}]}]