{"public_id":"cl_86f3a20d72ab57a3be5e7ef0c678d318","status":"active","superseded_by_public_id":null,"corpus_id":25883292,"text":"Trp337 and Glu632 appear crucial for formation of the third intermediate in the wild-type reaction, which precedes the transition state.","confidence":0.95,"paper":{"corpus_id":25883292,"title":"Functional roles of Trp337 and Glu632 in Clostridium glucoamylase, as determined by chemical modification, mutagenesis, and the stopped-flow method.","url":"https://sah.borca.ai/papers/25883292"},"contributors":[{"id":32,"public_id":"7c402c1b98","public_label":"뀨 (7c402c1b98)","roles":["extraction"],"url":"https://sah.borca.ai/u/7c402c1b98"},{"id":1,"public_id":"12632b8b5f","public_label":"Anonymous (12632b8b5f)","roles":["review"],"url":"https://sah.borca.ai/u/12632b8b5f"}],"origin_summary":{"object_type":"claim","status":"active","confidence":0.95,"origin_kinds":["extraction","extraction_create"],"contribution_count":1,"contribution_task_types":["extraction"],"contribution_statuses":["applied"],"verifier_verdict_count":2,"verifier_classes":["system"],"verifier_class_counts":{"system":2,"user_agent":0},"verdict_counts":{"approve":1,"reject":1},"verifier_state":"system_only","basis":["kg_settlement_results.decision_payload.legacy_bridge","kg_entity_origin_refs","kg_assertion_proposals","contributions","verifications","claim.status","claim.confidence"],"limits":["ledger provenance is aggregated; raw contribution and verifier audit rows are not expanded","entity matching uses settlement bridge refs and edge commands"]},"concepts":[{"public_id":"co_20ce8755f390b034daee3449f33b24a9","name":"third intermediate","description":"The third intermediate in the wild-type CGA reaction that precedes the transition state and whose formation depends on Trp337 and Glu632.","types":["intermediate"],"url":"https://sah.borca.ai/concepts/co_20ce8755f390b034daee3449f33b24a9"},{"public_id":"co_4df3c144917575cccb202afe1369c3a3","name":"Clostridium glucoamylase","description":"Glucoamylase (EC 3.2.1.3) from Clostridium sp. G0005, the enzyme studied in this work.","types":["enzyme"],"url":"https://sah.borca.ai/concepts/co_4df3c144917575cccb202afe1369c3a3"},{"public_id":"co_8902ceadc780c24fe021e70a0833c197","name":"Glu632","description":"Glutamate residue at position 632 in CGA, the putative catalytic base mutated to Gln in this study.","types":["residue"],"url":"https://sah.borca.ai/concepts/co_8902ceadc780c24fe021e70a0833c197"},{"public_id":"co_bed3c3a85054a824a71b99c978fd70d1","name":"Trp337","description":"Tryptophan residue at position 337 in CGA, identified as important for catalytic activity via mutagenesis (Trp337→Phe).","types":["residue"],"url":"https://sah.borca.ai/concepts/co_bed3c3a85054a824a71b99c978fd70d1"}],"related_claims":[],"url":"https://sah.borca.ai/claims/cl_86f3a20d72ab57a3be5e7ef0c678d318"}