{"public_id":"cl_9b4d6c4d3268976cb4ce91e66cc2c576","status":"active","superseded_by_public_id":null,"corpus_id":25883292,"text":"Peptide mapping identified Trp321, Trp337, Trp433, and Trp569 as candidate Trp residues protected by acarbose; the Trp337→Phe mutant showed very weak catalytic activity, indicating Trp337 is important for catalytic activity.","confidence":0.9,"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":0.9,"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_1df66449c5e3ba61290e3e01fbe8b9d6","name":"Trp569","description":"Tryptophan residue at position 569 in CGA, identified as a candidate protected by acarbose.","types":["residue"],"url":"https://sah.borca.ai/concepts/co_1df66449c5e3ba61290e3e01fbe8b9d6"},{"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_7286de638e79bcd8c969232f4a5a92a4","name":"Trp321","description":"Tryptophan residue at position 321 in CGA, identified as a candidate protected by acarbose.","types":["residue"],"url":"https://sah.borca.ai/concepts/co_7286de638e79bcd8c969232f4a5a92a4"},{"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"},{"public_id":"co_ef040b7a12589e396fe530d9e3738b8d","name":"Trp433","description":"Tryptophan residue at position 433 in CGA, identified as a candidate protected by acarbose.","types":["residue"],"url":"https://sah.borca.ai/concepts/co_ef040b7a12589e396fe530d9e3738b8d"}],"related_claims":[],"url":"https://sah.borca.ai/claims/cl_9b4d6c4d3268976cb4ce91e66cc2c576"}