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Calculation of the equilibrium constant for the enzymatic reaction. (1983). https://pubmed.ncbi.nlm.nih.gov/6863314/ DOI: 10.1016/s0021-9258(18)32137-9","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Purified glyoxalase I","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"7b1aab46-eea6-5e2b-8adc-f52a6194df29","evidence_kind":"source_excerpt","locator":"Lines 918-929","start_line":918,"end_line":929,"excerpt":"### glutathione-glo1-product\nHuman erythrocyte GLO1 forms S-D-lactoylglutathione through the methylglyoxal/GSH hemithioacetal intermediate.\nCondition category: normal\nnutrient_topic: Glutathione research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: The first enzyme supplies the substrate processed by glyoxalase II.\norganism: Human erythrocyte enzyme; separate yeast comparison\ntissue_or_cell_type: Purified glyoxalase I\nexperimental_model: Forward/reverse enzyme kinetics\nlimitations: Artificial trapping reveals reversibility; it does not reverse the usual physiological net flux.\nexposure: Lactoyl-GSH and thiol-trapping experiments\nevidence_span: {\"source_cache\": \"artifacts/glutathione-research/6863314.abstract.txt\", \"locator\": \"Primary indexed abstract; zero-based, end-exclusive Unicode character offsets\", \"file_sha256\": \"fc40fe8d31ed36ad75af255cf31121d46ab8905d456f4ff9d94cc857e6b0e00d\", \"start_char\": 0, \"end_char\": 2097, \"text_sha256\": \"fc40fe8d31ed36ad75af255cf31121d46ab8905d456f4ff9d94cc857e6b0e00d\"}\n[glutathione-p6863314] Reversal of the reaction catalyzed by glyoxalase I. 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