[{"data":1,"prerenderedAt":-1},["ShallowReactive",2],{"doc-seo-181982-105":3,"detail-sidebar-cat-0-en-105":85,"doc-detail-181982-en":135},{"code":4,"msg":5,"data":6},0,"ok",{"site_id":7,"language":8,"slug":9,"title":10,"keywords":11,"description":12,"schema_data":13,"social_meta":78,"head_meta":80,"extra_data":82,"updated_unix":84},105,"en","research-report-on-chiral-synthesis","Research Report On Chiral Synthesis","","This document presents a detailed research report focused on chiral synthesis, specifically investigating the formation of enantiomers through enzymatic catalysis. The report meticulously details various substrate modifications and their corresponding enantiomeric excess (e.r.) and turnover numbers (TON) when combined with specific enzyme mutants, namely Ir(Me)-mOCR-Myo. It systematically outlines the effects of amino acid substitutions at key positions within the enzyme's active site, such as positions 93, 64, 43, and 68, on the stereoselectivity and efficiency of the catalytic process. Several substrate types are examined, including those with substitutions like 93A, 64L, 43L, 33V, leading to varying ratios of (–) and (+) enantiomers. The data is presented in a table format, clearly indicating the specific substrate, the mutant used, the enantiomeric ratio, and the turnover number achieved for each experimental condition. Special attention is given to conditions that yield high enantiomeric excess, signifying successful chiral induction. The report also includes notations for specific conditions, such as those marked with asterisks and daggers, likely indicating unique or amplified results. This comprehensive analysis provides critical insights into enzyme engineering for enantioselective synthesis, a fundamental area in pharmaceutical and fine chemical production.",{"@graph":14,"@context":77},[15,34,56],{"@type":16,"itemListElement":17},"BreadcrumbList",[18,23,27,31],{"item":19,"name":20,"@type":21,"position":22},"https://docshare.wps.com","Home","ListItem",1,{"item":24,"name":25,"@type":21,"position":26},"https://docshare.wps.com/document/","Document",2,{"item":28,"name":29,"@type":21,"position":30},"https://docshare.wps.com/document/research-report/","Research & 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research report focuses on chiral synthesis, specifically the formation of enantiomers through enzymatic catalysis using specific enzyme mutants.","Answer",{"name":66,"@type":61,"acceptedAnswer":67},"What parameters are measured in the experimental results?",{"text":68,"@type":64},"The experimental results measure the enantiomeric excess (e.r.) and turnover number (TON) for the formation of both (–) and (+) enantiomers for various substrate modifications with specific enzyme mutants.",{"name":70,"@type":61,"acceptedAnswer":71},"What role do enzyme mutants play in this research?",{"text":72,"@type":64},"Enzyme mutants like Ir(Me)-mOCR-Myo are crucial as they are used to catalyze the reactions and their specific amino acid substitutions are investigated for their impact on stereoselectivity and efficiency in forming enantiomers.",{"name":74,"@type":61,"acceptedAnswer":75},"How is the data presented in the report?",{"text":76,"@type":64},"The data is presented in a table format, detailing the substrate's composition, the mutant used, and the resulting enantiomeric ratios and turnover numbers for both enantiomers.","https://schema.org",{"og:url":32,"og:type":79,"og:title":10,"og:site_name":45,"og:description":12},"article",{"robots":81,"canonical":32},"index,follow",{"doc_id":83,"site_id":7},181982,1788346712,{"code":4,"msg":86,"data":87},"success",[88,92,96,100,105,110,115,119,124,127,131],{"id":22,"doc_module":4,"doc_module_name":25,"category_name":89,"show_sort_weight":90,"slug":91},"Story & 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--- | --- | --- |\n|  | Mutant of Ir(Me)-mOCR-Myo | e. r. (TON) | Mutant of Ir(Me)-mOCR-Myo | e. r. (TON) |\n|  |  | . |  | . |\n| 1 | 93A, 64L, 43L, 33V | 85:15 (134) | 93G, 64L, 68A, 33F, 99V | 16:84 (62) |\n| 6 | 93A, 64V, 43Y, 68A, 97W | 81:19 (128) | 93A, 64L, 68A, 99V | 20:80 (26) |\n| 7 | 93G, 64L, 43L, 99F | 92:8 (92) | 93A, 64L, 43W, 68A, 97Y | 25:75 (68) |\n| 8 9 | 93A, 64V, 68A, 103C, 108C 93A, 64L, 43W, 68A, 33I | 90:10 (98)\u003Cbr>85:15 (86) | 93A, 64L, 43W, 68T\u003Cbr>93A, 64L, 43I, 68T | 23:77(164)\u003Cbr>25:75 (138) |\n| 10 | 93A, 64V, 43H, 68S | 77:23 (44) | 93A, 64V, 68A, 33V, 97Y | 17:83 (44) |\n| 11 | 93A, 64A, 43W, 68G . | 90:10 (52)\u003Cbr>90:10 (160)*\u003Cbr>84:16 (7,260)† | 93G, 64L, 68A, 32F, 97Y . | 13:87 (144) |","cbCaikwyy6iAHdGT","https://ap.wps.com/l/cbCaikwyy6iAHdGT","pdf",750250,"English","# Chiral Synthesis Research\n## Substrates and Enantiomer Formation\n### Formation of (–) enantiomer\n### Formation of (+) enantiomer","[{\"question\":\"What is the primary focus of this research report?\",\"answer\":\"The research report focuses on chiral synthesis, specifically the formation of enantiomers through enzymatic catalysis using specific enzyme mutants.\"},{\"question\":\"What parameters are measured in the experimental results?\",\"answer\":\"The experimental results measure the enantiomeric excess (e.r.) and turnover number (TON) for the formation of both (–) and (+) enantiomers for various substrate modifications with specific enzyme mutants.\"},{\"question\":\"What role do enzyme mutants play in this research?\",\"answer\":\"Enzyme mutants like Ir(Me)-mOCR-Myo are crucial as they are used to catalyze the reactions and their specific amino acid substitutions are investigated for their impact on stereoselectivity and efficiency in forming enantiomers.\"},{\"question\":\"How is the data presented in the report?\",\"answer\":\"The data is presented in a table format, detailing the substrate's composition, the mutant used, and the resulting enantiomeric ratios and turnover numbers for both enantiomers.\"}]","Research Report On Chiral Synthesis | PDF",13]