{"title":"甘氨酸的仿生醛醇反应","authors":"Luca Bernardi","doi":"10.1038/s41929-025-01383-w","DOIUrl":null,"url":null,"abstract":"The enantioselective aldol reaction of glycinates with aldehydes — a direct entry to an important class of noncanonical amino acids — has so far eluded small-molecule catalysis. Now, mimicking the cofactor of threonine aldolase enzymes, a chiral carbonyl catalyst that is remarkably effective for this reaction has been developed. This asymmetric protocol has been successfully applied to more than a thousand aldehyde substrates.","PeriodicalId":18845,"journal":{"name":"Nature Catalysis","volume":"8 7","pages":"627-628"},"PeriodicalIF":44.6000,"publicationDate":"2025-07-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"Biomimetic aldol reaction of glycinate\",\"authors\":\"Luca Bernardi\",\"doi\":\"10.1038/s41929-025-01383-w\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"The enantioselective aldol reaction of glycinates with aldehydes — a direct entry to an important class of noncanonical amino acids — has so far eluded small-molecule catalysis. Now, mimicking the cofactor of threonine aldolase enzymes, a chiral carbonyl catalyst that is remarkably effective for this reaction has been developed. This asymmetric protocol has been successfully applied to more than a thousand aldehyde substrates.\",\"PeriodicalId\":18845,\"journal\":{\"name\":\"Nature Catalysis\",\"volume\":\"8 7\",\"pages\":\"627-628\"},\"PeriodicalIF\":44.6000,\"publicationDate\":\"2025-07-24\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Nature Catalysis\",\"FirstCategoryId\":\"92\",\"ListUrlMain\":\"https://www.nature.com/articles/s41929-025-01383-w\",\"RegionNum\":1,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"CHEMISTRY, PHYSICAL\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Nature Catalysis","FirstCategoryId":"92","ListUrlMain":"https://www.nature.com/articles/s41929-025-01383-w","RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, PHYSICAL","Score":null,"Total":0}
The enantioselective aldol reaction of glycinates with aldehydes — a direct entry to an important class of noncanonical amino acids — has so far eluded small-molecule catalysis. Now, mimicking the cofactor of threonine aldolase enzymes, a chiral carbonyl catalyst that is remarkably effective for this reaction has been developed. This asymmetric protocol has been successfully applied to more than a thousand aldehyde substrates.
期刊介绍:
Nature Catalysis serves as a platform for researchers across chemistry and related fields, focusing on homogeneous catalysis, heterogeneous catalysis, and biocatalysts, encompassing both fundamental and applied studies. With a particular emphasis on advancing sustainable industries and processes, the journal provides comprehensive coverage of catalysis research, appealing to scientists, engineers, and researchers in academia and industry.
Maintaining the high standards of the Nature brand, Nature Catalysis boasts a dedicated team of professional editors, rigorous peer-review processes, and swift publication times, ensuring editorial independence and quality. The journal publishes work spanning heterogeneous catalysis, homogeneous catalysis, and biocatalysis, covering areas such as catalytic synthesis, mechanisms, characterization, computational studies, nanoparticle catalysis, electrocatalysis, photocatalysis, environmental catalysis, asymmetric catalysis, and various forms of organocatalysis.