Jiawei Yang , Zhimei Yuan , Yang Zhou , Jia Zhao , Min Yang , Xiaoling Cheng , Gangwei Ou , Yongzheng Chen
{"title":"重组蒙氏假单胞菌甲硫氨酸亚砜还原酶对外消旋亚砜的不对称还原分解","authors":"Jiawei Yang , Zhimei Yuan , Yang Zhou , Jia Zhao , Min Yang , Xiaoling Cheng , Gangwei Ou , Yongzheng Chen","doi":"10.1016/j.molcatb.2017.02.005","DOIUrl":null,"url":null,"abstract":"<div><p>In this study, the methionine sulfoxide reductase A from a <em>pseudomonas monteilii</em> strain (<em>pm</em>MsrA) was reported to synthesize optically active sulfoxides (<em>R</em>)-<strong>1a</strong>-<strong>4a</strong>, through asymmetric biocatalytic reductive resolution. Several biotransformation parameters including the reaction time, cell density, and substrate concentration were optimized. Moreover, Substrate scope of <em>pmMsrA</em> catalyzed asymmetric reductive resolution was investigated, which gave chiral (<em>R</em>)-<strong>1a</strong>-<strong>4a</strong> with 61%-97% <em>ee</em>.</p></div>","PeriodicalId":16416,"journal":{"name":"Journal of Molecular Catalysis B-enzymatic","volume":"133 ","pages":"Pages S588-S592"},"PeriodicalIF":0.0000,"publicationDate":"2016-11-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.molcatb.2017.02.005","citationCount":"8","resultStr":"{\"title\":\"Asymmetric reductive resolution of racemic sulfoxides by recombinant methionine sulfoxide reductase from a pseudomonas monteilii strain\",\"authors\":\"Jiawei Yang , Zhimei Yuan , Yang Zhou , Jia Zhao , Min Yang , Xiaoling Cheng , Gangwei Ou , Yongzheng Chen\",\"doi\":\"10.1016/j.molcatb.2017.02.005\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>In this study, the methionine sulfoxide reductase A from a <em>pseudomonas monteilii</em> strain (<em>pm</em>MsrA) was reported to synthesize optically active sulfoxides (<em>R</em>)-<strong>1a</strong>-<strong>4a</strong>, through asymmetric biocatalytic reductive resolution. Several biotransformation parameters including the reaction time, cell density, and substrate concentration were optimized. Moreover, Substrate scope of <em>pmMsrA</em> catalyzed asymmetric reductive resolution was investigated, which gave chiral (<em>R</em>)-<strong>1a</strong>-<strong>4a</strong> with 61%-97% <em>ee</em>.</p></div>\",\"PeriodicalId\":16416,\"journal\":{\"name\":\"Journal of Molecular Catalysis B-enzymatic\",\"volume\":\"133 \",\"pages\":\"Pages S588-S592\"},\"PeriodicalIF\":0.0000,\"publicationDate\":\"2016-11-01\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://sci-hub-pdf.com/10.1016/j.molcatb.2017.02.005\",\"citationCount\":\"8\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Journal of Molecular Catalysis B-enzymatic\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S1381117717300243\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q2\",\"JCRName\":\"Chemical Engineering\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of Molecular Catalysis B-enzymatic","FirstCategoryId":"1085","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S1381117717300243","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q2","JCRName":"Chemical Engineering","Score":null,"Total":0}
Asymmetric reductive resolution of racemic sulfoxides by recombinant methionine sulfoxide reductase from a pseudomonas monteilii strain
In this study, the methionine sulfoxide reductase A from a pseudomonas monteilii strain (pmMsrA) was reported to synthesize optically active sulfoxides (R)-1a-4a, through asymmetric biocatalytic reductive resolution. Several biotransformation parameters including the reaction time, cell density, and substrate concentration were optimized. Moreover, Substrate scope of pmMsrA catalyzed asymmetric reductive resolution was investigated, which gave chiral (R)-1a-4a with 61%-97% ee.
期刊介绍:
Journal of Molecular Catalysis B: Enzymatic is an international forum for researchers and product developers in the applications of whole-cell and cell-free enzymes as catalysts in organic synthesis. Emphasis is on mechanistic and synthetic aspects of the biocatalytic transformation.
Papers should report novel and significant advances in one or more of the following topics;
Applied and fundamental studies of enzymes used for biocatalysis;
Industrial applications of enzymatic processes, e.g. in fine chemical synthesis;
Chemo-, regio- and enantioselective transformations;
Screening for biocatalysts;
Integration of biocatalytic and chemical steps in organic syntheses;
Novel biocatalysts, e.g. enzymes from extremophiles and catalytic antibodies;
Enzyme immobilization and stabilization, particularly in non-conventional media;
Bioprocess engineering aspects, e.g. membrane bioreactors;
Improvement of catalytic performance of enzymes, e.g. by protein engineering or chemical modification;
Structural studies, including computer simulation, relating to substrate specificity and reaction selectivity;
Biomimetic studies related to enzymatic transformations.