• 文献检索
  • 文档翻译
  • 深度研究
  • 学术资讯
  • Suppr Zotero 插件Zotero 插件
  • 邀请有礼
  • 套餐&价格
  • 历史记录
应用&插件
Suppr Zotero 插件Zotero 插件浏览器插件Mac 客户端Windows 客户端微信小程序
定价
高级版会员购买积分包购买API积分包
服务
文献检索文档翻译深度研究API 文档MCP 服务
关于我们
关于 Suppr公司介绍联系我们用户协议隐私条款
关注我们

Suppr 超能文献

核心技术专利:CN118964589B侵权必究
粤ICP备2023148730 号-1Suppr @ 2026

文献检索

告别复杂PubMed语法,用中文像聊天一样搜索,搜遍4000万医学文献。AI智能推荐,让科研检索更轻松。

立即免费搜索

文件翻译

保留排版,准确专业,支持PDF/Word/PPT等文件格式,支持 12+语言互译。

免费翻译文档

深度研究

AI帮你快速写综述,25分钟生成高质量综述,智能提取关键信息,辅助科研写作。

立即免费体验

通过添加氧气实现酶促动力学拆分。

Enzymatic Kinetic Resolution by Addition of Oxygen.

机构信息

Department of Chemistry, University of Oxford, Chemistry Research Laboratory, Mansfield Road, Oxford, OX1 3TA, UK.

Department of Chemistry, University of Oxford, Inorganic Chemistry Laboratory, South Parks Road, Oxford, OX1 3QR, UK.

出版信息

Angew Chem Int Ed Engl. 2021 Feb 23;60(9):4434-4447. doi: 10.1002/anie.202011468. Epub 2020 Dec 22.

DOI:10.1002/anie.202011468
PMID:33037837
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC7986699/
Abstract

Kinetic resolution using biocatalysis has proven to be an excellent complementary technique to traditional asymmetric catalysis for the production of enantioenriched compounds. Resolution using oxidative enzymes produces valuable oxygenated structures for use in synthetic route development. This Minireview focuses on enzymes which catalyse the insertion of an oxygen atom into the substrate and, in so doing, can achieve oxidative kinetic resolution. The Baeyer-Villiger rearrangement, epoxidation, and hydroxylation are included, and biological advancements in enzyme development, and applications of these key enantioenriched intermediates in natural product synthesis are discussed.

摘要

利用生物催化进行动力学拆分已被证明是一种极好的、与传统不对称催化相辅相成的技术,可用于生产手性富集化合物。利用氧化酶进行拆分可以得到有价值的含氧结构,用于合成路线的开发。本综述重点介绍了能够催化氧原子插入底物的酶,从而实现氧化动力学拆分。其中包括 Baeyer-Villiger 重排、环氧化和羟化反应,并讨论了酶开发方面的生物学进展,以及这些关键的手性富集中间体在天然产物合成中的应用。

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/ad7fc13d3c48/ANIE-60-4434-g023.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/6b3890672b5a/ANIE-60-4434-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/9c8ce977dfd1/ANIE-60-4434-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/0bf3328ca1d7/ANIE-60-4434-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/5abfa9692b30/ANIE-60-4434-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/043a1e751245/ANIE-60-4434-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/205f89ca691b/ANIE-60-4434-g009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/6cd6c8bd22cf/ANIE-60-4434-g010.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/5f2e07dd99b9/ANIE-60-4434-g011.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/b4a0e151e24f/ANIE-60-4434-g012.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/76641089862c/ANIE-60-4434-g013.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/24cb0857fe6e/ANIE-60-4434-g014.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/08221c8ed403/ANIE-60-4434-g015.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/531e41000e5d/ANIE-60-4434-g016.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/5ac78eb08952/ANIE-60-4434-g017.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/3fd3c1c9ce2e/ANIE-60-4434-g018.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/ddec7ef7bc3f/ANIE-60-4434-g019.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/a5630affe580/ANIE-60-4434-g020.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/f06a1d5abf02/ANIE-60-4434-g021.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/1ce391a3c526/ANIE-60-4434-g022.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/ad7fc13d3c48/ANIE-60-4434-g023.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/6b3890672b5a/ANIE-60-4434-g004.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/9c8ce977dfd1/ANIE-60-4434-g006.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/0bf3328ca1d7/ANIE-60-4434-g007.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/5abfa9692b30/ANIE-60-4434-g005.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/043a1e751245/ANIE-60-4434-g008.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/205f89ca691b/ANIE-60-4434-g009.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/6cd6c8bd22cf/ANIE-60-4434-g010.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/5f2e07dd99b9/ANIE-60-4434-g011.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/b4a0e151e24f/ANIE-60-4434-g012.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/76641089862c/ANIE-60-4434-g013.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/24cb0857fe6e/ANIE-60-4434-g014.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/08221c8ed403/ANIE-60-4434-g015.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/531e41000e5d/ANIE-60-4434-g016.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/5ac78eb08952/ANIE-60-4434-g017.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/3fd3c1c9ce2e/ANIE-60-4434-g018.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/ddec7ef7bc3f/ANIE-60-4434-g019.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/a5630affe580/ANIE-60-4434-g020.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/f06a1d5abf02/ANIE-60-4434-g021.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/1ce391a3c526/ANIE-60-4434-g022.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/c725/7986699/ad7fc13d3c48/ANIE-60-4434-g023.jpg

相似文献

1
Enzymatic Kinetic Resolution by Addition of Oxygen.通过添加氧气实现酶促动力学拆分。
Angew Chem Int Ed Engl. 2021 Feb 23;60(9):4434-4447. doi: 10.1002/anie.202011468. Epub 2020 Dec 22.
2
Flavoprotein monooxygenases for oxidative biocatalysis: recombinant expression in microbial hosts and applications.用于氧化生物催化的黄素蛋白单加氧酶:在微生物宿主中的重组表达及应用
Front Microbiol. 2014 Feb 6;5:25. doi: 10.3389/fmicb.2014.00025. eCollection 2014.
3
Discovery of Two Native Baeyer-Villiger Monooxygenases for Asymmetric Synthesis of Bulky Chiral Sulfoxides.发现两种用于手性大体积砜类化合物不对称合成的内源性 Baeyer-Villiger 单加氧酶。
Appl Environ Microbiol. 2018 Jul 2;84(14). doi: 10.1128/AEM.00638-18. Print 2018 Jul 15.
4
Protein engineering of stereoselective Baeyer-Villiger monooxygenases.立体选择性 Baeyer-Villiger 单加氧酶的蛋白质工程。
Chemistry. 2012 Aug 13;18(33):10160-72. doi: 10.1002/chem.201202163. Epub 2012 Jul 16.
5
The Application of Biocatalysis in the Preparation and Resolution of Morita-Baylis-Hillman Adducts and Their Derivatives.生物催化在 Morita-Baylis-Hillman 加合物及其衍生物的制备和拆分中的应用。
Chembiochem. 2022 Apr 5;23(7):e202100527. doi: 10.1002/cbic.202100527. Epub 2021 Dec 6.
6
[Baeyer-Villiger monooxygenases in the biosynthesis of microbial secondary metabolites].[微生物次级代谢产物生物合成中的拜耳-维利格单加氧酶]
Sheng Wu Gong Cheng Xue Bao. 2019 Mar 25;35(3):351-362. doi: 10.13345/j.cjb.180294.
7
Chemo-enzymatic Baeyer-Villiger oxidation of 4-methylcyclohexanone via kinetic resolution of racemic carboxylic acids: direct access to enantioenriched lactone.通过外消旋羧酸的动力学拆分实现4-甲基环己酮的化学酶法拜耳-维利格氧化反应:直接获得对映体富集的内酯。
Chem Commun (Camb). 2016 Jan 21;52(6):1230-3. doi: 10.1039/c5cc08519e.
8
Discovery and Characterization of a Baeyer-Villiger Monooxygenase Using Sequence Similarity Network Analysis.利用序列相似性网络分析发现并鉴定一种Baeyer-Villiger单加氧酶
Chembiochem. 2023 May 16;24(10):e202200746. doi: 10.1002/cbic.202200746. Epub 2023 Apr 27.
9
Biocatalytic Enantioselective Synthesis of Atropisomers.生物催化对映异构体的立体选择性合成。
Acc Chem Res. 2022 Dec 6;55(23):3362-3375. doi: 10.1021/acs.accounts.2c00572. Epub 2022 Nov 7.
10
Kinetic resolution of aliphatic acyclic beta-hydroxyketones by recombinant whole-cell Baeyer-Villiger monooxygenases--formation of enantiocomplementary regioisomeric esters.重组全细胞Baeyer-Villiger单加氧酶对脂肪族无环β-羟基酮的动力学拆分——对映体互补区域异构体酯的形成
Bioorg Med Chem Lett. 2009 Jul 15;19(14):3739-43. doi: 10.1016/j.bmcl.2009.05.014. Epub 2009 May 9.

引用本文的文献

1
Choose Your Own Adventure: A Comprehensive Database of Reactions Catalyzed by Cytochrome P450 BM3 Variants.《选择你自己的冒险:细胞色素P450 BM3变体催化反应的综合数据库》
ACS Catal. 2024 Mar 29;14(8):5560-5592. doi: 10.1021/acscatal.4c00086. eCollection 2024 Apr 19.
2
An Enantiospecific Synthesis of 5--α-Bulnesene.(5S)-β-布藜烯的对映选择性合成。
Molecules. 2023 May 5;28(9):3900. doi: 10.3390/molecules28093900.
3
Enzymatic strategies for asymmetric synthesis.不对称合成的酶促策略。

本文引用的文献

1
Evaluating Ylehd, a recombinant epoxide hydrolase from as a potential biocatalyst for the resolution of benzyl glycidyl ether.评估来自[具体来源未给出]的重组环氧化物水解酶Ylehd作为拆分苄基缩水甘油醚的潜在生物催化剂。
RSC Adv. 2018 Apr 6;8(23):12918-12926. doi: 10.1039/c8ra00628h. eCollection 2018 Apr 3.
2
Synthesis of enantiomerically pure alcohols and amines biocatalytic deracemisation methods.对映体纯醇和胺的合成:生物催化消旋化方法
Catal Sci Technol. 2019 Oct 21;9(20):5487-5503. doi: 10.1039/C9CY01539F. Epub 2019 Sep 3.
3
Biocatalysis: Enzymatic Synthesis for Industrial Applications.
RSC Chem Biol. 2021 Jun 1;2(4):958-989. doi: 10.1039/d1cb00080b. eCollection 2021 Aug 5.
生物催化:工业应用中的酶法合成。
Angew Chem Int Ed Engl. 2021 Jan 4;60(1):88-119. doi: 10.1002/anie.202006648. Epub 2020 Aug 17.
4
The Hitchhiker's guide to biocatalysis: recent advances in the use of enzymes in organic synthesis.生物催化指南:酶在有机合成中的最新应用进展
Chem Sci. 2020 Feb 13;11(10):2587-2605. doi: 10.1039/c9sc05746c. eCollection 2020 Mar 14.
5
Recent advances in the chemoenzymatic synthesis of bioactive natural products.生物活性天然产物的化学酶法合成研究进展。
Curr Opin Chem Biol. 2020 Apr;55:111-118. doi: 10.1016/j.cbpa.2020.01.005. Epub 2020 Feb 18.
6
Enzymatic self-sufficient hydride transfer processes.酶催化自给氢转移过程。
Chem Soc Rev. 2019 Nov 25;48(23):5596-5615. doi: 10.1039/c8cs00903a.
7
Investigation of a New Type I Baeyer-Villiger Monooxygenase from Amycolatopsis thermoflava Revealed High Thermodynamic but Limited Kinetic Stability.从热脂土放线菌中发现新型 I 型 Baeyer-Villiger 单加氧酶,揭示了其具有高热力学稳定性但有限的动力学稳定性。
Chembiochem. 2020 Apr 1;21(7):971-977. doi: 10.1002/cbic.201900501. Epub 2020 Jan 9.
8
Emulating evolutionary processes to morph aureothin-type modular polyketide synthases and associated oxygenases.模拟进化过程来塑造金核菌素型模块化聚酮合酶及其相关的加氧酶。
Nat Commun. 2019 Sep 2;10(1):3918. doi: 10.1038/s41467-019-11896-1.
9
Asymmetric Chemoenzymatic Synthesis of (-)-Podophyllotoxin and Related Aryltetralin Lignans.不对称的酶促化学合成(-)-鬼臼毒素和相关芳基四氢萘木脂素。
Angew Chem Int Ed Engl. 2019 Aug 19;58(34):11657-11660. doi: 10.1002/anie.201904102. Epub 2019 Jul 17.
10
Efficient Kinetic Resolution of Sulfur-Stereogenic Sulfoximines by Exploiting Cp Rh -Catalyzed C-H Functionalization.利用 CpRh 催化的 C-H 功能化实现硫手性亚砜亚胺的高效动力学拆分。
Angew Chem Int Ed Engl. 2019 Jun 24;58(26):8902-8906. doi: 10.1002/anie.201904543. Epub 2019 May 24.