人工智能。zymes -进化酶设计的模块化平台

IF 16.1 1区 化学 Q1 CHEMISTRY, MULTIDISCIPLINARY
Lucas P. Merlicek, Jannik Neumann, Abbie Lear, Vivian Degiorgi, Moor M. de Waal, Tudor-Stefan Cotet, Prof. Adrian J. Mulholland, Dr. H. Adrian Bunzel
{"title":"人工智能。zymes -进化酶设计的模块化平台","authors":"Lucas P. Merlicek,&nbsp;Jannik Neumann,&nbsp;Abbie Lear,&nbsp;Vivian Degiorgi,&nbsp;Moor M. de Waal,&nbsp;Tudor-Stefan Cotet,&nbsp;Prof. Adrian J. Mulholland,&nbsp;Dr. H. Adrian Bunzel","doi":"10.1002/anie.202507031","DOIUrl":null,"url":null,"abstract":"<p>The ability to create new-to-nature enzymes would substantially advance bioengineering, medicine, and the chemical industry. Despite recent breakthroughs in protein design and structure prediction, designing novel biocatalysts remains challenging. Here, we present AI.zymes, a modular platform integrating cutting-edge protein engineering algorithms within an evolutionary framework (https://github.com/bunzela/AIzymes). By combining bioengineering tools such as Rosetta, ESMFold, ProteinMPNN, and FieldTools in iterative rounds of design and selection, AI.zymes can optimize a broad range of catalytically relevant properties. In addition to enhancing transition state affinity and protein stability, AI.zymes can also improve properties that are not targeted by the employed design algorithms. For instance, AI.zymes can enhance electrostatic catalysis by iteratively selecting variants with stronger catalytic electric fields. Benchmarking AI.zymes on the promiscuous Kemp eliminase activity of ketosteroid isomerase led to a 7.7-fold activity increase after experimentally testing just 7 variants. Due to its modularity, AI.zymes can readily incorporate emerging design algorithms, paving the way for a unifying framework for enzyme design.</p>","PeriodicalId":125,"journal":{"name":"Angewandte Chemie International Edition","volume":"64 27","pages":""},"PeriodicalIF":16.1000,"publicationDate":"2025-04-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":"{\"title\":\"AI.zymes: A Modular Platform for Evolutionary Enzyme Design\",\"authors\":\"Lucas P. Merlicek,&nbsp;Jannik Neumann,&nbsp;Abbie Lear,&nbsp;Vivian Degiorgi,&nbsp;Moor M. de Waal,&nbsp;Tudor-Stefan Cotet,&nbsp;Prof. Adrian J. Mulholland,&nbsp;Dr. H. Adrian Bunzel\",\"doi\":\"10.1002/anie.202507031\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p>The ability to create new-to-nature enzymes would substantially advance bioengineering, medicine, and the chemical industry. Despite recent breakthroughs in protein design and structure prediction, designing novel biocatalysts remains challenging. Here, we present AI.zymes, a modular platform integrating cutting-edge protein engineering algorithms within an evolutionary framework (https://github.com/bunzela/AIzymes). By combining bioengineering tools such as Rosetta, ESMFold, ProteinMPNN, and FieldTools in iterative rounds of design and selection, AI.zymes can optimize a broad range of catalytically relevant properties. In addition to enhancing transition state affinity and protein stability, AI.zymes can also improve properties that are not targeted by the employed design algorithms. For instance, AI.zymes can enhance electrostatic catalysis by iteratively selecting variants with stronger catalytic electric fields. Benchmarking AI.zymes on the promiscuous Kemp eliminase activity of ketosteroid isomerase led to a 7.7-fold activity increase after experimentally testing just 7 variants. Due to its modularity, AI.zymes can readily incorporate emerging design algorithms, paving the way for a unifying framework for enzyme design.</p>\",\"PeriodicalId\":125,\"journal\":{\"name\":\"Angewandte Chemie International Edition\",\"volume\":\"64 27\",\"pages\":\"\"},\"PeriodicalIF\":16.1000,\"publicationDate\":\"2025-04-28\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Angewandte Chemie International Edition\",\"FirstCategoryId\":\"92\",\"ListUrlMain\":\"https://onlinelibrary.wiley.com/doi/10.1002/anie.202507031\",\"RegionNum\":1,\"RegionCategory\":\"化学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"CHEMISTRY, MULTIDISCIPLINARY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Angewandte Chemie International Edition","FirstCategoryId":"92","ListUrlMain":"https://onlinelibrary.wiley.com/doi/10.1002/anie.202507031","RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, MULTIDISCIPLINARY","Score":null,"Total":0}
引用次数: 0

摘要

创造新的天然酶的能力将大大推动生物工程、医学和化学工业的发展。尽管最近在蛋白质设计和结构预测方面取得了突破,但设计具有酶样效率的生物催化剂仍然具有挑战性。在这里,我们介绍人工智能。Zymes是一个模块化平台,在进化框架内集成了尖端的蛋白质工程算法。通过将Rosetta, ESMFold, ProteinMPNN和FieldTools等程序结合在设计和选择的迭代轮中,AI。Zymes优化了广泛的催化相关性质。除了增强过渡态亲和力和蛋白质稳定性外,AI。酶还可以改善所采用的设计算法没有针对的特性。例如,人工智能。酶通过迭代选择具有更强催化电场的变体来增强静电催化作用。基准测试人工智能。在实验测试了7个变异后,混杂的Kemp消除酶的酮类固醇异构酶活性增加了7.7倍。由于它的模块化,AI。酶可以很容易地结合新兴的设计算法,为酶设计的统一框架铺平了道路。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

AI.zymes: A Modular Platform for Evolutionary Enzyme Design

AI.zymes: A Modular Platform for Evolutionary Enzyme Design

The ability to create new-to-nature enzymes would substantially advance bioengineering, medicine, and the chemical industry. Despite recent breakthroughs in protein design and structure prediction, designing novel biocatalysts remains challenging. Here, we present AI.zymes, a modular platform integrating cutting-edge protein engineering algorithms within an evolutionary framework (https://github.com/bunzela/AIzymes). By combining bioengineering tools such as Rosetta, ESMFold, ProteinMPNN, and FieldTools in iterative rounds of design and selection, AI.zymes can optimize a broad range of catalytically relevant properties. In addition to enhancing transition state affinity and protein stability, AI.zymes can also improve properties that are not targeted by the employed design algorithms. For instance, AI.zymes can enhance electrostatic catalysis by iteratively selecting variants with stronger catalytic electric fields. Benchmarking AI.zymes on the promiscuous Kemp eliminase activity of ketosteroid isomerase led to a 7.7-fold activity increase after experimentally testing just 7 variants. Due to its modularity, AI.zymes can readily incorporate emerging design algorithms, paving the way for a unifying framework for enzyme design.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
CiteScore
26.60
自引率
6.60%
发文量
3549
审稿时长
1.5 months
期刊介绍: Angewandte Chemie, a journal of the German Chemical Society (GDCh), maintains a leading position among scholarly journals in general chemistry with an impressive Impact Factor of 16.6 (2022 Journal Citation Reports, Clarivate, 2023). Published weekly in a reader-friendly format, it features new articles almost every day. Established in 1887, Angewandte Chemie is a prominent chemistry journal, offering a dynamic blend of Review-type articles, Highlights, Communications, and Research Articles on a weekly basis, making it unique in the field.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:604180095
Book学术官方微信