{"title":"NAC4ED:用于合理设计酶活性和底物选择性的高通量计算平台。","authors":"Chuanxi Zhang, Yinghui Feng, Yiting Zhu, Lei Gong, Hao Wei, Lujia Zhang","doi":"10.1002/mlf2.12154","DOIUrl":null,"url":null,"abstract":"<p><p>In silico computational methods have been widely utilized to study enzyme catalytic mechanisms and design enzyme performance, including molecular docking, molecular dynamics, quantum mechanics, and multiscale QM/MM approaches. However, the manual operation associated with these methods poses challenges for simulating enzymes and enzyme variants in a high-throughput manner. We developed the NAC4ED, a high-throughput enzyme mutagenesis computational platform based on the \"near-attack conformation\" design strategy for enzyme catalysis substrates. This platform circumvents the complex calculations involved in transition-state searching by representing enzyme catalytic mechanisms with parameters derived from near-attack conformations. NAC4ED enables the automated, high-throughput, and systematic computation of enzyme mutants, including protein model construction, complex structure acquisition, molecular dynamics simulation, and analysis of active conformation populations. Validation of the accuracy of NAC4ED demonstrated a prediction accuracy of 92.5% for 40 mutations, showing strong consistency between the computational predictions and experimental results. The time required for automated determination of a single enzyme mutant using NAC4ED is 1/764th of that needed for experimental methods. This has significantly enhanced the efficiency of predicting enzyme mutations, leading to revolutionary breakthroughs in improving the performance of high-throughput screening of enzyme variants. NAC4ED facilitates the efficient generation of a large amount of annotated data, providing high-quality data for statistical modeling and machine learning. NAC4ED is currently available at http://lujialab.org.cn/software/.</p>","PeriodicalId":94145,"journal":{"name":"mLife","volume":"3 4","pages":"505-514"},"PeriodicalIF":4.5000,"publicationDate":"2024-12-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11685835/pdf/","citationCount":"0","resultStr":"{\"title\":\"NAC4ED: A high-throughput computational platform for the rational design of enzyme activity and substrate selectivity.\",\"authors\":\"Chuanxi Zhang, Yinghui Feng, Yiting Zhu, Lei Gong, Hao Wei, Lujia Zhang\",\"doi\":\"10.1002/mlf2.12154\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<p><p>In silico computational methods have been widely utilized to study enzyme catalytic mechanisms and design enzyme performance, including molecular docking, molecular dynamics, quantum mechanics, and multiscale QM/MM approaches. However, the manual operation associated with these methods poses challenges for simulating enzymes and enzyme variants in a high-throughput manner. We developed the NAC4ED, a high-throughput enzyme mutagenesis computational platform based on the \\\"near-attack conformation\\\" design strategy for enzyme catalysis substrates. This platform circumvents the complex calculations involved in transition-state searching by representing enzyme catalytic mechanisms with parameters derived from near-attack conformations. NAC4ED enables the automated, high-throughput, and systematic computation of enzyme mutants, including protein model construction, complex structure acquisition, molecular dynamics simulation, and analysis of active conformation populations. Validation of the accuracy of NAC4ED demonstrated a prediction accuracy of 92.5% for 40 mutations, showing strong consistency between the computational predictions and experimental results. The time required for automated determination of a single enzyme mutant using NAC4ED is 1/764th of that needed for experimental methods. This has significantly enhanced the efficiency of predicting enzyme mutations, leading to revolutionary breakthroughs in improving the performance of high-throughput screening of enzyme variants. NAC4ED facilitates the efficient generation of a large amount of annotated data, providing high-quality data for statistical modeling and machine learning. NAC4ED is currently available at http://lujialab.org.cn/software/.</p>\",\"PeriodicalId\":94145,\"journal\":{\"name\":\"mLife\",\"volume\":\"3 4\",\"pages\":\"505-514\"},\"PeriodicalIF\":4.5000,\"publicationDate\":\"2024-12-25\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC11685835/pdf/\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"mLife\",\"FirstCategoryId\":\"1085\",\"ListUrlMain\":\"https://doi.org/10.1002/mlf2.12154\",\"RegionNum\":0,\"RegionCategory\":null,\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"2024/12/1 0:00:00\",\"PubModel\":\"eCollection\",\"JCR\":\"Q1\",\"JCRName\":\"MICROBIOLOGY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"mLife","FirstCategoryId":"1085","ListUrlMain":"https://doi.org/10.1002/mlf2.12154","RegionNum":0,"RegionCategory":null,"ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"2024/12/1 0:00:00","PubModel":"eCollection","JCR":"Q1","JCRName":"MICROBIOLOGY","Score":null,"Total":0}
NAC4ED: A high-throughput computational platform for the rational design of enzyme activity and substrate selectivity.
In silico computational methods have been widely utilized to study enzyme catalytic mechanisms and design enzyme performance, including molecular docking, molecular dynamics, quantum mechanics, and multiscale QM/MM approaches. However, the manual operation associated with these methods poses challenges for simulating enzymes and enzyme variants in a high-throughput manner. We developed the NAC4ED, a high-throughput enzyme mutagenesis computational platform based on the "near-attack conformation" design strategy for enzyme catalysis substrates. This platform circumvents the complex calculations involved in transition-state searching by representing enzyme catalytic mechanisms with parameters derived from near-attack conformations. NAC4ED enables the automated, high-throughput, and systematic computation of enzyme mutants, including protein model construction, complex structure acquisition, molecular dynamics simulation, and analysis of active conformation populations. Validation of the accuracy of NAC4ED demonstrated a prediction accuracy of 92.5% for 40 mutations, showing strong consistency between the computational predictions and experimental results. The time required for automated determination of a single enzyme mutant using NAC4ED is 1/764th of that needed for experimental methods. This has significantly enhanced the efficiency of predicting enzyme mutations, leading to revolutionary breakthroughs in improving the performance of high-throughput screening of enzyme variants. NAC4ED facilitates the efficient generation of a large amount of annotated data, providing high-quality data for statistical modeling and machine learning. NAC4ED is currently available at http://lujialab.org.cn/software/.