{"title":"The allosteric regulation mechanism on the catalytic activity of fructosyltransferase studied by molecular dynamics simulations","authors":"Chaofan Yu, Yanqi Liu, Liang Fu, Zhengyu Shu, Mojie Duan, Yi Zheng","doi":"10.1039/d4cp04131c","DOIUrl":null,"url":null,"abstract":"Fructosyltransferase (FTase) is a key glycosidase with hydrolytic and transglycosylation functions that can utilize sucrose to generate oligofructose (FOS), which is extremely important in the food industry as well as in plants and microorganisms. However, there remain significant gaps in our understanding of the catalytic mechanism of FTase, particularly regarding the regulatory mechanisms of residues on enzyme catalytic activity. In this study, molecular dynamics simulations and immobilized enzyme catalysis experiments were employed to investigate the structural dynamics and catalytic activity of QU10-FTase. The regulations on the structures and activity of QU10-FTase induced by different environments, including the immobilized Fe3O4 interface and solvent temperatures were characterized. The results show that the catalytic activity of QU10-FTase is suppressed by the immobilized Fe3O4. The all-atom MD simulations revealed that the binding sites of QU10-FTase to the Fe3O4 interface are far away from the catalytic triad, but the structures of the catalytic sites are influenced by the interface binding via an allosteric mechanism. The relationship between structure and catalytic activity of QU10-FTase under different temperatures further demonstrated the allosteric regulation in the FTase. Our results not only give the ability to improve the enzyme activity of QU10-FTase to produce FOS but also provide new insights into the allosteric mechanisms of fructosyltransferase.","PeriodicalId":99,"journal":{"name":"Physical Chemistry Chemical Physics","volume":"39 1","pages":""},"PeriodicalIF":2.9000,"publicationDate":"2025-01-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Physical Chemistry Chemical Physics","FirstCategoryId":"92","ListUrlMain":"https://doi.org/10.1039/d4cp04131c","RegionNum":3,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q3","JCRName":"CHEMISTRY, PHYSICAL","Score":null,"Total":0}
引用次数: 0
Abstract
Fructosyltransferase (FTase) is a key glycosidase with hydrolytic and transglycosylation functions that can utilize sucrose to generate oligofructose (FOS), which is extremely important in the food industry as well as in plants and microorganisms. However, there remain significant gaps in our understanding of the catalytic mechanism of FTase, particularly regarding the regulatory mechanisms of residues on enzyme catalytic activity. In this study, molecular dynamics simulations and immobilized enzyme catalysis experiments were employed to investigate the structural dynamics and catalytic activity of QU10-FTase. The regulations on the structures and activity of QU10-FTase induced by different environments, including the immobilized Fe3O4 interface and solvent temperatures were characterized. The results show that the catalytic activity of QU10-FTase is suppressed by the immobilized Fe3O4. The all-atom MD simulations revealed that the binding sites of QU10-FTase to the Fe3O4 interface are far away from the catalytic triad, but the structures of the catalytic sites are influenced by the interface binding via an allosteric mechanism. The relationship between structure and catalytic activity of QU10-FTase under different temperatures further demonstrated the allosteric regulation in the FTase. Our results not only give the ability to improve the enzyme activity of QU10-FTase to produce FOS but also provide new insights into the allosteric mechanisms of fructosyltransferase.
期刊介绍:
Physical Chemistry Chemical Physics (PCCP) is an international journal co-owned by 19 physical chemistry and physics societies from around the world. This journal publishes original, cutting-edge research in physical chemistry, chemical physics and biophysical chemistry. To be suitable for publication in PCCP, articles must include significant innovation and/or insight into physical chemistry; this is the most important criterion that reviewers and Editors will judge against when evaluating submissions.
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