Cleavage of hexopyranose to short-chain carbohydrates plays crucial roles in carbon metabolism and energy supply. Currently, the carbon–carbon bond scission of hexopyranose involves two types of reaction: the widely distributed retro-aldol reaction and the transketo-like reaction observed in Bifidobacteria. Here we report the discovery and characterization of metalloenzyme Art22, which is involved in the sugar moiety modification of aurantinin B (ART B), an antibacterial agent from Bacillus. Art22 adopts a TIM-barrel fold, enabling the activation of 4-keto ART B into potent antibiotic ART B via rapid isomerization. In addition, it protects the ART-producing Bacillus by detoxifying cellular ART B to ART B1–B3 via slow oxidative cleavage of the 3-keto hexopyranose to short-chain carbohydrates and CO2. Guided by structural, mutagenic and computational studies, we reveal an anhydride-mediated mechanism for Art22-catalysed oxygenation reactions, which expands the catalytic repertoire of TIM-barrel enzymes and adds an oxidative path for hexopyranose cleavage. Hexopyranose cleavage is a crucial step in carbon metabolism. Here the authors report the discovery and characterization of metalloenzyme Art22, which is involved in the sugar moiety modification of aurantinin B, an antibacterial agent from Bacillus.
六吡喃糖裂解成短链碳水化合物在碳代谢和能量供应中起着至关重要的作用。目前己吡喃糖的碳-碳键断裂涉及两种反应：广泛分布的反醛醇反应和双歧杆菌中观察到的类转酮反应。本文报道了一种新的金属酶Art22的发现和鉴定，该酶参与了来自芽孢杆菌的一种抗菌剂金菌素B （aurantinin B, ART B）的糖段修饰。Art22采用TIM-barrel折叠，通过快速异构化使4-酮类ART B活化为强效抗生素ART B。此外，它通过将3-酮己糖缓慢氧化裂解为短链碳水化合物和二氧化碳，将细胞中的ART B解毒为ART B1-B3，从而保护产生ART的芽胞杆菌。在结构、诱变和计算研究的指导下，我们揭示了一种酸酐介导的art22催化氧化反应机制，这扩大了tim桶酶的催化范围，并增加了六吡喃糖裂解的氧化途径。六吡喃糖的裂解是碳代谢的关键步骤。本文报道了一种新的金属酶Art22的发现和鉴定，该酶参与了金霉素B的糖段修饰。
{"title":"Oxidative cleavage of hexopyranose by a TIM-barrel isomerase","authors":"Pengwei Li, Dacheng Wang, Lu Guo, Yanru Chen, Huijin Mao, Zelian Zhao, Min Wang, Meng Chen, Zhengren Xu, Binju Wang, Defeng Li, Yihua Chen","doi":"10.1038/s41929-025-01412-8","DOIUrl":"10.1038/s41929-025-01412-8","url":null,"abstract":"Cleavage of hexopyranose to short-chain carbohydrates plays crucial roles in carbon metabolism and energy supply. Currently, the carbon–carbon bond scission of hexopyranose involves two types of reaction: the widely distributed retro-aldol reaction and the transketo-like reaction observed in Bifidobacteria. Here we report the discovery and characterization of metalloenzyme Art22, which is involved in the sugar moiety modification of aurantinin B (ART B), an antibacterial agent from Bacillus. Art22 adopts a TIM-barrel fold, enabling the activation of 4-keto ART B into potent antibiotic ART B via rapid isomerization. In addition, it protects the ART-producing Bacillus by detoxifying cellular ART B to ART B1–B3 via slow oxidative cleavage of the 3-keto hexopyranose to short-chain carbohydrates and CO2. Guided by structural, mutagenic and computational studies, we reveal an anhydride-mediated mechanism for Art22-catalysed oxygenation reactions, which expands the catalytic repertoire of TIM-barrel enzymes and adds an oxidative path for hexopyranose cleavage. Hexopyranose cleavage is a crucial step in carbon metabolism. Here the authors report the discovery and characterization of metalloenzyme Art22, which is involved in the sugar moiety modification of aurantinin B, an antibacterial agent from Bacillus.","PeriodicalId":18845,"journal":{"name":"Nature Catalysis","volume":"8 10","pages":"1010-1022"},"PeriodicalIF":44.6,"publicationDate":"2025-09-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145371978","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-09-24DOI: 10.1038/s41929-025-01415-5
Rudi Fasan
The 2025 RepArtZymes conference featured the latest developments in the design and development of artificial and repurposed enzymes for synthetic and biotechnological applications. These contributions illustrate the impact of this rapidly expanding research area towards addressing key challenges in organic synthesis, medicinal chemistry, polymer chemistry, energy conversion, and environmental remediation.
{"title":"Pushing the boundaries of biocatalysis","authors":"Rudi Fasan","doi":"10.1038/s41929-025-01415-5","DOIUrl":"10.1038/s41929-025-01415-5","url":null,"abstract":"The 2025 RepArtZymes conference featured the latest developments in the design and development of artificial and repurposed enzymes for synthetic and biotechnological applications. These contributions illustrate the impact of this rapidly expanding research area towards addressing key challenges in organic synthesis, medicinal chemistry, polymer chemistry, energy conversion, and environmental remediation.","PeriodicalId":18845,"journal":{"name":"Nature Catalysis","volume":"8 9","pages":"867-869"},"PeriodicalIF":44.6,"publicationDate":"2025-09-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145129518","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-09-24DOI: 10.1038/s41929-025-01401-x
Dmitry Yu. Murzin
Adsorption on solid surfaces is extremely important for various phenomena and applications. In the 1910s, adsorption and subsequent catalysis was described mainly in terms of diffusion through a fluid film to the interface. Langmuir developed the concept of a monolayer adsorption, which became the cornerstone of modern surface science.
{"title":"From isotherms to modern kinetics","authors":"Dmitry Yu. Murzin","doi":"10.1038/s41929-025-01401-x","DOIUrl":"10.1038/s41929-025-01401-x","url":null,"abstract":"Adsorption on solid surfaces is extremely important for various phenomena and applications. In the 1910s, adsorption and subsequent catalysis was described mainly in terms of diffusion through a fluid film to the interface. Langmuir developed the concept of a monolayer adsorption, which became the cornerstone of modern surface science.","PeriodicalId":18845,"journal":{"name":"Nature Catalysis","volume":"8 9","pages":"861-862"},"PeriodicalIF":44.6,"publicationDate":"2025-09-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145129523","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-09-24DOI: 10.1038/s41929-025-01400-y
Peter Westh, Jeppe Kari
The 1913 study ‘Die Kinetik der Invertinwirkung’, by Michaelis and Menten, marked a pivotal advancement in enzymology by illustrating the application of mechanistic models and quantitative kinetics to biocatalysis. The foundational framework described back then continues to have a strong impact on enzymology, with profound influences that range from undergraduate education to structure–function studies and the format and content of contemporary kinetic databases.
1913年Michaelis和Menten的研究“Die Kinetik der Invertinwirkung”，通过说明机理模型和定量动力学在生物催化中的应用，标志着酶学的关键进步。当时描述的基本框架继续对酶学产生强烈的影响，从本科教育到结构-功能研究以及当代动力学数据库的格式和内容都产生了深远的影响。
{"title":"From descriptive to quantitative biocatalysis","authors":"Peter Westh, Jeppe Kari","doi":"10.1038/s41929-025-01400-y","DOIUrl":"10.1038/s41929-025-01400-y","url":null,"abstract":"The 1913 study ‘Die Kinetik der Invertinwirkung’, by Michaelis and Menten, marked a pivotal advancement in enzymology by illustrating the application of mechanistic models and quantitative kinetics to biocatalysis. The foundational framework described back then continues to have a strong impact on enzymology, with profound influences that range from undergraduate education to structure–function studies and the format and content of contemporary kinetic databases.","PeriodicalId":18845,"journal":{"name":"Nature Catalysis","volume":"8 9","pages":"859-860"},"PeriodicalIF":44.6,"publicationDate":"2025-09-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145129522","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-09-24DOI: 10.1038/s41929-025-01413-7
A TIM-barrel metalloenzyme — Art22 — involved in the sugar-moiety modification of the antibiotic aurantinin B (ART B) has been discovered. This enzyme activates 4-keto ART B to ART B through rapid isomerization. Additionally, Art22 slowly converts ART B into inactive products through oxidative cleavage of the 3-keto hexopyranose.
{"title":"A TIM-barrel metalloenzyme with sugar-cleavage activity","authors":"","doi":"10.1038/s41929-025-01413-7","DOIUrl":"10.1038/s41929-025-01413-7","url":null,"abstract":"A TIM-barrel metalloenzyme — Art22 — involved in the sugar-moiety modification of the antibiotic aurantinin B (ART B) has been discovered. This enzyme activates 4-keto ART B to ART B through rapid isomerization. Additionally, Art22 slowly converts ART B into inactive products through oxidative cleavage of the 3-keto hexopyranose.","PeriodicalId":18845,"journal":{"name":"Nature Catalysis","volume":"8 10","pages":"984-985"},"PeriodicalIF":44.6,"publicationDate":"2025-09-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145371951","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Pub Date : 2025-09-24DOI: 10.1038/s41929-025-01410-w
Jiri Damborsky, Petr Kouba, Josef Sivic, Michal Vasina, David Bednar, Stanislav Mazurenko
Quantum computing, by leveraging the unique principles of quantum mechanics, offers transformative potential for biocatalysis and related disciplines. Compared to classical algorithms, quantum algorithms deliver immense acceleration to quantum computers, making them suited for tackling computationally challenging problems such as simulating many-body biomolecular systems or enzyme-catalysed chemical reactions. However, current quantum hardware is constrained by noise, limited qubit coherence and high error rates, restricting its capacity to model complex biochemical phenomena. Here we explore the rapidly advancing landscape of quantum computing and its future applications in the discovery and rational engineering of biocatalysts. We identify key areas where quantum algorithms could surpass classical limitations, including the quantum chemistry-based design of biocatalysts with enhanced catalytic activity or selectivity, parallelized mining of novel enzymes, accurate ancestral sequence reconstruction, and combinatorial in silico protein evolution. Overcoming current hardware limitations could unlock transformative advances in both fundamental enzymology and industrial bioprocessing. Quantum computing is a promising technology to solve complex challenges that would take classical computers an impractical amount of time. This Perspective discusses the current state of quantum computing and possible applications in enzyme engineering and biocatalysis.
{"title":"Quantum computing for faster enzyme discovery and engineering","authors":"Jiri Damborsky, Petr Kouba, Josef Sivic, Michal Vasina, David Bednar, Stanislav Mazurenko","doi":"10.1038/s41929-025-01410-w","DOIUrl":"10.1038/s41929-025-01410-w","url":null,"abstract":"Quantum computing, by leveraging the unique principles of quantum mechanics, offers transformative potential for biocatalysis and related disciplines. Compared to classical algorithms, quantum algorithms deliver immense acceleration to quantum computers, making them suited for tackling computationally challenging problems such as simulating many-body biomolecular systems or enzyme-catalysed chemical reactions. However, current quantum hardware is constrained by noise, limited qubit coherence and high error rates, restricting its capacity to model complex biochemical phenomena. Here we explore the rapidly advancing landscape of quantum computing and its future applications in the discovery and rational engineering of biocatalysts. We identify key areas where quantum algorithms could surpass classical limitations, including the quantum chemistry-based design of biocatalysts with enhanced catalytic activity or selectivity, parallelized mining of novel enzymes, accurate ancestral sequence reconstruction, and combinatorial in silico protein evolution. Overcoming current hardware limitations could unlock transformative advances in both fundamental enzymology and industrial bioprocessing. Quantum computing is a promising technology to solve complex challenges that would take classical computers an impractical amount of time. This Perspective discusses the current state of quantum computing and possible applications in enzyme engineering and biocatalysis.","PeriodicalId":18845,"journal":{"name":"Nature Catalysis","volume":"8 9","pages":"872-880"},"PeriodicalIF":44.6,"publicationDate":"2025-09-24","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145129519","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"化学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
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