ACS Synthetic Biology最新文献

{"title":"Establishing a High-Yield Bacillus subtilis-Based Cell-Free Protein Synthesis System for In Vitro Prototyping and Natural Product Biosynthesis","authors":"Xiangyang Ji,&nbsp;Wan-Qiu Liu,&nbsp;Zhiling Cao,&nbsp;Shuhui Huang and Jian Li*,&nbsp;","doi":"10.1021/acssynbio.5c0002110.1021/acssynbio.5c00021","DOIUrl":"https://doi.org/10.1021/acssynbio.5c00021https://doi.org/10.1021/acssynbio.5c00021","url":null,"abstract":"<p >Cell-free systems are emerging as powerful platforms for synthetic biology with widespread applications in both fundamental research, such as artificial cell construction, and practical uses like recombinant protein production. Among these, cell-free protein synthesis (CFPS) plays a crucial role in gene expression for various downstream applications. However, the development of CFPS systems based on certain chassis, such as <i>Bacillus subtilis</i>, still remains limited due to their low in vitro productivity. Here, we report the development of a highly productive CFPS system derived from an engineered <i>B. subtilis</i> 164T7P strain, which contains a genomic integration of the T7 RNA polymerase gene. This modification allows the preparation of cell extracts that inherently contain T7 RNA polymerase, enabling T7 promoter-based transcription without the supplementation of purified T7 RNA polymerase in CFPS reactions. Through systematic optimization of cell extract preparation and key reaction parameters, we achieved the synthesis of 286 ± 16.7 μg/mL of sfGFP in batch reactions, with yields increasing to over 1100 μg/mL in a semicontinuous format that can replenish substrates and remove inhibitory byproducts. We further demonstrated the system’s versatility by using it for two synthetic biology applications: prototyping ribosome binding site (RBS) elements and synthesizing pulcherriminic acid─a bioactive cyclodipeptide. The system successfully characterized RBS performance, with in vitro and in vivo rankings correlating with predicted strengths, and expressed two active biosynthetic enzymes (cyclodipeptide synthase─YvmC and cytochrome P450 enzyme─CypX), leading to the production of pulcherriminic acid. Overall, our <i>B. subtilis</i>-based CFPS system offers a robust platform for high-yield protein synthesis, in vitro prototyping of gene regulatory elements, and natural product biosynthesis, highlighting its broad potential for synthetic biology and biotechnology applications.</p>","PeriodicalId":26,"journal":{"name":"ACS Synthetic Biology","volume":"14 4","pages":"1288–1297 1288–1297"},"PeriodicalIF":3.7,"publicationDate":"2025-04-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143842496","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Concentration-Dependent CsrA Regulation of the uxuB Transcript Leads to Development of a Post-Transcriptional Bandpass Filter","authors":"Alejandra M. Rojano-Nisimura,&nbsp;Trevor R. Simmons,&nbsp;Alexandra J. Lukasiewicz,&nbsp;Ryan Buchser,&nbsp;Josie S. Ruzek,&nbsp;Jacqueline L. Avila and Lydia M. Contreras*,&nbsp;","doi":"10.1021/acssynbio.4c0066810.1021/acssynbio.4c00668","DOIUrl":"https://doi.org/10.1021/acssynbio.4c00668https://doi.org/10.1021/acssynbio.4c00668","url":null,"abstract":"<p >Post-transcriptional control systems offer new avenues for designing synthetic circuits that provide reduced burden and fewer synthetic regulatory components compared to transcriptionally based tools. Herein, we repurpose a newly identified post-transcriptional interaction between the <i>uxuB</i> mRNA transcript, specifically the 5’ UTR + 100 nucleotides of coding sequence (100 nt CDS), and the <i>E. coli</i> Carbon Storage Regulatory A (CsrA) protein to design a biological post-transcriptional bandpass filter. In this work, we characterize <i>the uxuB</i> mRNA as a heterogeneous target of CsrA, where the protein can both activate and repress <i>uxuB</i> activity depending on its intracellular concentration. We leverage this interaction to implement a novel strategy of regulation within the 5’ UTR of an mRNA. Specifically, we report a hierarchical binding strategy that may be leveraged by CsrA within <i>uxuB</i> to produce a dose-dependent response in regulatory outcomes. In our semisynthetic circuit, the <i>uxuB</i> 5’ UTR + 100 nt CDS sequence is used as a scaffold that is fused to a gene of interest, which allows the circuit to transition between ON/OFF states based on the concentration range of free natively expressed CsrA. Notably, this system exerts regulation comparable to previously developed transcriptional bandpass filters while reducing the number of synthetic circuit components and can be used in concert with additional post-transcriptionally controlled circuits to achieve complex multi-signal control. We anticipate that future characterization of native regulatory RNA-protein systems will enable the development of more complex RNP-based circuits for synthetic biology applications.</p>","PeriodicalId":26,"journal":{"name":"ACS Synthetic Biology","volume":"14 4","pages":"1084–1098 1084–1098"},"PeriodicalIF":3.7,"publicationDate":"2025-04-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143842171","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Concentration-Dependent CsrA Regulation of the <i>uxuB</i> Transcript Leads to Development of a Post-Transcriptional Bandpass Filter.","authors":"Alejandra M Rojano-Nisimura, Trevor R Simmons, Alexandra J Lukasiewicz, Ryan Buchser, Josie S Ruzek, Jacqueline L Avila, Lydia M Contreras","doi":"10.1021/acssynbio.4c00668","DOIUrl":"https://doi.org/10.1021/acssynbio.4c00668","url":null,"abstract":"<p><p>Post-transcriptional control systems offer new avenues for designing synthetic circuits that provide reduced burden and fewer synthetic regulatory components compared to transcriptionally based tools. Herein, we repurpose a newly identified post-transcriptional interaction between the <i>uxuB</i> mRNA transcript, specifically the 5' UTR + 100 nucleotides of coding sequence (100 nt CDS), and the <i>E. coli</i> Carbon Storage Regulatory A (CsrA) protein to design a biological post-transcriptional bandpass filter. In this work, we characterize <i>the uxuB</i> mRNA as a heterogeneous target of CsrA, where the protein can both activate and repress <i>uxuB</i> activity depending on its intracellular concentration. We leverage this interaction to implement a novel strategy of regulation within the 5' UTR of an mRNA. Specifically, we report a hierarchical binding strategy that may be leveraged by CsrA within <i>uxuB</i> to produce a dose-dependent response in regulatory outcomes. In our semisynthetic circuit, the <i>uxuB</i> 5' UTR + 100 nt CDS sequence is used as a scaffold that is fused to a gene of interest, which allows the circuit to transition between ON/OFF states based on the concentration range of free natively expressed CsrA. Notably, this system exerts regulation comparable to previously developed transcriptional bandpass filters while reducing the number of synthetic circuit components and can be used in concert with additional post-transcriptionally controlled circuits to achieve complex multi-signal control. We anticipate that future characterization of native regulatory RNA-protein systems will enable the development of more complex RNP-based circuits for synthetic biology applications.</p>","PeriodicalId":26,"journal":{"name":"ACS Synthetic Biology","volume":" ","pages":""},"PeriodicalIF":3.7,"publicationDate":"2025-04-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143810152","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Fundamental Trade-Offs in the Robustness of Biological Systems with Feedback Regulation.","authors":"Nguyen Hoai Nam Tran, An Nguyen, Tasfia Wasima Rahman, Ania-Ariadna Baetica","doi":"10.1021/acssynbio.4c00704","DOIUrl":"https://doi.org/10.1021/acssynbio.4c00704","url":null,"abstract":"<p><p>Natural biological systems use feedback regulation to effectively respond and adapt to their changing environment. Even though in engineered systems we understand how accurate feedback can be depending on the electronic or mechanical parts that it is implemented with, we largely lack a similar theoretical framework to study feedback regulation in biological systems. Specifically, it is not fully understood or quantified how accurate or robust the implementation of biological feedback actually is. In this paper, we study the sensitivity of biological feedback to variations in biochemical parameters using five example circuits: positive autoregulation, negative autoregulation, double-positive feedback, positive-negative feedback, and double-negative feedback (the toggle switch). We find that some of these examples of biological feedback are subjected to fundamental performance trade-offs, and we propose multi-objective optimization as a framework to study their properties. The impact of this work is to improve robust circuit design for synthetic biology and to improve our understanding of feedback for systems biology.</p>","PeriodicalId":26,"journal":{"name":"ACS Synthetic Biology","volume":" ","pages":""},"PeriodicalIF":3.7,"publicationDate":"2025-04-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143810191","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Thermostable Coenzyme a Ligase for Efficient Biosynthesis of 2-Pyrrolidone via Protein and Fermentation Engineering.","authors":"Bicheng Yu, Wei Song, Shenjie Wang, Wanqing Wei, Guipeng Hu, Xiaomin Li, Cong Gao, Jia Liu, Jian Wen, Jing Wu","doi":"10.1021/acssynbio.5c00092","DOIUrl":"https://doi.org/10.1021/acssynbio.5c00092","url":null,"abstract":"<p><p>2-Pyrrolidone is an important chemical intermediate with broad applications in the materials and pharmaceutical industries. Traditional petrochemical synthesis methods pose significant environmental challenges. In the case of biosynthesis, the limited thermostability of coenzyme A ligase (CaiC) represents a major barrier to industrial-scale production. This study focused on enhancing the thermostability and catalytic efficiency of EcCaiC through protein engineering. Conserved sequences were identified, and flexible regions were targeted for virtual mutagenesis using FoldX and Rosetta. The resulting mutant, M3, exhibited a 7.86-fold increase in half-life(<i>t</i>_1/2) at 55 °C and a <i>T</i>_m of 59.3 °C. Additionally, the catalytic efficiency (<i>k</i>_cat/<i>K</i>_m) of M3 improved by 52.8%, reaching 5.73 mM^-1 s^-1 compared to the wild type. Subsequently, EcCaiC^M3 was introduced into <i>Corynebacterium glutamicum</i> S9114, with targeted knockout of byproduct synthesis genes. Finally, fed-batch fermentation in a 5 L bioreactor achieved a 2-pyrrolidone yield of 58.28 g/L, a glucose conversion rate of 0.32 g/g, and a productivity of 0.97 g/L/h. This work establishes an efficient biosynthetic platform for 2-pyrrolidone, providing a robust foundation for its industrial production.</p>","PeriodicalId":26,"journal":{"name":"ACS Synthetic Biology","volume":" ","pages":""},"PeriodicalIF":3.7,"publicationDate":"2025-04-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143810193","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Fundamental Trade-Offs in the Robustness of Biological Systems with Feedback Regulation","authors":"Nguyen Hoai Nam Tran,&nbsp;An Nguyen,&nbsp;Tasfia Wasima Rahman and Ania-Ariadna Baetica*,&nbsp;","doi":"10.1021/acssynbio.4c0070410.1021/acssynbio.4c00704","DOIUrl":"https://doi.org/10.1021/acssynbio.4c00704https://doi.org/10.1021/acssynbio.4c00704","url":null,"abstract":"<p >Natural biological systems use feedback regulation to effectively respond and adapt to their changing environment. Even though in engineered systems we understand how accurate feedback can be depending on the electronic or mechanical parts that it is implemented with, we largely lack a similar theoretical framework to study feedback regulation in biological systems. Specifically, it is not fully understood or quantified how accurate or robust the implementation of biological feedback actually is. In this paper, we study the sensitivity of biological feedback to variations in biochemical parameters using five example circuits: positive autoregulation, negative autoregulation, double-positive feedback, positive–negative feedback, and double-negative feedback (the toggle switch). We find that some of these examples of biological feedback are subjected to fundamental performance trade-offs, and we propose multi-objective optimization as a framework to study their properties. The impact of this work is to improve robust circuit design for synthetic biology and to improve our understanding of feedback for systems biology.</p>","PeriodicalId":26,"journal":{"name":"ACS Synthetic Biology","volume":"14 4","pages":"1099–1111 1099–1111"},"PeriodicalIF":3.7,"publicationDate":"2025-04-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://pubs.acs.org/doi/epdf/10.1021/acssynbio.4c00704","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143842420","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Thermostable Coenzyme a Ligase for Efficient Biosynthesis of 2-Pyrrolidone via Protein and Fermentation Engineering","authors":"Bicheng Yu,&nbsp;Wei Song*,&nbsp;Shenjie Wang,&nbsp;Wanqing Wei,&nbsp;Guipeng Hu,&nbsp;Xiaomin Li,&nbsp;Cong Gao,&nbsp;Jia Liu,&nbsp;Jian Wen and Jing Wu*,&nbsp;","doi":"10.1021/acssynbio.5c0009210.1021/acssynbio.5c00092","DOIUrl":"https://doi.org/10.1021/acssynbio.5c00092https://doi.org/10.1021/acssynbio.5c00092","url":null,"abstract":"<p >2-Pyrrolidone is an important chemical intermediate with broad applications in the materials and pharmaceutical industries. Traditional petrochemical synthesis methods pose significant environmental challenges. In the case of biosynthesis, the limited thermostability of coenzyme A ligase (CaiC) represents a major barrier to industrial-scale production. This study focused on enhancing the thermostability and catalytic efficiency of EcCaiC through protein engineering. Conserved sequences were identified, and flexible regions were targeted for virtual mutagenesis using FoldX and Rosetta. The resulting mutant, M3, exhibited a 7.86-fold increase in half-life(<i>t</i>_1/2) at 55 °C and a <i>T</i>_m of 59.3 °C. Additionally, the catalytic efficiency (<i>k</i>_cat/<i>K</i>_m) of M3 improved by 52.8%, reaching 5.73 mM^–1 s^–1 compared to the wild type. Subsequently, EcCaiC^M3 was introduced into <i>Corynebacterium glutamicum</i> S9114, with targeted knockout of byproduct synthesis genes. Finally, fed-batch fermentation in a 5 L bioreactor achieved a 2-pyrrolidone yield of 58.28 g/L, a glucose conversion rate of 0.32 g/g, and a productivity of 0.97 g/L/h. This work establishes an efficient biosynthetic platform for 2-pyrrolidone, providing a robust foundation for its industrial production.</p>","PeriodicalId":26,"journal":{"name":"ACS Synthetic Biology","volume":"14 4","pages":"1298–1308 1298–1308"},"PeriodicalIF":3.7,"publicationDate":"2025-04-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143842372","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Metabolic Engineering of <i>Escherichia coli</i> for the Improved Malonic Acid Production.","authors":"Han Liu, Mengzhen Tian, Ping Dong, Yunying Zhao, Yu Deng","doi":"10.1021/acssynbio.5c00005","DOIUrl":"https://doi.org/10.1021/acssynbio.5c00005","url":null,"abstract":"<p><p>Malonic acid (MA) is a high-value chemical with diverse applications in the fields of food, agriculture, medicine, and chemical synthesis. Despite the successful biosynthesis of MA has been performed in <i><i>Escherichia coli</i></i>, <i>Myceliophthora thermophila</i>, and <i>Saccharomyces cerevisiae</i>, the resulting MA titers remain insufficient for industrial-scale production. In this study, three distinct metabolic pathways were designed and constructed to increase MA production in <i><i>E. coli</i></i>. Among these, the fumaric acid pathway comprising four key enzymes including the aspartase (AspA), the decarboxylase (PanD), the β-alanine-pyruvate transaminase (Pa0132), and the succinic aldehyde dehydrogenase (YneI) was identified as the most effective for MA production. Additionally, the supplementation of fumaric acid was found to significantly improve MA production. To further enhance the MA production, metabolic engineering strategies were employed, including the deletion of the <i>ydfG</i> gene, responsible for encoding the malonic semialdehyde reductase, and the <i>ptsG</i> gene, which encodes a glucose transporter. Finally, through the optimization of fermentation conditions and feeding strategies, the engineered strain achieved an MA titer of 1.4 g/L in shake flask and 17.8 g/L in fed-batch fermentation. This study provides new insights into the industrial-scale production of MA utilizing the metabolically engineered <i><i>E. coli</i></i> cells.</p>","PeriodicalId":26,"journal":{"name":"ACS Synthetic Biology","volume":" ","pages":""},"PeriodicalIF":3.7,"publicationDate":"2025-04-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143802013","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Metabolic Engineering of Escherichia coli for the Improved Malonic Acid Production","authors":"Han Liu,&nbsp;Mengzhen Tian,&nbsp;Ping Dong,&nbsp;Yunying Zhao* and Yu Deng*,&nbsp;","doi":"10.1021/acssynbio.5c0000510.1021/acssynbio.5c00005","DOIUrl":"https://doi.org/10.1021/acssynbio.5c00005https://doi.org/10.1021/acssynbio.5c00005","url":null,"abstract":"<p >Malonic acid (MA) is a high-value chemical with diverse applications in the fields of food, agriculture, medicine, and chemical synthesis. Despite the successful biosynthesis of MA has been performed in <i><i>Escherichia coli</i></i>, <i>Myceliophthora thermophila</i>, and <i>Saccharomyces cerevisiae</i>, the resulting MA titers remain insufficient for industrial-scale production. In this study, three distinct metabolic pathways were designed and constructed to increase MA production in <i><i>E. coli</i></i>. Among these, the fumaric acid pathway comprising four key enzymes including the aspartase (AspA), the decarboxylase (PanD), the β-alanine-pyruvate transaminase (Pa0132), and the succinic aldehyde dehydrogenase (YneI) was identified as the most effective for MA production. Additionally, the supplementation of fumaric acid was found to significantly improve MA production. To further enhance the MA production, metabolic engineering strategies were employed, including the deletion of the <i>ydfG</i> gene, responsible for encoding the malonic semialdehyde reductase, and the <i>ptsG</i> gene, which encodes a glucose transporter. Finally, through the optimization of fermentation conditions and feeding strategies, the engineered strain achieved an MA titer of 1.4 g/L in shake flask and 17.8 g/L in fed-batch fermentation. This study provides new insights into the industrial-scale production of MA utilizing the metabolically engineered <i><i>E. coli</i></i> cells.</p>","PeriodicalId":26,"journal":{"name":"ACS Synthetic Biology","volume":"14 4","pages":"1277–1287 1277–1287"},"PeriodicalIF":3.7,"publicationDate":"2025-04-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143842283","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Redesigning CYP109E1 for Improving Catalytic Performance in 25-Hydroxyvitamin D3 Synthesis Through Synergistic Enhancement of Electron Transfer and NADPH Regeneration","authors":"Jiaying Ai,&nbsp;Ziyang Yin,&nbsp;Jikai Gao,&nbsp;Wenjing Wang,&nbsp;Fuping Lu*,&nbsp;Hui-Min Qin* and Shuhong Mao*,&nbsp;","doi":"10.1021/acssynbio.4c0087910.1021/acssynbio.4c00879","DOIUrl":"https://doi.org/10.1021/acssynbio.4c00879https://doi.org/10.1021/acssynbio.4c00879","url":null,"abstract":"<p >P450 enzymes are promising biocatalysts and play an important role in the field of drug synthesis due to their high catalytic activity and stereoselectivity. CYP109E1 from <i>Bacillus megaterium</i> was used to convert VD₃ for the production of 25(OH)VD₃. However, the industrial production was still limited due to the low catalytic performance of CYP109E1. To overcome this, we constructed an engineered strain containing a modified CYP109E1 coupled with an efficient electron transfer chain and NADPH regeneration system. First, Adx_4–108T69E-Fpr was identified as the most compatible redox partner for the enzyme based on in-silico analysis. Then, targeted mutations were introduced at the substrate channel of CYP109E1, resulting in higher production efficiency. Next, the production of 25(OH)VD₃ was increased by 13.1% after introducing a double Adx_4–108T69E expression cassette. Finally, an NADPH regeneration system was introduced by overexpressing <i>zwf</i>, which increased the yield of 25(OH)VD₃ 48.7%. These results demonstrate that recombinant <i>Escherichia coli</i> BL21 (DE3) coexpressing CYP109E1_R70A-ZWF and 2Adx_4–108T69Es-Fpr is an efficient whole-cell biocatalyst for the synthesis of 25(OH)VD₃, illustrating an attractive strategy for improving the catalytic efficiency of P450 enzymes.</p>","PeriodicalId":26,"journal":{"name":"ACS Synthetic Biology","volume":"14 4","pages":"1240–1249 1240–1249"},"PeriodicalIF":3.7,"publicationDate":"2025-04-04","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143842488","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":2,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}