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Structure-Guided Subunit Interface Engineering to Improve the Catalytic Efficiency of Dimeric Enzymes of FAH Family

文献类型：期刊论文

作者Liang, Bo5; Meng, Chenfei5; Wang, Qian1,4; Du, Yafei5; Luo, Yu5; Zhao, Jixiang5; Wu, Danni2,3,5; Liang, Yajing2,3; Lu, Xuefeng2,3; Yang, Jianming5
刊名JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY
出版日期2025-12-17
卷号73期号:50页码:32094-32106
关键词dimeric enzyme FAH family subunitinterfaceengineering Weimberg pathway alpha-ketoglutaricacid
ISSN号0021-8561
DOI10.1021/acs.jafc.5c09893
通讯作者Liang, Bo(liangbo@qau.edu.cn) ; Liang, Yajing(liangyj@qibebt.ac.cn) ; Lu, Xuefeng(lvxf@qibebt.ac.cn) ; Yang, Jianming(yjming888@126.com)
英文摘要The subunit interface plays a substantial role in the structures and functions of oligomeric enzymes, yet targeted mutations remain difficult to predict. Here, we targeted 2-keto-3-deoxy-d-xylonate dehydratase (CcXylX), the rate-limiting catalyst in the Weimberg pathway for d-xylose catabolism and a member of the fumarylacetoacetate hydrolase (FAH) family, which forms a compact homodimer. Guided by its crystal structure, we engineered the dimer interface and obtained triple mutant L210A/P181Q/Q308A, which showed a 6.04-fold increase in catalytic efficiency. Molecular dynamics simulations revealed that moderate enhancement of intersubunit flexibility accelerates substrate binding. When the mutant was coupled with other Weimberg enzymes in a one-pot process, 77% of d-xylose was converted to 56.05 +/- 0.39 g/L alpha-ketoglutaric acid within 6 h. Moreover, this strategy is also applicable to other dimeric enzymes within the FAH family. This study highlights a promising strategy for engineering dimeric enzymes with a higher catalytic efficiency for producing valuable chemicals.
WOS关键词KETO ACIDS ; THERMOSTABILITY ; METABOLISM ; DESIGN
资助项目Natural Science Foundation of Shandong Province[ZR2025MS127] ; National Natural Science Foundation of China[22278233]
WOS研究方向Agriculture ; Chemistry ; Food Science & Technology
语种英语
WOS记录号WOS:001630991400001
出版者AMER CHEMICAL SOC
源URL[http://ir.qdio.ac.cn/handle/337002/204366]  
专题海洋研究所_实验海洋生物学重点实验室
通讯作者Liang, Bo; Liang, Yajing; Lu, Xuefeng; Yang, Jianming
作者单位1.Chinese Acad Sci, Inst Oceanol, Shandong Prov Key Lab Expt Marine Biol, Qingdao 266071, Shandong, Peoples R China
2.Shandong Energy Inst, Qingdao 266101, Peoples R China
3.Chinese Acad Sci, Qingdao Inst Bioenergy & Bioproc Technol, Shandong Prov Key Lab Synthet Biol, Qingdao 266101, Peoples R China
4.Chinese Acad Sci, CAS, Inst Oceanol, Qingdao 266071, Shandong, Peoples R China
5.Qingdao Agr Univ, Coll Life Sci, Energy Rich Cpds Prod Photosynthet Carbon Fixat Re, Shandong Prov Key Lab Microbial Resource Explorati, Qingdao 266109, Peoples R China
推荐引用方式
GB/T 7714		 Liang, Bo,Meng, Chenfei,Wang, Qian,et al. Structure-Guided Subunit Interface Engineering to Improve the Catalytic Efficiency of Dimeric Enzymes of FAH Family[J]. JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY,2025,73(50):32094-32106.
APA Liang, Bo.,Meng, Chenfei.,Wang, Qian.,Du, Yafei.,Luo, Yu.,...&Yang, Jianming.(2025).Structure-Guided Subunit Interface Engineering to Improve the Catalytic Efficiency of Dimeric Enzymes of FAH Family.JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY,73(50),32094-32106.
MLA Liang, Bo,et al."Structure-Guided Subunit Interface Engineering to Improve the Catalytic Efficiency of Dimeric Enzymes of FAH Family".JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY 73.50(2025):32094-32106.

入库方式： OAI收割

来源：海洋研究所

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