Investigating the origin of high efficiency in confined multienzyme catalysis

被引:64
作者
Cao, Yufei [1 ]
Li, Xiaoyang [1 ]
Xiong, Jiarong [1 ]
Wang, Licheng [1 ]
Yan, Li-Tang [2 ]
Ge, Jun [1 ]
机构
[1] Tsinghua Univ, Dept Chem Engn, Minist Educ, Key Lab Ind Biocatalysis, Beijing 100084, Peoples R China
[2] Tsinghua Univ, Dept Chem Engn, State Key Lab Chem Engn, Beijing 100084, Peoples R China
基金
北京市自然科学基金; 中国国家自然科学基金;
关键词
METAL-ORGANIC FRAMEWORKS; ENZYMATIC INTERESTERIFICATION; OLIVE OIL; CASCADES; ENZYMES; COMPLEX;
D O I
10.1039/c9nr07381g
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
Biomimetic strategies have successfully been applied to confine multiple enzymes on scaffolds to obtain higher catalytic efficiency of enzyme cascades than freely distributed enzymes. However, the origin of high efficiency is poorly understood. We developed a coarse-grained, particle-based model to understand the origin of high efficiency. We found that a reaction intermediate is the key in affecting reaction kinetics. In the case of unstable intermediates, the confinement of multiple enzymes in clusters enhanced the catalytic efficiency and a shorter distance between enzymes resulted in a higher reaction rate and yield. This understanding was verified by co-encapsulating multiple enzymes in metal-organic framework (MOF) nanocrystals as artificially confined multienzyme complexes. The activity enhancement of multiple enzymes in MOFs depended on the distance between enzymes, when the decay of intermediates existed. The finding of this study is useful for designing in vitro synthetic biology systems based on artificial multienzyme complexes.
引用
收藏
页码:22108 / 22117
页数:10
相关论文
共 45 条
[11]   Industrial use of immobilized enzymes [J].
DiCosimo, Robert ;
McAuliffe, Joseph ;
Poulose, Ayrookaran J. ;
Bohlmann, Gregory .
CHEMICAL SOCIETY REVIEWS, 2013, 42 (15) :6437-6474
[12]   Synthetic protein scaffolds provide modular control over metabolic flux [J].
Dueber, John E. ;
Wu, Gabriel C. ;
Malmirchegini, G. Reza ;
Moon, Tae Seok ;
Petzold, Christopher J. ;
Ullal, Adeeti V. ;
Prather, Kristala L. J. ;
Keasling, Jay D. .
NATURE BIOTECHNOLOGY, 2009, 27 (08) :753-U107
[13]   Stable metal-organic frameworks containing single-molecule traps for enzyme encapsulation [J].
Feng, Dawei ;
Liu, Tian-Fu ;
Su, Jie ;
Bosch, Mathieu ;
Wei, Zhangwen ;
Wan, Wei ;
Yuan, Daqiang ;
Chen, Ying-Pin ;
Wang, Xuan ;
Wang, Kecheng ;
Lian, Xizhen ;
Gu, Zhi-Yuan ;
Park, Jihye ;
Zou, Xiaodong ;
Zhou, Hong-Cai .
NATURE COMMUNICATIONS, 2015, 6
[14]   Interenzyme Substrate Diffusion for an Enzyme Cascade Organized on Spatially Addressable DNA Nanostructures [J].
Fu, Jinglin ;
Liu, Minghui ;
Liu, Yan ;
Woodbury, Neal W. ;
Yan, Hao .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 2012, 134 (12) :5516-5519
[15]   Coarse-grained simulation reveals key features of HIV-1 capsid self-assembly [J].
Grime, John M. A. ;
Dama, James F. ;
Ganser-Pornillos, Barbie K. ;
Woodward, Cora L. ;
Jensen, Grant J. ;
Yeager, Mark ;
Voth, Gregory A. .
NATURE COMMUNICATIONS, 2016, 7
[16]   Dissipative particle dynamics: Bridging the gap between atomistic and mesoscopic simulation [J].
Groot, RD ;
Warren, PB .
JOURNAL OF CHEMICAL PHYSICS, 1997, 107 (11) :4423-4435
[17]  
Hyde C. C., 2010, J PHYS CHEM LETT, V1, P1332
[18]  
HYDE CC, 1988, J BIOL CHEM, V263, P17857
[19]   Enzymatic interesterification of palm stearin and coconut oil by a dual lipase system [J].
Ibrahim, Nuzul A. ;
Guo, Zheng ;
Xu, Xuebing .
JOURNAL OF THE AMERICAN OIL CHEMISTS SOCIETY, 2008, 85 (01) :37-45
[20]   Origins of Activity Enhancement in Enzyme Cascades on Scaffolds [J].
Idan, Ofer ;
Hess, Henry .
ACS NANO, 2013, 7 (10) :8658-8665