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Enzyme Kinetics for Complex System Enables Accurate Determination of Specificity Constants of Numerous Substrates in a Mixture by Proteomics Platform
Deng, Zhenzhen1,2; Mao, Jiawei1,2; Wang, Yan1,2; Zou, Hanfa1; Ye, Mingliang1
刊名MOLECULAR & CELLULAR PROTEOMICS
2017
DOI10.1074/mcp.M116.062869
16期:1页:135-145
收录类别SCI
文章类型Article
WOS标题词Science & Technology ; Life Sciences & Biomedicine
类目[WOS]Biochemical Research Methods
研究领域[WOS]Biochemistry & Molecular Biology
关键词[WOS]PEPTIDE LIBRARIES ; QUANTITATIVE PROTEOMICS ; PROTEASE ; IDENTIFICATION ; DIGESTION ; ENDONUCLEASE ; DISSOCIATION ; PROTEINS ; COVERAGE ; DATABASE
英文摘要Many important experiments in proteomics including protein digestion, enzyme substrate screening, enzymatic labeling, etc., involve the enzymatic reactions in a complex system where numerous substrates coexists with an enzyme. However, the enzyme kinetics in such a system remains unexplored and poorly understood. Herein, we derived and validated the kinetics equations for the enzymatic reactions in complex system. We developed an iteration approach to depict the enzymatic reactions in complex system. It was validated by 630 time-course points from 24 enzymatic reaction experiments and was demonstrated to be a powerful tool to simulate the reactions in the complex system. By applying this approach, we found that the ratio of substrate depletion is independent of other coexisted substrates under specific condition. This observation was then validated by experiments. Based on this striking observation, a simplified model was developed to determine the catalytic efficiencies of numerous competing substrates presented in the complex enzyme reaction system. When coupled with high-throughput quantitative proteomics technique, this simplified model enabled the accurate determination of catalytic efficiencies for 2369 peptide substrates of a protease by using only one enzymatic reaction experiment. Thus, this study provided, in the first time, a validated model for the large scale determination of specificity constants which could enable the enzyme substrate screening approach turned from a qualitative method of identifying substrates to a quantitative method of identifying and prioritizing substrates. Data are available via ProteomeXchange with identifier PXDO04665.
语种英语
WOS记录号WOS:000392205300011
引用统计
文献类型期刊论文
条目标识符http://cas-ir.dicp.ac.cn/handle/321008/151861
专题中国科学院大连化学物理研究所
作者单位1.Chinese Acad Sci, Dalian Inst Chem Phys, Key Lab Separat Sci Analyt Chem, Dalian 116023, Peoples R China
2.Chinese Acad Sci, Grad Sch, Beijing 100049, Peoples R China
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Deng, Zhenzhen,Mao, Jiawei,Wang, Yan,et al. Enzyme Kinetics for Complex System Enables Accurate Determination of Specificity Constants of Numerous Substrates in a Mixture by Proteomics Platform[J]. MOLECULAR & CELLULAR PROTEOMICS,2017,16(1):135-145.
APA Deng, Zhenzhen,Mao, Jiawei,Wang, Yan,Zou, Hanfa,&Ye, Mingliang.(2017).Enzyme Kinetics for Complex System Enables Accurate Determination of Specificity Constants of Numerous Substrates in a Mixture by Proteomics Platform.MOLECULAR & CELLULAR PROTEOMICS,16(1),135-145.
MLA Deng, Zhenzhen,et al."Enzyme Kinetics for Complex System Enables Accurate Determination of Specificity Constants of Numerous Substrates in a Mixture by Proteomics Platform".MOLECULAR & CELLULAR PROTEOMICS 16.1(2017):135-145.
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