DICP OpenIR
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
Source PublicationMOLECULAR & CELLULAR PROTEOMICS
2017
DOI10.1074/mcp.M116.062869
Volume16Issue:1Pages:135-145
Indexed BySCI
SubtypeArticle
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
WOS SubjectBiochemical Research Methods
WOS Research AreaBiochemistry & Molecular Biology
WOS KeywordPEPTIDE LIBRARIES ; QUANTITATIVE PROTEOMICS ; PROTEASE ; IDENTIFICATION ; DIGESTION ; ENDONUCLEASE ; DISSOCIATION ; PROTEINS ; COVERAGE ; DATABASE
AbstractMany 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.
Language英语
WOS IDWOS:000392205300011
Citation statistics
Document Type期刊论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/151861
Collection中国科学院大连化学物理研究所
Affiliation1.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
Recommended Citation
GB/T 7714
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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