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Jurkat 2D-LC-MS/MS - Enzyme Kinetics for Complex System Enables Accurate Determination of Specificity Constants of Numerous Substrates in a Mixture by Proteomics Platform

ABSTRACT: We found the ratio of substrate depletion is independent of other coexisted substrates under specific condition with the application of self-developed iteration approach. The further established simplified model was applied to determine the catalytic efficiencies of peptide substrates of a protease in a complex reaction system.

INSTRUMENT(S): LTQ Orbitrap Velos

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): T Cell, Cell Culture

DISEASE(S): Leukemia

SUBMITTER: Zhenzhen Deng

LAB HEAD: Mingliang Ye

PROVIDER: PXD004665 | Pride | 2017-02-08

REPOSITORIES: Pride

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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 Zhenzhen Z Mao Jiawei J Wang Yan Y Zou Hanfa H Ye Mingliang M

Molecular & cellular proteomics : MCP 20161116 1

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 sy ...[more]

PMID: 27852747

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