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Title: Extracting enzyme processivity from kinetic assays

A steady-state analysis for the catalytic turnover of molecules containing two substrate sites is presented. A broad class of Markovian dynamic models, motivated by the action of DNA modifying enzymes and the rich variety of translocation mechanisms associated with these systems (e.g., sliding, hopping, intersegmental transfer, etc.), is considered. The modeling suggests an elementary and general method of data analysis, which enables the extraction of the enzyme’s processivity directly and unambiguously from experimental data. This analysis is not limited to the initial velocity regime. The predictions are validated both against detailed numerical models and by revisiting published experimental data for EcoRI endonuclease acting on DNA.
Authors:
;  [1] ;  [2] ;  [1]
  1. Department of Chemistry and Biochemistry, University of California, Santa Barbara, California 93106 (United States)
  2. (United States)
Publication Date:
OSTI Identifier:
22493308
Resource Type:
Journal Article
Resource Relation:
Journal Name: Journal of Chemical Physics; Journal Volume: 143; Journal Issue: 22; Other Information: (c) 2015 AIP Publishing LLC; Country of input: International Atomic Energy Agency (IAEA)
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL AND ANALYTICAL CHEMISTRY; DATA ANALYSIS; DNA; ENZYMES; EXTRACTION; MARKOV PROCESS; MOLECULES; SIMULATION; STEADY-STATE CONDITIONS; SUBSTRATES; TRANSLOCATION; VELOCITY