Quantitative analysis of the time courses of enzyme-catalyzed reactions.
The catalytic properties of enzymes are usually evaluated by measuring and analyzing reaction rates. However, analyzing the complete time course can be advantageous because it contains additional information about the properties of the enzyme. Moreover, for systems that are not at steady state, the analysis of time courses is the preferred method. One of the major barriers to the wide application of time courses is that it may be computationally more difficult to extract information from these experiments. Here the basic approach to analyzing time courses is described, together with some examples of the essential computer code to implement these analyses. A general method that can be applied to both steady state and non-steady-state systems is recommended.
Duggleby
R G
RG
Centre for Protein Structure, Function and Engineering, Department of Biochemistry, The University of Queensland, Brisbane, Queensland, 4072, Australia. duggleby@biosci.uq.edu.au
D001671:Biochemistry / Q000379:methods*; D002384:Catalysis; D004798:Enzymes / Q000737:chemistry*; D008956:Models, Chemical; D008962:Models, Theoretical; D012984:Software; D013997:Time Factors
D004798:Enzymes