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. Author manuscript; available in PMC: 2018 Jan 1.
Published in final edited form as: Methods Enzymol. 2016 Dec 7;584:229–253. doi: 10.1016/bs.mie.2016.10.025

Table 1.

DETERGENT MICELLE SYSTEM PROPERTIES IMPLICATIONS FOR KINETIC ANALYSIS
Sequestration: enzyme and substrate are in separate detergent
micelles
Imicellar fusion/fission rates introduce additional and unaccounted
kinetic step
Micelle Dilution Effect: concentration of micelles is the effective
'volume' of the reaction
kinetic parameters scale with both type and concentration of
detergent, not just concentration of proteins
Cooperativity: detergents self-associate in a strongly cooperative
manner
danger of misappropriating cooperativity to enzyme:substrate
interaction
Solubility: limit of solubility imposed by maximal protein:detergent
ratios
substrate solubility limit and/or distorted micelle structure may
plateau reaction rates before enzyme is truly saturated
Altered Dynamics: increased protein dynamics in detergent cleavage at ectopic sites in substrates or even non-substrates
Accessibility: altered accessibility of inhibitors to enzyme active-
site
loverestimation of inhibitor efficacies
Altered Conformation: non-native environment changes enzyme
conformation/function
catalysis may be enhanced, diminished, or even disallowed
Enzyme Bias: only some intramembrane proteases are active in
detergent (many require a membrane environment)
kinetic properties of the subset of enzymes active in detergent
may not be generally applicable to entire class of proteases