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Comment
. 2015 Sep 15;112(37):11430-1.
doi: 10.1073/pnas.1515239112. Epub 2015 Sep 8.

Allostery vs. "allokairy"

Vincent J Hilser  1 , Jeremy A Anderson  2 , Hesam N Motlagh  2
Affiliations
Comment

Allostery vs. "allokairy"

Vincent J Hilser et al. Proc Natl Acad Sci U S A. .
No abstract available

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Conflict of interest statement

The authors declare no conflict of interest.

Figures

Fig. 1.
Fig. 1.
Allosteric and allokairic regulation. (A) Tunability requires that an enzyme can populate at least two states, depicted here as low-affinity (L) and high-affinity (H) with the ligand represented as the blue oval. (B) In allostery, binding and conformational change are coupled. Binding substrate to one molecule of a dimer, for example, converts both to the high-affinity H state, increasing the binding affinity. (C) In allokairy, the enzyme is in the H state after turnover (upper right) and relaxes back to the L state (lower left) determined by the time between turnover and binding, which depends on substrate concentration ([S]). (D) Allostery (two-site dimer, light gray; four-site tetramer, dark gray) and allokairy (red dashed lines) both lead to S-shaped curves when activity is plotted against substrate concentration. The curves for a fully L state or H state are shown in blue and green (top and bottom). Although both regulation mechanisms produce a sigmoidal change in activity, transitioning from the L state at low [S] to the H state at high [S], cooperativity in allokairy is more tunable (gray shading).
See this image and copyright information in PMC

Comment on

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