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J. Biol. Chem., Vol. 259, Issue 23, 14441-14447, Dec, 1984
A Goldbeter and DE Koshland Jr
A previous analysis of covalent modification systems (Goldbeter, A., and
Koshland, D. E., Jr. (1981) Proc. Natl. Acad. Sci. U. S. A. 78, 6840-6844)
showed that steep transitions in the amount of modified protein can occur
when the converter enzymes are saturated by their protein substrate. This
"zero-order ultrasensitivity" can further be amplified when an effector
acts at more than one step in a monocyclic or multicyclic cascade of
covalent modification. We analyze the limitations of the latter "multistep
ultrasensitivity" and show how it can combine with the zero-order effect to
enhance the sensitivity of biochemical systems controlled by covalent
modification.
Ultrasensitivity in biochemical systems controlled by covalent modification. Interplay between zero-order and multistep effects
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