An amplified sensitivity arising from covalent modification in biological systems.
نویسندگان
چکیده
The transient and steady-state behavior of a reversible covalent modification system is examined. When the modifying enzymes operate outside the region of first-order kinetics, small percentage changes in the concentration of the effector controlling either of the modifying enzymes can give much larger percentage changes in the amount of modified protein. This amplification of the response to a stimulus can provide additional sensitivity in biological control, equivalent to that of allosteric proteins with high Hill coefficients.
منابع مشابه
Ultrasensitivity in biochemical systems controlled by covalent modification. Interplay between zero-order and multistep effects.
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...
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ورودعنوان ژورنال:
- Proceedings of the National Academy of Sciences of the United States of America
دوره 78 11 شماره
صفحات -
تاریخ انتشار 1981