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- W3021221566 abstract "This chapter provides an overview of enzyme regulation. Cooperativity has long been considered an intrinsic property of an enzyme. The simplest type of kinetic cooperativity is generated by the cooperation of two free enzyme forms that appear during the reaction process. This situation may occur even with a monomeric one-sited enzyme. In order to observe the occurrence of this cooperativity in time, the reaction process should occur under thermodynamic nonequilibrium conditions and the time scale of the conformational transition should be of the same order as, or slower than, the other reaction steps. Enzyme hysteresis and enzyme memory typically pertain to this situation. For bound enzymes, cooperativity may appear as a systemic property and not as an intrinsic property of an enzyme. If an enzyme that follows Michaelian kinetics with a charged substrate is bound to a charged matrix, electrostatic attraction or repulsion effects may generate apparent positive or negative cooperativity. This cooperativity is clearly not an intrinsic property of the enzyme, but rather a property of the system because of the association of the enzyme with the matrix. The amplitude of these effects depends on the ionic strength of the bulk phase." @default.
- W3021221566 created "2020-05-13" @default.
- W3021221566 creator A5004599075 @default.
- W3021221566 date "1987-01-01" @default.
- W3021221566 modified "2023-10-18" @default.
- W3021221566 title "Enzyme Regulation" @default.
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- W3021221566 doi "https://doi.org/10.1016/b978-0-12-675411-7.50009-4" @default.
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