[Deviations from hyperbolic kinetics in slowly dissociating allosteric enzyme systems].

B I Kuranov; A I Dorozhko; Z S Kagan; V A Iakovlev

PubMed · 1203389

[Deviations from hyperbolic kinetics in slowly dissociating allosteric enzyme systems].

B I Kuranov·A I Dorozhko·Z S Kagan·V A Iakovlev

Abstract

The feautres of kinetic behavior of dissociating enzyme systems for which the rate of equilibrium between the oligomeric forms is slow in comparison with the rate of the enzymatic process are discussed. It is shown that in slowly dissociating enzyme system of the type Np in equilibrium P (P is the enzyme oligomer, and p is the subunit: N greater than or equal to2) in which P and p forms differ by the character of allosteric interaction between the active and allosteric sites the plots of the initial reaction rate (v) versus substrate (S) or effector (F) concentration may be a very complicated shape. In similar systems the v versus [S]0 plots may have intermediate plateau, maximum and minimum simultaneously, sigmoidality followed by intermediate plateau and so on, and the v versus [F]0 plots may have intermediate plateau.

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Allosteric Regulation Allosteric Site Binding Sites Enzymes Kinetics Macromolecular Substances Mathematics English Abstract Journal Article

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B I Kuranov, A I Dorozhko, Z S Kagan, V A Iakovlev. [Deviations from hyperbolic kinetics in slowly dissociating allosteric enzyme systems].. https://pubmed.ncbi.nlm.nih.gov/1203389/

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