Kinetics Of Allosteric Enzymes

The MWC model postulates that all subunits in an enzyme oligomer change conformation in a concerted fashion, while the KNF model assumes this change may be sequential for the different subunits. Most K-type enzymes have positive cooperativity; a limited number of regulatory enzymes have negative cooperativity. This controlled change in affinity makes the enzyme more sensitive to changes in substrate concentration (positive cooperativity), or dampens the enzyme’s response to changes in substrate concentration (negative cooperativity). When multiple enzymes work in concert for some cellular process, and are regulated in concert by the same original effector, this may produce very high ultrasensitivity.


Substrate Concentration Purine Nucleoside Phosphorylase Positive Cooperativity Hyperbolic Curve Negative Cooperativity 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.


Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

Copyright information

© Springer Science+Business Media, LLC 2008

Personalised recommendations