Induced fit model of Enzyme-Substrate interaction


 

Answer to Question E-05

 

b) Induced fit

 

 

The Induced fit model describes the formation of the E-S as a result of the interaction between the  substrate and a flexible active site.  The substrate produces changes in the conformation on the enzyme, aligning properly the groups in the enzyme. It allows  better binding and catalytic effects. 

 

 

 

 

This model opposes to the former Lock and Key model (c) , that explained the formation of the E-S complex as a result of the binding of complementary geometrical rigid structures, as a lock and a key.

 

Follow this link to find a very good animation that represents these two models:

 

http://www.wiley.com/legacy/college/boyer/0470003790/animations/enzyme_binding/enzyme_binding.htm

 

 

The Concerted model (a) and the Sequential model (e) are models used to explain the allosteric changes of conformation of an enzyme from the T structure to the R structure and viceversa. In the concerted model all the subunits that form the allosteric protein change conformation at once, while in the sequential model the change in conformation of one subunit favors the change in conformation of the other subunits and so on.

 

The Michaellis Menten model (d) is related to the kinetics of enzyme catalyzed reactions, and describes the relationship between the concentration of substrate and enzyme velocity in a reaction where no allosteric effects exist.

 

More information about:

 

Michaelis Menten model:

http://themedicalbiochemistrypage.org/enzyme-kinetics.html#michaelis

 

http://en.wikipedia.org/wiki/Michaelis-Menten_kinetics

 

Induced fit model:

http://themedicalbiochemistrypage.org/enzyme-kinetics.html#interactions

 

Concerted Model and Sequential Model:

http://www.aw-bc.com/mathews/ch07/c07hsob.htm

 

http://en.wikipedia.org/wiki/Allosteric_regulation

 

http://www-ssrl.slac.stanford.edu/research/highlights_archive/allosteric_transition.html

 

 

 

 

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