Wikibooks

Structural Biochemistry/Enzyme Catalytic Mechanism/Summary

< Structural Biochemistry | Enzyme Catalytic Mechanism
This page may need to be reviewed for quality.

Enzyme Catalysis: Summary

edit

Enzymes accelerate reactions using  :

Proximity and orientation effects

Electrostatic catalysis

Preferential Transition State Binding

Induced fit

General acid/base catalysis

Covalent catalysis

Metal ion catalysis


Enzymes accelerate chemical reactions by lowering the activation energy, DG‡.

Strong binding of the transition state and weak binding of the substrate leads to the maximum rate because all the binding energy is used to lower DG‡.

Any process that uses some of the binding energy for another purpose, e.g., a protein conformational change, will lower the maximum rate.

Under physiological conditions, the maximum rate is achieved by maximizing kcat/Km AND having Km greater than the physiological [S]. This means that most of the enzyme will be free to interact with a substrate molecule and that every encounter will lead to a reaction.

Reference

edit

http://www.bmb.psu.edu/courses/bmb401_spring2004/lecture_notes/lecture11_2004.pdf

Retrieved from "https://en.wikibooks.org/wiki/Structural_Biochemistry/Enzyme_Catalytic_Mechanism/Summary"