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Substrate Transition State Product: Adapted From Nelson & Cox (2000) Lehninger Principles of Biochemistry (3e) p.252

Enzymes catalyze reactions by stabilizing the transition state. The enzyme's active site provides a catalytic surface that complements and stabilizes the transition state, lowering the energy required to reach it. This allows the transition state to be transformed into products more easily. The active site is deeper than an antibody binding site and shields the reaction from water molecules, sustaining the formation of stable ion pairs and intermediates needed for catalysis.

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92 views6 pages

Substrate Transition State Product: Adapted From Nelson & Cox (2000) Lehninger Principles of Biochemistry (3e) p.252

Enzymes catalyze reactions by stabilizing the transition state. The enzyme's active site provides a catalytic surface that complements and stabilizes the transition state, lowering the energy required to reach it. This allows the transition state to be transformed into products more easily. The active site is deeper than an antibody binding site and shields the reaction from water molecules, sustaining the formation of stable ion pairs and intermediates needed for catalysis.

Uploaded by

Anisam Abhi
Copyright
© Attribution Non-Commercial (BY-NC)
We take content rights seriously. If you suspect this is your content, claim it here.
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Download as PPT, PDF, TXT or read online on Scribd
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Stickase

Substrate

Transition state Product

X
If enzyme just binds substrate
then there will be no further reaction

Enzyme not only recognizes substrate,


but also induces the formation of transition state
Adapted from Nelson & Cox (2000) Lehninger Principles of Biochemistry (3e) p.252
The Nature of Enzyme Catalysis

● Enzyme provides a catalytic surface


● This surface stabilizes transition state
● Transformed transition state to product

B
A

A B Catalytic surface
Juang RH (2004) BCbasics
Enzyme Stabilizes Transition State
Energy change
ST
Energy required (no catalysis)

Energy decreases (under catalysis)


EST
S

ES
EP P

Reaction direction
T = Transition state What’s the difference?
Adapted from Alberts et al (2002) Molecular Biology of the Cell (4e) p.166
Active Site Is a Deep Buried Pocket

hy energy required to reach transition st


lower in the active site?
It is a magic pocket
+ (1) Stabilizes transitio
(2) Expels water
CoE (1) (2)
(3) Reactive groups
(4) - (4) Coenzyme helps
(3)
Juang RH (2004) BCbasics
Enzyme Active Site Is Deeper than Ab Binding

Instead, active site on enzyme


also recognizes substrate, but
g binding site on Ab binds to Ag
actually complementally fits the
mplementally, no further reaction
transition state and stabilized it.
curs.

Adapted from Nelson & Cox (2000) Lehninger Principles of Biochemistry (3e) p.252
Active Site Avoids the Influence of Water

+
-

ng the influence of water sustains the formation of stable ion


Adapted from Alberts et al (2002) Molecular Biology of the Cell (4e) p.115

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