Enzymes

Enzymes
• Enzymes are biocatalysts. Almost every (type)
biological reaction has an enzyme to catalyze it.
• Hydrolases, synthases, transferases, oxidases, reductases,
polymerases, peptidases, ATPases,
• They are long chain proteins.

• Very efficient : convert large number of substrate

molecules into products per unit time; high turn over
number, ‘n’

• They are specific: catalyze only specific reactions.

• E + S P
• Enzyme Substrate Product
 Enzymes decrease Activation Energy
• High efficiency is due to reduction in Activation energy.
• How can an enzyme reduce the activation energy?

• (1) Binding to the substrate can be done such that the

formation of the transition state is favored.

• (2) Orientation and positioning of substrate(s)

• (3) Bonds in the substrate can be ‘activated’ by

functional groups in the catalytic site.

• All these are due to H- bonding, ion-dipole interactions,

salt bridges & structural changes of Enzyme.
Enzymes provide low activation energy paths
Enzymes provide low activation energy paths.
 Enzyme active site
• Enzymes have active sites .
• This provides proper environment for E-S complex
formation & decrease Activation energy.
• The active site of the Enzyme
• 1. brings & holds the E & S within bonding distances-
proximity effect
• 2. holds them in proper orientations : orientation effect
• 3. provides substrate bond activation by inducing strain.
• 4. provides acid-base catalysis in some cases.
• All these are due to H- bonding, ion- ion, ion-dipole,
hydrophobic interactions, salt bridges & surface structural
complementarities - Molecular Recognition.
 Enzyme active site - structural complementarity.

• Active site is the area of an enzyme (E) that binds to

the substrate (S)
• The Structure at the active site has a unique geometric
shape that is designed to fit the molecular shape of the
substrate.
• Each enzyme is substrate specific.
• Thus, the active site structure is complementary to
the geometric shape of a substrate molecule.
Structural complementarity
Structural complementarity
CPA
•Chymotrypsin (Cuts next to Hydrophobic Groups)
•Trypsin (Cuts next to Arg & Lys)
•Elastase (Cuts next to Val & Thr)
 Mechanism of Enzyme Action

• Lock and key model

 Lock and Key Model
An enzyme binds a substrate in a region called the active
site.

The active site structure and substrate structures are

complementatary like the Lock & key.

So only certain substrates can fit the active site.

This model explains the specificity of enzymes.

But some enzymes are not very specific in their action.

Also enzyme structure is not rigid, flexible.
 Induced Fit Model
• Enzyme structure is flexible, not rigid.

• Enzyme and active site adjust shape to bind

substrate.
• This Increases range of substrate specificity.

• Shape changes also improve catalysis during

reaction.
Lock & key and Induced Fit Models
 Metalloproteins and Metalloenzymes

• Metalloenzymes contain a metal ion as

active site.

• conjugated proteins = protein +

prosthetic (cofactor)

• Holo-enzyme = apo-enzyme +
prosthetic (cofactor)
 Bioinorganic Chemistry of Iron

• Oxygen Carriers: hemoglobin, myoglobin,

hemerythrin
• Redox proteins: iron sulfur protein,
cytochrome c, cytochrome b5, etc.
• Redox enzymes: cytochrome p450,
peroxidase, catalase,etc.
 Bioinorganic Chemistry of Zinc
• Hydrolysis Enzymes - Lewis Acid
carbonic anhydrase
carboxypeptidase
alkaline phosphatase
proteinase
• NAD-dependent dehydrogenases
alcohol dehydrogenase
glutamate dehydrogenase
lactate dehydrogenase
malate dehydrogenase
* Structure Roles
 Bioinorganic Chemistry of Copper

• Oxygen Carriers
Hemocyanin
• Redox Proteins - Electron Transfer Protein
Plastocyanin
Azurin
Stellacyanin
• Oxido - Reductase …see next slide
• Oxido-Reductase Enzymes

• Superoxide Dismutase, SOD

• Tyrosinase
• Ascorbate Oxidase
• Galactose Oxidase 半
• Dopamine-B-Hydroxylase 多
• Amine Oxidase 胺
• Urate Oxidase 尿
• Cytochrome c Oxidase
 Metalloenzymes

• Metalloenzymes contain a metal ion as active site.

• They have two structural components:
• - the protein part called apoenzyme
• - a non – protein part called prosthetic (cofactor).
• Enzymes with both protein & non protein part are
Holoenzymes.
• Holoenzymes = apoenzyme + prosthetic
• Apoenzyme & prosthetic group work jointly.
• The selectivity & catalytic efficiency largely depend on
protein structure.