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Enzymes

What Are Enzymes?


Most enzymes are

Proteins (tertiary and quaternary structures) Act as Catalyst to accelerate a reaction Not permanently changed in the process

Enzymes
Are specific

for what they will catalyze Are Reusable End in ase

-Sucrase -Lactase -Maltase

Biological Role of Enzymes


Cheese Making Fruit Juice Making Desizing Fabrics

Destaining fabrics
Dehairing hides Recovering silver from photographic films Wound healing Augmentingsurgery Disolving Blood clot ClinicaL Chemistry Bioremediation Bioprocessing
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Biofermentor

Production f Chemicals

How do enzymes Work?


Enzymes work by weakening bonds which lowers activation energy

Enzymes
Without Enzyme With Enzyme

Free Energy

Free energy of activation Reactants

Products

Progress of the reaction


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Enzyme-Substrate Complex The substance (reactant) an enzyme acts on the substrate


Substrate Joins

Enzyme

Active Site
A restricted region of an enzyme

molecule which binds to the substrate . Active


Site Substrate

Enzyme

Mechanisms of Enzyme Action


Lock and Key Model- Emil Fisher Induced Fit Model- Daniel Koshland

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Induced Fit
A change in the

shape of an enzymes active site Induced by the substrate

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Induced Fit
A change in the configuration of an

enzymes active site (H+ and ionic bonds are involved). Induced by the substrate.
Active Site substrate Enzyme induced fit
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What Affects Enzyme Activity?


Three factors:

1. Environmental Conditions 2. Cofactors and Coenzymes


3. Enzyme Inhibitors

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1. Environmental Conditions
1. Extreme Temperature are the most dangerous - high temps may denature (unfold) the enzyme. 2. pH (most like 6 - 8 pH near neutral) 3. Ionic concentration (salt ions)
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2. Cofactors and Coenzymes


Inorganic substances (zinc, iron) and

vitamins (respectively) are sometimes need for proper enzymatic activity.

Example: Iron must be present in the quaternary structure - hemoglobin in order for it to pick up oxygen.

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Two examples of Enzyme Inhibitors


a. Competitive inhibitors: are

chemicals that resemble an enzymes normal substrate and compete with it for the active site.
Substrate

Competitive inhibitor
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Enzyme

Inhibitors
b. Noncompetitive inhibitors: Inhibitors that do not enter the active site, but bind to another part of the enzyme causing the enzyme to change its shape, which in turn alters the active site.
Substrate active site altered
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Enzyme

Noncompetitive Inhibitor

Regulation of Enzymes
Regulation of enzymatic

pathways prevent the deletion of substrate Regulation happens at the level of the enzyme in a pathway Feedback inhibition is when the end product regulates the enzyme early in the pathway

Feedback Regulation
Negative feedback

pathway is inhibited by accumulation of final product Positive feedback a regulatory molecule stimulates the activity of the enzyme, usually between 2 pathways
ADP levels cause the

activation of the glycolysis pathway to make more ATP

Allostery
Conformational coupling of 2 widely

separated binding sites must be responsible for regulation active site recognizes substrate and 2nd site recognizes the regulatory molecule Protein regulated this way undergoes allosteric transition or a conformational change Protein regulated in this manner is an allosteric protein

Allosteric Regulation

Method of regulation is also used in other

proteins besides enzymes


Receptors, structural and motor proteins

Allosteric Regulation

Enzyme is only partially active with sugar only but

much more active with sugar and ADP present

Phosphorylation
Some proteins are regulated by the addition of a

PO4 group that allows for the attraction of + charged side chains causing a conformation change Reversible protein phosphorylations regulate many eukaryotic cell functions turning things on and off Protein kinases add the PO4 and protein phosphatase remove them

Phosphorylation/Dephosphorylation
Kinases capable of

putting the PO4 on 3 different amino acid residues


Have a OH group on R

group
Serine Threonine

Tyrosine

Phosphatases that

remove the PO4 may be specific for 1 or 2 reactions or many be non-specific

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