Enzymes

Introduction
The authors of enzyme :
Beadle

(1948) Fairley and Kilgour (1966) Devlin (1970)

What Are Enzymes?

Most

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

Cont...
Are

specific for what they will catalyze Are Reusable End in ase -Sucrase -Lactase -Maltase

Enzymes

Cofactors Coenzymes Holoenzyme Apoenzyme

Classification of Enzyme
Oxidoreductases Transferases Hydrolases Lyases Isomerases Ligases

ENZYME FUNCTION
LOWERING ACTIVATION ENERGY

THE FUNCTION OF CATAYST

ENZYME IS A BIOCATALYST

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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Enzymes speed up metabolic reactions by lowering energy barriers

Enzyme speed reactions by lowering EA. The transition state can be reached at moderate temperatures. Enzymes do not change delta G. It speed-up reactions that would occur eventually. Because enzymes are so selective,they determine which chemical processes will occur at any time

Factor Affecting Enzyme Activity

Enzyme

Concentration Substrate Concentration Temperature PH Ion (Cation and Anion) Accumulation of End Product

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. 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. site

Substrate

Competitive inhibitor

Enzyme

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

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Biological function of enzymes

In

digestive system in animals Enzymes such as amylases and proteases break down large molecules (starch or proteins, respectively) into smaller ones, so they can be absorbed by the intestines. In ruminants which have herbivorous diets, microorganisms in the gut produce another enzyme, cellulase to break down the cellulose cell walls of plant fiber.

Cont..
They

are indispensable for signal transduction and cell regulation, often via kinases and phosphatases. They also generate movement, with myosin hydrolysing ATP to generate muscle contraction and also moving cargo around the cell as part of the cytoskeleton

Industrial application of enzymes

Food processing Amylases catalyze the release of simple sugars from starch

Cont
Dairy

industry Lipase : Is implemented during the production of Roquefort cheese to enhance the ripening of the blue-mould cheese.

Cont
Paper

industry Amylases, Xylanases, Cellulases and ligninases Degrade starch to lower viscosity, aiding sizing and coating paper. Xylanases reduce bleach required for decolorising; cellulases smooth fibers, enhance water drainage, and promote ink removal; lipases reduce pitch and lignindegrading enzymes remove lignin to soften paper.

Cont

Molecular biology Restriction enzymes, DNA ligase and polymerases Used to manipulate DNA in genetic engineering, important in pharmacology, agriculture and medicine. Essential for restriction digestion and the polymerase chain reaction. Molecular biology is also important in forensic science.

Thank You