What are Enzymes?

Most enzymes are Proteins (tertiary and quaternary structures) Act as Catalyst to accelerates a reaction Not permanently changed in the process Are specific for what they will catalyze Are Reusable End in ase -Sucrase -Lactase -Maltase

Enzymes work by weakening bonds which lowers activation energy

The active site

Hexokinase, an enzyme (blue), binding its substrate, glucose (yellow).

Typically a pocket or groove on the surface of the protein into which the substrate fits. The specificity of an enzyme fit between the active site and that of the substrate. Enzyme changes shape tighter induced fit, bringing chemical groups in position to catalyze the reaction.

Enzyme Action: Lock and Key Model

Conventionally we say the enzyme (E) acts on the substrate (S) to yield products (P)

E S

Since E is a catalyst it remains unchanged at the end of the reaction

 The lock and key model is proposed by Emil Fischer. According to this model, the union between the substrate and enzyme takes place at the active site in a manner in which a key fits a lock and results in the formation of an enzyme-substrate complex. The enzyme substrate complex is highly unstable and decomposes to produce the end products of the reaction and to regenerate the free enzyme. The enzyme-substrate union results in the release of energy. It is this energy, raises the energy level of the substrate molecule, thus inducing the activated state.

Specificity
Enzymes selectively recognize proper substrates over other molecules Specificity is controlled by structure the unique fit of substrate with enzyme controls the selectivity for substrate and the product yield

What Affects Enzyme Activity?

Three factors: 1. Environmental Conditions 2. Cofactors and Coenzymes 3. Enzyme Inhibitors

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) 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.

Enzyme inhibition
Compounds which convert the enzymes into inactive substances and thus adversely affect the rate of enzymatically catalyzed reactions are called as inhibitors. Such a process is known as enzyme inhibition. There are two types of inhibition competitive and noncompetitive.

Competitive inhibition
This type of competition occurs in the active site. The structure of the inhibitor closely resemble with that of the substrate. It thus combine with the enzyme, forming an enzyme-inhibitor complex. The inhibitor competes with the substrate to combine with the enzyme. Example: An enzyme, succinic dehydrogenase catalyzes the conversion of succinic acid to fumaric acid. Malonic acid act as the inhibitor.

Competitive inhibition
Here no competition occurs between the substrate and the inhibitor. The inhibitor has little or no structural resemblance with the substrate and it binds with the enzyme at a place other than the active site. Example: Various ions of heavy metals act on a variety of enzymes.

3. Enzyme Inhibitors
Two Types: a. Competitive inhibitors: are chemicals that resemble an enzymes normal substrate and compete with it for the active site. 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
Enzyme
Noncompetitive Inhibitor

Substrate

Enzyme

Competitive inhibitor