ENZYMES

D. F. Palacio

ENZYMES
Biological catalyst Named after the reaction or reactions they catalyze KINDS OF ENZYMES
1. Oxidoreductases: oxidation-reduction reactions. 2. ransferases: group transfer reactions.

3. Hydrolases: hydrolysis reactions. 4. Lyases: addition of groups to a double bond, or removal of groups to create a double bond. 5. Isomerases: isomerization reactions. 6. Ligases: the joining to two molecules.

TERMINOLOGY IN ENZYME CHEMISTRY

Active site: the specific portion of the enzyme to which a substrate binds during reaction. Substrate: the compound or compounds whose reaction an enzyme catalyzes. Cofactor: a nonprotein portion of an enzyme that is necessary for catalytic function; examples are metallic ions such as Zn2+ and Mg2+.

 Apoenzyme: the protein part of an enzyme. Coenzyme: a nonprotein organic molecule, frequently a B vitamin, that acts as a cofactor. Activation: process that increases the action of an enzyme Inhibition: process that makes an enzyme inactive

 Competitive inhibition: binds to the active site of the enzyme surface preventing the binding of substrate Non-competitive inhibitors: binds to other portion of the enzyme surface

FACTORS THAT AFFECT ENZYME ACTIVITY

Enzyme concentration Substrate concentration Temperature pH

Enzyme Concentration
The effect of enzyme concentration on the rate of an enzyme-catalyzed reaction. Substrate concentration, temperature, and pH are constant.

Substrate Concentration
The effect of substrate concentration on the rate of an enzyme-catalyzed reaction. Enzyme concentration, temperature, and pH are constant.

Temperature
The effect of temperature on the rate of an enzymecatalyzed reaction. Substrate and enzyme concentrations and pH are constant.

pH
The effect of pH on the rate of an enzymecatalyzed reaction. Substrate and enzyme concentrations and temperature are constant.

MECHANISM OF ENZYME ACTION

Enzyme substrate complex- proper alignment of the substrate in the active site 1. LOCK AND KEY MODEL -active site has a rigid, nonflexible shape -the shape of the active site is analogous to a lock, and the

 Proper substrate is the key that fits into the lock

2. Induced-Fit Model
The active site becomes modified to accommodate the substrate.

ENZYME INHIBITION
1. REVERSIBLE INHIBITION - Enzymes regain activity when the inhibitor dissociates from the enzyme a. COMPETITIVE INHIBITION - The inhibitor fits into the active site the same way the substrate, preventing the substrate from entering

Competitive Inhibition

2. Noncompetitive Inhibition -the inhibitor binds to a site other than the active site. The substrate cannot fit in the active site

Noncompetitive Inhibition

Irreversible Inhibition
-caused by molecules that causes an enzyme to lose its activity Examples: 1. Insecticides and nerve gases 2. Antibiotics

Enzyme kinetics in the presence and absence of inhibitors.

1. ENZYME REGULATION
a. Proenzyme (zymogen): an inactive form of an enzyme

that must have part of its polypeptide chain hydrolyzed and removed before it becomes active.
An example is trypsin, a digestive enzyme. It is synthesized and stored as trypsinogen, which has no enzyme activity. It becomes active only after a six-amino acid fragment is hydrolyzed and removed from the N-terminal end of its chain. Removal of this small fragment changes in not only the primary structure but also the tertiary structure, allowing the molecule to achieve its active form

2. FEEDBACK CONTROL

- an enzyme-regulation process where

the product of a series of enzyme-catalyzed reactions inhibits an earlier reaction in the sequence.
fe edback inhibition E1 E2 E3 A B C D The inhibition may be competitive or noncompetitive.

3.Allosterism
A regulation process that takes place at a site other than the active site but eventually affects the active site. An enzyme regulated by this mechanism is called an allosteric enzyme. Allosteric enzymes often have multiple polypeptide chains. REGULATOR- the substance that binds to the allosteric enzyme

 Types of regulator 1. Positive regulator- speeds the rxn by changing the shape of the active site 2. Negative regulator- slows down rxn by preventing proper binding of a substrate

The Allosteric Effect

The allosteric effect. Binding of the regulator to a site other than the active site changes the shape of the active site.

D. PROTEIN MODIFICATION
Protein modification: the process of affecting enzyme activity by covalently modifying it.
The best known examples of protein modification involve phosphorylation/dephosphorylation. Example: pyruvate kinase (PK) is the active form of the enzyme; it is inactivated by phosphorylation to pyruvate kinase phosphate (PKP)
ATP active PK phos phatase Pi H2 O AD P inactive PKP

k inase

E. ISOENZYME
Isoenzyme: an enzyme that occurs in multiple forms; each catalyzes the same reaction. Example: lactate dehydrogenase (LDH) catalyzes the oxidation of lactate to pyruvate. The enzyme is a tetramer of H and M chains. H4 is present predominately in heart muscle. M4 is present predominantly in the liver and in skeletal muscle. H3M, H2M2, and HM3 also exist. H4 is allosterically inhibited by high levels of pyruvate while M4 is not. H4 in serum correlates with the severity of heart attack.

ENZYMES IN MEDICINE Enzymes useful in medical diagnosis

En zyme Alan ine amin otrans ferase (ALT) Acid phosp hatase Alk alin e phosp hatase (ALP) Amylase Body Flu id Serum D iseas e Diagnosed Hepatitis Prostate cancer Liver or bone dis ease Pan creatic diseas e Heart attack or hep atitis Heart attack Heart attack Heart attack

Serum Serum Serum As partate aminotransferase (AST) Serum, Cereb rosp in al fluid Lactate dehydrogenas e (LD H) Serum Creatin e phosph ok inase (CK) Serum Ph os phohexose isomeras e (PHI) Serum

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