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Nomenclature and classification of enzymes, mechanism of enzyme action , factor affecting rate of enzyme catalyzed reaction?
Anonymous
Jan 3
#factors-affecting-rate-of-enzyme-catalyzed-reaction
#mechanism-of-enzyme-action
#nomenclature
#classification-of-enzymes
Nomenclature and classification of enzymes, mechanism of enzyme action , factor affecting rate of enzyme catalyzed reaction?
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Jan 3
Nomenclature and Classification of Enzymes:
Enzymes are typically named by adding the suffix "-ase" to the name of the substrate they act upon. For example, the enzyme that breaks down lactose is called lactase. However, there are exceptions to this naming convention.
Enzymes are classified into six main classes based on the type of reaction they catalyze:
1. Oxidoreductases: These enzymes catalyze oxidation-reduction reactions, transferring electrons from one molecule to another.
2. Transferases: Transferases catalyze the transfer of functional groups, such as amino groups or phosphate groups, from one molecule to another.
3. Hydrolases: Hydrolases catalyze hydrolysis reactions, breaking chemical bonds by adding water.
4. Lyases: Lyases catalyze the addition or removal of groups to form double bonds or the reverse, without hydrolysis or oxidation.
5. Isomerases: Isomerases catalyze the rearrangement of atoms within a molecule, resulting in the formation of isomers.
6. Ligases: Ligases catalyze the joining of two molecules, often using energy from ATP.
Mechanism of Enzyme Action:
Enzymes facilitate chemical reactions by lowering the activation energy required for the reaction to occur. They do this by binding to the substrate and forming an enzyme-substrate complex. The enzyme then catalyzes the conversion of the substrate into the product(s) of the reaction.
The mechanism of enzyme action typically involves the following steps:
1. Substrate Binding: The substrate(s) bind to the active site of the enzyme, forming an enzyme-substrate complex.
2. Catalysis: The enzyme facilitates the conversion of the substrate into the product(s) of the reaction. This can involve various mechanisms, such as acid-base catalysis, covalent catalysis, or metal ion catalysis.
3. Product Release: The product(s) of the reaction are released from the active site of the enzyme, allowing the enzyme to bind to another substrate molecule and repeat the process.
Factors Affecting Rate of Enzyme-Catalyzed Reaction:
Several factors can influence the rate of an enzyme-catalyzed reaction:
1. Substrate Concentration: Increasing the concentration of the substrate generally increases the rate of the reaction until the enzyme becomes saturated with substrate.
2. Enzyme Concentration: Increasing the concentration of the enzyme typically increases the rate of the reaction until the substrate becomes limiting.
3. Temperature: Enzymes have an optimal temperature at which they function most efficiently. Increasing the temperature can initially increase the rate of the reaction, but excessively high temperatures can denature the enzyme and decrease its activity.
4. pH: Enzymes also have an optimal pH at which they function best. Deviations from this pH can affect the enzyme's structure and activity.
5. Inhibitors: Inhibitors can bind to the enzyme and decrease its activity. Competitive inhibitors compete with the substrate for binding to the active site, while non-competitive inhibitors bind to a different site on the enzyme, altering its shape and reducing its activity.
6. Activators: Activators can bind to the enzyme and increase its activity. They can either bind to the active site or a separate regulatory site on the enzyme.
These factors can either enhance or inhibit the rate of enzyme-catalyzed reactions, ultimately affecting the efficiency of biochemical processes in living organisms.
Enzymes are typically named by adding the suffix "-ase" to the name of the substrate they act upon. For example, the enzyme that breaks down lactose is called lactase. However, there are exceptions to this naming convention.
Enzymes are classified into six main classes based on the type of reaction they catalyze:
1. Oxidoreductases: These enzymes catalyze oxidation-reduction reactions, transferring electrons from one molecule to another.
2. Transferases: Transferases catalyze the transfer of functional groups, such as amino groups or phosphate groups, from one molecule to another.
3. Hydrolases: Hydrolases catalyze hydrolysis reactions, breaking chemical bonds by adding water.
4. Lyases: Lyases catalyze the addition or removal of groups to form double bonds or the reverse, without hydrolysis or oxidation.
5. Isomerases: Isomerases catalyze the rearrangement of atoms within a molecule, resulting in the formation of isomers.
6. Ligases: Ligases catalyze the joining of two molecules, often using energy from ATP.
Mechanism of Enzyme Action:
Enzymes facilitate chemical reactions by lowering the activation energy required for the reaction to occur. They do this by binding to the substrate and forming an enzyme-substrate complex. The enzyme then catalyzes the conversion of the substrate into the product(s) of the reaction.
The mechanism of enzyme action typically involves the following steps:
1. Substrate Binding: The substrate(s) bind to the active site of the enzyme, forming an enzyme-substrate complex.
2. Catalysis: The enzyme facilitates the conversion of the substrate into the product(s) of the reaction. This can involve various mechanisms, such as acid-base catalysis, covalent catalysis, or metal ion catalysis.
3. Product Release: The product(s) of the reaction are released from the active site of the enzyme, allowing the enzyme to bind to another substrate molecule and repeat the process.
Factors Affecting Rate of Enzyme-Catalyzed Reaction:
Several factors can influence the rate of an enzyme-catalyzed reaction:
1. Substrate Concentration: Increasing the concentration of the substrate generally increases the rate of the reaction until the enzyme becomes saturated with substrate.
2. Enzyme Concentration: Increasing the concentration of the enzyme typically increases the rate of the reaction until the substrate becomes limiting.
3. Temperature: Enzymes have an optimal temperature at which they function most efficiently. Increasing the temperature can initially increase the rate of the reaction, but excessively high temperatures can denature the enzyme and decrease its activity.
4. pH: Enzymes also have an optimal pH at which they function best. Deviations from this pH can affect the enzyme's structure and activity.
5. Inhibitors: Inhibitors can bind to the enzyme and decrease its activity. Competitive inhibitors compete with the substrate for binding to the active site, while non-competitive inhibitors bind to a different site on the enzyme, altering its shape and reducing its activity.
6. Activators: Activators can bind to the enzyme and increase its activity. They can either bind to the active site or a separate regulatory site on the enzyme.
These factors can either enhance or inhibit the rate of enzyme-catalyzed reactions, ultimately affecting the efficiency of biochemical processes in living organisms.
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