Enzymes

Activation energy of uncatalyzed reaction

Activation energy of catalyzed reaction

gibbs free energy

Secondary Structure

Primary Structure

Tertiary Structure

Quaternary Structure

Active-site cleft

Substrate entering active site of enzyme

Induced Fit theory

Enzyme/Substrate complex

Enzyme/Products complex

Products leaving active site of enzyme

Temperature Graph

pH Graph

Normal Reaction

Competitive Inhibitor

NonCompetitive Inhibitor

Normal enzyme

Competitive inhibitor

Non competitive inhibitor

Allosteric Inhibition

Allosteric Activation

Enzyme

biological catalysts that greatly increase the rates of biochemical reaction most of which are protein.

Enzymes are usually named after

their substrates by adding the suffix “-ase”

Catalyst

a substance that speeds up a chemical reaction without being a reactant

reaction activation energy

the amount of energy that must be put in for the reaction to begin

Amino Acid

20 different side chains with a large variety of groups that have different chemical and physical properties, including hydrophilic, or hydrophobic groups, charged or neutral polar groups, and acidic or basic groups

Proteins

are composed of long chains of amino acids linked by amide bonds, known as peptide bonds

Protein structure

1. primary structure

2. secondary structure

3. tertiary structure

4. quaternary structure

primary structure

refers to the sequence of amino acid residues

secondary structure

refers to regular, local structural units, usually held together by hydrogen bonds

tertiary structure

the final three-dimensional structure of the polypeptide - results from the packing together of the secondary structure units and the exclusion of solvent

quaternary structure

the association of two or more separate three-dimensional polypeptides

The factors that can affect or control enzyme activity

1. Temperature

2. pH

3. Regulatory molecules

4. Cofactors

5. Compartmentalization

6. Feedback inhibition

How temperature effects enzymes

a higher temperature generally makes for higher rates of reaction to a certain degree. once it hits 40C the protein begins to denature

How does pH affect the enzyme

The active site amino acid residues often have acidic or basic, meaning changes in pH can affect these residues and make it hard for the substrate to bind

Regulatory molecule

where other molecules either increase (activator) or decrease (inhibitor) the enzymes activity

Types of reversible inhibitor

1. Competitive

2. Non Competitive

Competitive

binds to an enzyme to block binding of the substrate and will decrease reaction rate when theres not much substrate but can be out competed by lots of substrates.The enzyme can still reach its maximum reaction rate given enough substrate.

Non Competitive

doesnt block the substrate from binding to the active site. enzyme-catalyzed reaction will never reach its normal maximum rate even with lots of substrate.

Allosteric regulation

the regulatory molecule binds to an enzyme someplace other than the active site

Allosteric site

the place where the regulator binds

Cofactor

inorganic ions that are attached temporarily to the enzyme

Coenzymes

Organic molecule example vitamins

Compartmentalization

that enzyme needed for specific processes can be kept in the places where they act, ensuring they can find their substrates readily, don’t damage the cell, and have the right microenvironment to work well

Feedback inhibition

the end product of a metabolic pathway acts on the key enzyme regulation entry to that pathway, keeping more of the end product from being produced