ENZYMES

Usually protein, but some are RNA. Work by lowering the activation energy of a reaction

 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

 HOW DO ENZYMES WORK?

- Enzymes work by weakening bonds which lowers activation energy

 ENZYME-SUBSTRATE COMPLEX
- The substance (reactant) an enzyme acts on is the substrate

 ACTIVE SITE
- A restricted region of an enzyme molecule which binds to the substrate.

 INDUCED FIT
- A change in the shape of an enzyme’s active site
- Induced by the substrate
- A change in the configuration of an enzyme’s active site (H+ and ionic bonds are involved).

 WHAT AFFECTS ENZYME ACTIVITY?

 3 FACTORS

1. Environmental Conditions
- Extreme Temperature are the most dangerous
- - high temps may denature (unfold) the enzyme.
- pH (most like 6 - 8 pH near neutral)
- Ionic concentration (salt ions)

2. Cofactors and Coenzymes

- Inorganic substances (zinc, iron) and vitamins (respectively) are sometimes need for proper
enzymatic activity.
- EX: Iron must be present in the quaternary structure - hemoglobin in order for it to pick
up oxygen.

3. Enzyme Inhibitors
- EX: Competitive inhibitors: are chemicals that resemble an enzyme’s normal substrate and compete
with it for the active site.
- EX: 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.

1|Enzymes
 General Characteristic
 Catalyst for biological reactions
 Cause cellular reactions to occur faster
 Most are globular proteins, some are simple proteins
 Are large biomolecules that are responsible for many chemical reactions that are necessary to
sustain life
 A protein molecule and are biological catalysts
 They function with only one reactant to produce specific products
 Have three-dimensional structure and they utilize organic molecules like biotin and inorganic
molecules like metal ions (magnesium ions) for assistance in catalysis

- SUBSTRATE is the reactant in an enzyme catalyzed reaction. The portion of the molecule that is
responsible for catalytic action of enzyme is the active site.
 Enzymes show varying degree of specificities
 Absolute specificity where enzymes react only with one substrate.
 Apoenzyme – The protein part of the enzyme.
 Cofactor – Non protein part of the enzyme.
 The apoenzyme and the cofactor together is called the Holoenzyme
 Cofactors may be of three types: Prosthetic Groups (organic groups that are permanently bound to
enzymes), Activators (are cations – positively charged metal ions), Coenzymes (organic molecules
usually vitamins or made from vitamins, they are not bound permanently to enzymes but they
combine with enzymes)
 Functions
 Major components in signal transduction and cell regulation, kinases, and phosphatases help in this
function.
 Take part in the movement with the help of the protein myosin which aids in muscle contraction.
 Acts as ion pumps in active transport mechanism.
 Present in the virus are for infecting cell.
 Plays an important role in the digestive activity of the enzymes.
 Amylases and proteases are enzyme that breakdown large molecules into absorbable molecules.
 Forming metabolic pathways. Example: Glycolisis
 Factors affecting enzymes (Read further page 72)
 Enzymes Concentration
 Temperature
 Effect of PH
 Other Substances
 Radiation
 Classification
 Oxidoreductases
- Catalyze redox reactions, adds or removes 𝑂2 or 𝐻2
– are the enzymes that catalyze oxidation-reduction reactions Responsible for the production of
heat and energy

 Transferases
- Transfers functional groups
– catalyze reactions where transfer of functional group between two substrates takes place

2|Enzymes
  Hydrolases
- Hydrolyzes certain bonds
– A.K.A hydrolytic enzymes. Catalyze the hydrolysis reactons of carbohydrates, proteins and esters
 Lyases
- Cleaves bonds without hydrolysis
– catalyze the reaction involving the removal of groups from substrates by processes other than
hydrolysis by the formation of double bonds
 Isomerases
- Isomerizes part or all of the substrate
– catalyze the reactions where interconversion of cis-trans isomers is involved
 Ligases
- Covalently bonds two substrates with the use of ATP or any high energy compound
– A.K.A synthases. Catalyze the reactions where coupling of two compounds is involved with the
breaking of pyrophosphate bonds

 Enzyme Substrate Binding

- For an enzyme to work it must have physical contact with its substrate
 Active Site
- A small portion of the enzyme where actual catalysis takes place
 Enzyme-substrate Complex
- The combined enzyme and substrate
 Enzymes speed up cell’s chemical reactions by lowering energy barriers
 The enzyme increases the rate of a reaction without itself being changed
 Without enzymes, most metabolic reactions would occur too slowly to sustain life
 A specific enzyme catalyzes each cellular reaction
 A unique 3-D shape of an enzyme determines which chemical reaction it catalyzes
 A specific reactant that an enzyme acts on is called a substrate of the enzyme
 A substrate fit into a region of the enzyme called an active site
 An active site is typically a pocket or groove on the surface of the enzyme
 When a substrate binds to an enzyme, the active site change shape slightly so that it embraces the
substrate more snugly – induced fit
 The catalytic cycle of the enzyme sucrose which catalyzes the hydrolysis of sucrose
 Many enzymes will not function without nonprotein helpers called cofactors
 Cofactors may be inorganic substance, such as the ions of zinc, iron, or copper
 If the cofactor is an inorganic molecule, it is called a coenzyme
 Most coenzymes are madde from vitamins or are vitamins themselves
 Enzymes inhibitors block enzyme action
 A chemical that interferes with enzyme’s activity is called an inhibitor
 Irreversible inhibition an inhibitor attaches to the enzyme by covalent bonds
 Reversible inhibition an inhibitor attaches to the enzyme by weak bonds

 Two types of inhibitors

 Competitive inhibitor
 Noncompetitive inhibitor

 Factor Affecting Enzyme Activity

1. Enzymes concentration
2. Temperature

3|Enzymes
3. Effect of PH
4. Other substances
5. Radiation

4|Enzymes