Description of the Components of Enzyme
What is an enzyme?
Enzymes are protein macromolecules.
o They have a defined amino acid sequence and are typically 100-500 amino acids long.
o They have a defined three-dimensional structure.
Enzymes are catalysts.
o They act as a catalyst to a chemical or biochemical reaction, with a defined mechanism.
o They increase the speed of that reaction, typically by 106-1014 times faster than the rate of the uncatalyzed
reaction.
o They are selective for a single substrate.
o They speed up rate of reaction by lowering the activation energy (Ea).
o They are stereospecific, meaning the reaction produces a single product.
Common mistakes and misconceptions
Enzymes are "specific." Each type of enzyme typically only reacts with one (Fig 8.b.), or a couple, of substrates. Some
enzymes are more specific than others and will only accept one particular substrate. Other enzymes can act on a range of
molecules, as long as they contain the type of bond or chemical group that the enzyme targets.
Fig. 8.b. A substrate entering the active site of the enzyme.
Image modified from "Enzymes: Figure 2," by OpenStax College, Biology, CC BY 3.0.
.
Enzymes are reusable. Enzymes are not reactants and are not used up during the reaction. Once an enzyme binds to a
substrate and catalyzes the reaction, the enzyme is released, unchanged, and can be used for another reaction. This
means that for each reaction, there does not need to be a 1:1 ratio between enzyme and substrate molecules.
Nomenclature
Typically add “-ase” to name of substrate
e.g. lactase breaks down lactose (dissacharide of glucose and galactose)
Enzymes based upon the class of organic chemical reaction catalyzed:
1. Oxidoreductase - catalyze redox reactions; dehydrogenases, oxidases, peroxidases, reductases.
2. Transferases - catalyze group transfer reactions; often require coenzymes.
3. Hydrolases - catalyze hydrolysis reactions.
4. Lyases - lysis of substrate; produce contains double bond.
5. Isomerases - catalyze structural changes; isomerization.
6. Ligases - ligation or joining of two substrates with input of energy, usually from ATP hydrolysis; often called synthetases or
synthases.
ENZYME COMPONENTS
An enzyme as illustrated on Fig. 8.c. has different components which follow:
Apoenzyme- is an inactive enzyme, which activation occurs upon binding of an organic or inorganic cofactor. This
enzyme is a protein that lack its necessary cofactor(s) for proper functioning.
Holoenzymes-are the active forms of apoenzymes, (Apoenzyme plus cofactor). DNA polymerase and RNA polymerase
are examples (see Fig. 8.d.).
Cofactors are mostly metal ions or small organic molecules. They are inorganic and organic chemicals that assist
enzymes during the catalysis of reactions. These are nonprotein component (e.g. magnesium, zinc)
Coenzymes are non-protein organic molecules that are mostly derivatives of vitamins soluble in water by phosphorylation.
Examples are organic cofactor (e.g., NADH, FADH)
Many enzymes can catalyze a reaction only if coenzymes, or cofactors are present.
Fig. 8.c. Parts of an Enzyme
Fig. 8.d. Component of a Holoenzyme
Terminology:
Catalyst
A substance that speeds up a chemical reaction without being changed
Enzyme
A biological catalyst (usually a protein)
Substrate
The reactant molecule that an enzyme works on
Active Site
The part of the enzyme where the substrate binds
Enzyme-substrate complex
formed when the substrate molecule collides with the active site of its enzyme
Endoenzymes(intracellular) / Exoenzymes (extracellular)
Activation energy
the minimum energy required to start a chemical reaction
Transition state
the intermediate stage in a reaction in which the old bonds break and new bonds are formed
