Module 4 lesson 1 Flashcards
The first to discover an enzyme, diastase.
Anselme Payen
Explain what are enzymes?
Proteins are biological catalysts essential for chemical reactions in living organisms. Made primarily of amino acids, some also contain non-protein prosthetic groups. Extracted enzymes can function independently, with their catalytic activity and specificity stemming from their unique tertiary structure.
The reactant upon which enzymes act on is referred to as the.
substrate
is the major backbones of all enzymes.
Protein
are essential for the stability and activity of the enzyme.
Co-factors and co-enzymes
Compare and contrast the Co-factors and Co-enzymes
Co-factors and co-enzymes both assist enzymes in facilitating biochemical reactions, but they differ in structure and function. Co-factors are non-protein chemical compounds or metallic ions that bind to an enzyme, often permanently, to stabilize its active site or participate directly in the reaction. Examples include metal ions like magnesium or zinc. On the other hand, co-enzymes are organic molecules, often derived from vitamins, that temporarily bind to the enzyme to transfer specific chemical groups during the reaction. Unlike co-factors, co-enzymes are not permanently attached and can be reused in multiple reactions. While both are essential for enzymatic activity, co-factors provide structural support or direct chemical contributions, whereas co-enzymes act as transient carriers of molecules or electrons.
What are the Properties of Enzyme?
They are specific. They will react only with one given type of substrate.
Enzymes are affected by extreme temperatures and pH.
Each enzyme has an optimum pH and temperature at which it works best.
Enzymes are not affected by the chemical reaction that takes place.
Enzymes are affected by poisons, such as toxins and heavy metals, and by a high concentration of salts.
What are the Key Roles of Enzymes?
food and beverages,
cleaning supplies,
clothing,
paper products,
transportation fuels,
pharmaceuticals, and
monitoring devices called biosensors.
The most frequently used enzymes in biotechnology are Blank, which catalyzed the breakdown of molecules.
hydrolases
has been employed to modify substrate specificity and improve enzyme’s stability properties for increasing yields of enzyme-catalyzed reactions.
DNA technology
are used in metabolic engineering of cellular metabolism to increase the yield of fermentation products.
Enzymes
is highly specific and catalyzes only one or a small number of chemical reactions.
enzyme catalyst
Oxidation-Reduction
-Transfer of electrons from one substrate molecule to another (e.g., dehydrogenases, reductases, oxidases).
Oxidoreductases
Group Transfer
-Transfer of functional group from one substrate molecule to another (e.g., glycosyl transferases, acetyl transferases, and aminotransferases).
Transferases
Hydrolysis
- Transfer of functional group from substrate to water (e.g., glycoside hydrolases, peptidases, esterases)
Hydrolases
Group Removal / Group Addition
- Elimination of functional group from substrate with the formation of double bonds. Thus, bonds are cleaved using a different principle than hydrolysis (e.g., pectate lyases break glycosidic linkages by beta- elimination).
Lyases
Isomerization
- . Transfer of groups from one position to another in the same molecule (e.g., glucose isomerase).
Isomerases
Joining of two molecules coupled with cleavage of pyrophosphate bond of ATP or equivalent triphosphate.
- Addition of function group to substrate usually coupled with ATP hydrolysis (e.g., glycine– tRNA ligase).
Ligases (Synthetase)
Enzymes such as Blank from Blank is responsible for dextrinization of starch to produce sweetener
amylase, B. licheniformis
