UNIT3 - AOS 2 - Biochemical pathways & Enzymes Flashcards
What is a biochemical pathway?
A series of linked reactions starting with an initial reactant that is converted in steps to a final product. Each step requires activity of specific enzymes.
Anabolic pathways
- Simple molecules to complex molecules
- Energonic = requires energy
- Photosynthesis
Catabolic Pathways
- Complex molecules to simple molecules
- Exergonic = releases energy
- Cellular respiration
What is metabolism?
The total activity of the reactions of all biochemical pathways in a living organism
= Anabolism + Catabolism
how are enzymes involved in biochemical pathways
they are composed of proteins and their key role is to act as a catalyst of the reactions in the biochemical pathways.
5 key features of enzymes
- REUSABLE (the enzyme doesn’t break up after catalysing the reaction)
- SPECIFIC (most bind to 1 specific substrate)
- REVERSIBLE (anabolic and catabolic - most)
- SPEED UP NOT CREATE (catalyse reactions, not creating them)
- ACTIVE SITE (Substrate binds to - specific to substrate - complementary shape)
Enzyme-catalyst reaction
- Substrate enters active site = enzyme-substrate complex
- Reaction occurs
- Products leave active site of enzyme
Activation energy
Enzymes increase the rate of the biochemical reaction by decreasing activation energy.
Catabolic = Exergonic = release energy
Anabolic = Endogenic = requires energy
How does temperature affect reaction rate
Denature: when an enzyme gets too hot (past optimal temp) it can denature and stop functioning.
How does pH impact reaction rate
As pH increases or decreases from optimum, the rate of reaction and activity would decrease. Each enzyme has a different optimum pH.
How does substrate concentration impact reaction rate
At very start, increases in substrates may increase reaction if there are enzymes with free active sites.
- However once all available enzymes are involved in the reactions and proceeding at a steady rate —> any further increase in the substrate concentration will not increase RR.
How does enzyme concentration impact reaction rate.
Reaction rate will increase (if substrate remains constant)
- If increase in enzymes to a reaction the reaction rate will continue to increase until all substrates are used.
(* increased enzyme concentration = no effect on total amount of product made)
How does irreversible inhibition impact the rate of reaction
= Substance uses covalent bonds to bind to enzymes active site = permanent. (enzyme can no longer bind to a substrate -> active site is blocked)
e.g. poison interfering with enzyme activity.
How does reversible inhibition impact the rate of reaction
= Substance binds to active site but is not permanent (inhibitor can detach itself
COMPETITVE INHIBITOR
Inhibitor with similar shape to enzyme-substrate = bind to AS
= Enzyme=substrate complex cant be formed
NON-COMPETITIVE INHIBITOR
Inhibitor molecule doesn’t bind to AS, but binds to diff part of enzyme = ALLOSTERIC SITE
= Distorts enzymes shape of AS so substrate can no longer bind.