Cellular respiration, metabolism and enzymes Flashcards
Metabolism:
→ sum of all chemical reactions within a cell
Catabolism:
→ releases energy to breakdown complex molecules
Anabolism:
→ consumes energy to synthesis of complex molecules
Change in free energy (ΔG):
→ difference between free energy of final and initial states
Differences between anabolic reactions and catabolic reactions:
Adenosine triphosphate=
Adenine nitrogenous base + ribose sugars + 3 phosphate groups
Hydrolysis of ATP:
How does ATP function in powering cellular work? (3)
➔ By coupling exergonic with endergonic reactions
Chemical work: Hydrolysis of ATP into ADP is an exergonic reaction as it releases energy. This energy is then used to push endergonic reactions to make complex molecules.
Transport work: Hydrolysis of ATP releases energy which helps pump potassium out of cells and sodium into our cells. Active transport of cells across a membrane.
Mechanical work: Hydrolysis of ATP can allow for energy to be used to contract muscles and do work.
ATP is a renewable resource that can be regenerated by __ ____ to ADP.
+ phosphate
What are enzymes?
→ biological catalyst that speeds up a reaction without being consumed by the reaction.
What are the characteristics of enzymes? (4)
- Enzymes are reaction-specific
- Lock and key complex
- Since enzymes are proteins, can change shape.
- When an enzyme changes shape to better grasp substrate → induced fit
What is activation energy?
The minimum energy required to start reaction/energy required to contort/bend the reactant molecule so that
bonds can break.
How do Enzymes lower Activation energy?
- Enzyme has an active site to which substrate binds → Enzyme-substrate complex
- Active site reshapes to better grasp substrate known as
→ induced fit. Substrates are held together via weak interactions = hydrogen or ionic bonds - Active site can lower Activation energy and speed up
reaction
- Acting as a template for substrate orientation, bringing
substrates together in a way that the new bond is going
to form.
- Stresses the substrate and stabilises the transition state
to speed up the production of products.
- Provides a favourable microenvironment
- Participates directly in the catabolic reaction
BUT: enzyme must return to its original shape in order to
catalyse reaction again, - Substrates are converted to products
- Products are released leaving the active site exposed to more substrates to bind to, further increasing speed of reaction.
Optimal conditions: (2)
- Optimal temperature
- Optimal pH
Cofactor →
→ non-protein helper required to activate enzyme
- Inorganic (___, ___, ___,___)
- Organic = ____ (_____).
- Inorganic (Z, Fe, Cu ions)
- Organic = coenzyme (vitamins)
What is an enzyme inhibitor?
→ selectively inhibits the action of specific enzyme
What are the effects of an enzyme inhibitor? (2)
- Permanent
- Reversible
What is competitive inhibition? (2)
→ competitive inhibitor binds to the active site and takes place of the substrate so that substrate-enzyme binding cannot take place
→ competes with the substrate for the active site
What is non-competitive inhibition?
→ non-competitive inhibitor binds away from the active site, but in binding, causes the active site to change shape, not allowing for substrate-enzyme binding
What is allosteric regulation? (4)
- Type of non-competitive inhibition – binding away
from the active site.
‘Allo’ = different ‘Steric’ = form
- Protein function at one site is affected by the binding of a regulatory molecule to a separate site.
- An allosteric enzyme has 4 subunits, each with its own active site.
- A regulatory/allosteric site is also present between the active site subunits.
How does an allosteric enzyme oscillate?
The allosteric enzyme oscillates between active (can bind with substrate) and inactive (changed shape therefore cannot bind with substrate) forms.
What is the function of the inhibitor and activator?
- Activator can bind to the regulatory site and stabilize the allosteric enzyme at the active form.
- Inhibitor can bind to regulatory site and stabilize the allosteric enzyme at the inactive form.
The shape change in one subunit will be_____ to all the other subunits.