Lectures 1-5 Flashcards
(211 cards)
Definition of bioenergetics
The study of the transformation of energy in living organisms
What is metabolism? (Definition)
The sum of all chemical reactions in the body
What are the two types of metabolic reaction?
Catabolic and anabolic
What is a catabolic reaction?
The breakdown/degradation of molecules
When molecules are broken down (e.g., carbs/fat and protein) they release energy
What is an anabolic reaction?
Synthesis of new molecules
The energy released from anabolic reactions can be used to build new molecules
Examples of catabolic pathways
Proteolysis
Lipolysis
Glycolysis
Glycogenolysis
Anything ending in lysis
Examples of anabolic pathways
Protein synthesis
Lipogenesis
Gluconeogenesis
Glycogenesis
Anything really ending in genesis/sis
How are catabolic and anabolic pathways regulated?
Substrate supply - food and other compounds
Hormonal control - switch on or turn off pathways and alter enzyme activity
Allosteric control - speed or slow enzyme activity
What is our body fueled by?
Adenosine Triphosphate (ATP)
What is ATP?
The energy currency of the cell
ATP is what we use to fuel all our metabolic reactions
What is the link between food and ATP?
The food we consume is digested and used to generate ATP
Look at structure of ATP
Lecture 1, slide 19
How do we generate ATP?
Look at on recap lecture 1, slide 21
Look at enzyme substrate thing
Recap, lecture 1, slide 22
When an enzyme is attached to the substrate what does it form?
It forms a complex
What does the enzyme catalyse the formation of after the enzyme has attached to the substrate and formed a complex?
The formation of a product
Interaction and specificity with enzymes can be explained in two ways, what are they?
Lock and key
Induced fit
What is lock and key (enzyme interaction and specificity)
The binding site has a complementary shape to the substrate
What is induced fit (enzyme interaction and specificity)
Contact between part of the binding site and the substrate induces a change in the shape of the active site to bind to the substrate
Look at examples of lock and key and induced fit
Lecture 1, slide 24
What is allosteric control? (Listen on recap)
Refers to a type of enzyme regulation involving the binding of a non-substrate molecule, known as the allosteric effector, at locations on the enzyme other than the active site
What is allosteric inhibition? (Listen on recap) (lecture 1, slide 27)
Where the allosteric effector binds to the allosteric site, causing the enzymes active site to alter, meaning that the enzyme cannot bind to the substrate
What is allosteric activation? (Listen on recap) (lecture 1, slide 27)
Where the allosteric effector binds to the allosteric site, causing the enzymes active site to change so that the enzyme is able to bind to the substrate
What is a good example of one of the most important allosteric regulatory effects?
When we go from a stand still to a sprint within milliseconds, (we require a huge amount of energy in a short period of time)
The active site enzymes are not quick enough to provide the energy, so the allosteric enzymes take charge