Molecules: Enzymes And Metabolism Flashcards
What is anabolism
Synthesis of complex molecules from simpler molecules
Requires input of energy
What is catabolism?
Breakdown of complex molecules into simpler molecules (e.g. hydrolysis)
Energy is released
Describe the structure of a catalyst
Active site formed by folding of polypeptide chain(s)
Resulting 3D shape forms the active site, where substrate interacts with enzyme
What is collision theory?
- Particles must collide to react
- Must have sufficient energy to break and make new bonds
- Must collide at the correct orientation
What is the induced fit model?
Active site undergoes a slight change in shape to tighter fit the substrate (lock and key)
Enzyme then induces weakening of bonds thus reducing activation energy needed for reaction
Goes back to its original shape after releases products
How does Denaturation destroy enzyme function?
Destroys tertiary/quaternary conformation of protein
Occurs due to: extreme temp, pH, heavy metal
Activation energy and transition state
Activation energy is minimum amount of energy needed to reach transition state in which bonds in substrate are broken
Enzymes help lower activation energy (MODS)
What are the 3 factors affecting enzyme concentration?
Temp
pH
Substrate concentration
Enzyme concentration
What happens when pH is extreme?
Will alter 3D structure of its active site:
Affects charges on amino acid molecule=no more attraction between amino acids—> Denaturation
Intracellular enzyme-catalysed reactions
Metabolic reactions in cell catalysed by enzymes produced by free ribosomes
Glycolysis—>cytoplasm
Krebs cycle—>mitochondria
Extracellular enzyme-catalysed reactions
Outside cell, catalysed by enzymes produced by bound rbibosomes and secreted outside cell by exocytosis
Lipase, protease, amylase in gut
Explain the generation of heat by metabolic reactions
2nd law thermodynamics no energy transformation is 100% efficient
Some energy is always lost in metabolic reaction and used to maintain constant body temp in warm blooded mammals
Competitive vs non-competitive inhibition
Competitive: inhibitor competes w substrate to bind to active site (increase in substrate conc.=reduced inhibitor rate) chemically similar to substrate
Non-competitive: inhibitors bind to allosteric site (away from active site) altering enzyme shape, increase in conc. no effect
Example or competitive & non-competitive inhibition
Statin drugs competitive lower cholesterol levels (inhibit enzyme HMG-CoA that plays role in cholesterol synthesis)
Hexokinase role in glucose metabolism. Glucose-6-phosphate a product of hexokinase activity can bind to allosteric site of hexokinate and regulate glucose metabolism in brain
What is end-product inhibition?
Where end-product of reaction acts as non-competitive inhibitor (e.g. hexokinase)