Topic 7.6 Enzymes Flashcards
7.6.1 State that metabolic pathways consist of chains and cycles of ______-catalysed reactions.
Metabolic pathways consist of chains and cycles of enzyme-catalysed reactions.
7.6.2 Describe the induced-fit model.
- enzymes undergo significant changes in their conformation when substrates combine with their active sites
- Induced-fit model (hand & glove analogy):
- initially, substrate doesn’t fit perfectly into active sit of enzyme
- when substrate binds to active site, the shape of the active site is changed, and the substrate fits perfectly - induced fit
- accounts for ability of some enzymes to bind to several substrates - if shape of active site changes when substrate binds, allows for many different but similar substrates to bind to one enzyme
7.6.3 Explain that enzymes lower the activation energy of the chemical reactions that they catalyse.
- chemical environment provided by active site of enzyme for substrate causes changes within substrate molecule, weakening its bonds
- substrate changed to a transition state (different from transition state when enzyme isn’t involved)
- activation energy lowers & substrate is altered by rearrangement of existing atoms
- transformed substrate (product) is released from active site
- unchanged enzyme is then free to combine with other substrate molecules
7.6.4 Explain the difference between competitive and non-competitive inhibition, with reference to one example of each.
Competitive inhibition
- molecule called competitive inhibitor competes directly for active site of enzyme
- substrate has fewer encounters with active site, thus chemical reaction rate ↓
- competitive inhibitor must have similar structure to substrate to function this way
- e.g. use of sulfanilamide to kill bacteria during an infection
- folic acid is essential as coenzyme to bacteria → produced in bacterial cells by enzyme action of PABA
- sulfanilamide competes with PABA and blocks enzyme
- human cells don’t use PABA to produce folic acid ∴ unaffected by drug
Non-competitive Inhibition
- AKA allosteric inhibition
- involves inhibitor that doesn’t compete for enzyme’s active site
- inhibitor binds to allosteric site (different from active site)
- binding at allosteric site causes change in shape of enzymes active site, making it non-functional
- e.g. metallic ions (mercury) binding to sulfur groups of component amino acids of many enzymes → results in protein shape changes which causes inhibition of enzyme
Note: may be reversible or irreversible; also examples of allosteric interaction activating an enzyme rather than inhibiting it.
7.6.5 Explain the control of metabolic pathways by end-product inhibition, including the role of allosteric sites.
- End-product inhibition prevents cell from wasting chemical resources & energy by making more of a substance than needed.
- metabolic pathways consist of chains/cycles to produce an end-product; each step catalyzed by a specific enzyme.
- when ↑ concentration of end-product, end-product binds with allosteric site of 1st enzyme → brings inhibition
- prevents build-up of intermediates in cell
- form of negative feedback
- prevents build-up of intermediates in cell
- when ↓ concentration/existing end-product is used up by cell, fewer bindings with allosteric site of 1st enzyme → reactivates enzyme
- enzyme that is inhibited is called an allosteric enzyme