8.1 Enzymes HL Flashcards
metabolic chain reaction pathways vs. cyclical reaction pathways [CONTRAST]
- most metabolic pathways involve a chain of reactions
- some metabolic pathways form a cycle instead and in this type of pathway, end product of one reaction is the reactant that starts the rest of the pathway
activation energy
- energy necessary for reaciton to occur as it is used to weaken/break bonds in substrate
how enzymes lower activation energy
- the binding of substrate to active site of enzyme lowers the overall energy level of transition state & reduces the activation energy
enzyme inhibitor
- chemical substances that bind to enzymes & reduce the activity of enzyme
competitive vs. non-competitive enzyme inhibition [CONTRAST]
- competitive inhibitors: interfere w/ active site -> substrate can’t bind to active site
- non-competitive inhibitors: bind at a location other than active site (allosteric sites) -> substrate can’t bind to active site / reaction is slowed
example of competitive enzyme inhibitor
- sulfadiazine: blocks para-aminobenzoate from binding to dihydropteroate synthetase
example of non-competitive inhibitor
- xylitol-5-phosphate: blocks fructose-6-phosphate from binding to phosphofructokinase
allosteric regulation of enzyme activity
- regulation of enzyme by binding effector molecule at a site other than active site
mechanism of end-product inhibition
enzyme that is regulated catalyzes one of the first reactions in metabolic pathway & substance that binds to allosteric site is the end product of the pathway
- end product acts as inhibitor
benefit of end-product inhibition
- economical way to control metabolic pathways:
- allows concentration of the end product to be controlled
- increase in concentration of product causes reaction to eventually slow down and stop because reactions often reach equilibrium position instead of going to completion -> this reverberates back through metabolic pathway when end product accumulates w/ all intermediates accumulating
- end-product inhibition prevents this build-up of intermediate products
end-product inhibition of metabolic pathway that converts threonine to isoleucine
- through a series of 5 reactions, amino acid threonine is converted to isoleucine
- as concentration of isoleucine builds up, it binds to allosteric site of first enzyme in the chain, threonine deaminase <- isoleucine acts as non-competitive inhibitor
consequence of increase in isoleucine concentration
conc of isoleucine increases -> isoleucine binds to allosteric site of first enzyme in chain, threonine deaminase (isoleucine acts as non-competitive inhibitor)
reasons for development of new anti-malarial drugs
- increasing resistance of Plasmodium falciparum (pathogen that causes malaria) to anti-malarial drugs such as chloroquine
- dependence of all new drug combinations on narrow range of medicines
- increasing global efforts to eradicate malaria
use of databases in identification of potential new anti-malarial drugs
Plasmodium falciparum strain 3D7: variety of the malarial parasite for which the genome has been sequenced
why the rate of reaction with increasing substrate concentration is lower with a non-competitive inhibitor compared to a competitive inhibitor
- competitive inhibitor: concentration of substrate begins to exceed the amount of inhibitor -> maximum rate of uninhibited enzyme can be achieved BUT takes much higher concentration of substrate to achieve this maximum rate
- non-competitive inhibitor: enzyme doesn’t react the same maximum rate bc binding of non-competitive inhibitor prevents some enzymes from being able to react regardless of substrate concentration -> enzymes that don’t bind to inhibitors follow same pattern as normal enzyme -> takes approximately same conc of enzyme to reach maximum rate, but max rate is lower than uninhibited enzyme