03 Flashcards
What do enzymes do
increase the rate of chemical reaction
rate = # in set amount of time
Describe an enzyme
specific for one reaction (depends on the amino acids that make up the enzyme)
not permanently changed in these reactions
bind the substances that are reacting (substrates) and release the (productcs) once the reaaction is complete
What are the steps to an enzyme catalyzed reaction
- binding of substrate
E+S <-> ES - conversion of the bound substrate into a still bound product
ES <-> EP - release of the product
EP <-> E+P
*reversible reactions
What is the lock and key model
what are the limitations
enzyme and substrate fit together perfectly
this model explains the specificity of an enzyme
- not the ability of the enzyme to stablizie the transition state
What is the induced fit model
most accurate model
allows for flexibility of the enzyme in binding to the substrate
binding of the substrate induces changes in the shape/conformation of the enzyme
changes allow for enzyme catalysis to take place
explains changes in protein structure that occur when a substrate bidns to an enzyme
conromational change can stress the bonds –> allows for a reaciton to take place more easily
How do enzymes catalyze a reaction
lowers the activation energy needed to reach the final state
*doesn’t speed up the reaction progress, just the number of products made
What are the strategies used by enzymes to catalyze a reaction
- acid-base catalysis
- covalent catalysis
- metal-ion catalysis
- catalysis by approximation
- cofactor catalysis
enzymes can also use a combo of these
What are co-factors and co-enzymes
functional groups that help facilitate the enzymatic reaction
come from the enzymes themselves (aa side chains), other non-protein molecules or minerals that are part of the active site
- can donate a function group to the reaction
- stabilize the transition state of the reaction
What are examples of cofactors and coenzymes
zinc
iron
vitamin B6
Thiamine B1
How do cofactors work
incomplete enzyme + mineral cofactor join together to form an active enzyme
How do coenzymes work
incomplete enzyme + (vitamin + chemical group = functional coenzyme) join together to form an active enzyme
How is the rate of an enzymatic reaction measured
by how many products can be made in a period of time
What factors can impact the rate of reaction
pH
temp
substrate/enzyme/product concentration
inhibitors
protein modfications
What happens to an enzyme as pH is increased
each enzyme has an optimal pH
- below: not functioning to slow
- at pH: aa residues in the protein structure either protonaed or deprotonated –> can have correct structure // functional groups can catalyze
- above: denatured
most enzyme’s optimal pH = physiological pH or the pH of their environment
How does temp impact reaction rate
higher temp: more atoms and molecules vibrate
most human enzyme operate best at 37C
rate of reaction increases until the temperature at which the enzyme is denatured
temp increases = heat (vibrational) energy make it easier to break chemical bodns until the protein secondary and tertiary structure breaks down
What happens if there is little substrate, what is the impact of the rate of reaction
no substrate = no reaction
What happens if there is little enzyme, what is the impact of the rate of reaction
more enzymes = more product that can be made
enzyme concetration can be controlled by gene expression and protein degradation
What happens if there is little concentration of product, what is the impact of the rate of reaction
when a lot of product –> binds to active site and prevents the reaction from occuring, or go backwards to be converted back into the substrate
What are inhibitors
decrease the rate of reaction
reversible (competetive or noncompetetive or allosteric) or nonreversible
What are irreversible inhibitors
compounds that covalently modify an enzyme
permanent and not reversible and the enzyme is permanently changed
enzyme must be degraded and replaced with a new enzyme
What are reversible inhibitors
bind to enzymes, but not permanent
- competitve
- noncompetetice
- allosteric
What are competitive inhibitors
has similar shape to one of the substrates of an enzymes –> reactions can’t occur –> product is not produced
only inhibit when they are bound in the active site, many can be displaced by increasing the concentration of substrate
slower, gradually reaches vmax
What are noncompetetive inhibitors
does not compete with substrates for binding
- binds elsewhere on an enzyme
results in conformation change inthe enzyme –> prevents the substrate from binding or the reaction from preceeding
Allosteric inhbition: inhibitor binds to allosteric site, active site changes shape so substrate can’t bind
loweres the vmax
How do you turn off an enzyme
Location: keep the enzyme away from its substrate to prevent the reaction from happening
inactive enzyme: some enzymes are kept in an inactive state until they are needed
enzymes cna be modified to turn on and off (ex. post-translational modifications)