Test 3 Flashcards
metabolism
all the chemical reactions that take place within an organism
metabolic pathway (catabolic)
involves the breakdown of a molecule into smaller subunits, releasing energy stored in the chemical bonds of reactants
metabolic pathways (anabolic)
involves the synthesis (construction) of cellular molecules and macromolecules from smaller subunits, consuming energy
work
accomplishing a changes in the position or state of matter
kinetic energy
energy associated with movement
potential energy
stared energy due to structure or location
First Law of Thermodynamics
energy cannot be created or destroyed, but can be transferred/transformed from one type to another
Second Law of Thermodynamics
everything in the universe is subject to spontaneous disorder
entropy
measure of disorder/chaos
free energy
portions of systems energy that is usable for work when temperature and pressure are uniform
exergonic
releases energy
endergonic
requires energy
ATP
adenosine triphosphate - the universal energy currency of a cell
catalyst
chemical agent that speeds up the rate of a chemical reaction without being consumed by the reaction
enzymes
specialized catalytic proteins found in living cells
ribozymes
RNA molecules with catalytic properties
activation energy
initial input of energy needed to start a reaction (push reactants over an energy barrier)
substrate
reactant that binds to enzymes activate site
active site
the shape-specific building site on an enzyme into which its substrate fits
induced fit
the temporary gripping of substrate by an enzyme, due to shape change confirmation of the enzyme on order to have tight interactions with the substrates
cofactor
non-protein helpers that bind to enzymes to maximize their function and are the reason why you should take daily multivitamin supplements
coenzyme
organic molecules that help to optimize enzyme function, but are left uncharges by a reaction
free
free
competitive inhibition
the inhibitor binds to an active site of an enzyme, directly blocking any substrate from binding
noncompetitive inhibition
the inhibitor binds to an allotteric site not the active site changing the enzymes shape
allosteric regulation
a situation in which a proteins function at one site is affected by the binding of a regulatory molecule at a separate site
allosteric site
specific receptor region on an enzyme that is not the active site
activator
a molecule capable of stabilizing enzyme shape and function
inhibitor
will cause that enzyme to lose its functional shape
feedback inhibition
high levels of an “end product: of a metabolic pathway can inhibit the reaction that produces more of the product
cooperativity
the binding of one substrate to a multi-unit enzyme stabilizes favorable shape conformation for all of the other enzyme subunits
Is a cell a closed system
no
Why is some energy lost as heat during energy transfer
When energy is lost as heat it is the energy of random molecular motion and the universe tends towards entropy which is the measure of disorder
When would the coupling of endergonic reactions occur spontaneously
if the net ∆G is negative.
What are ATP molecules often used for
to store the energy harvested from exergonic reactions for later use in endergonic reactions
What type of molecule will have more potential energy
larger molecules have more than smaller ones
how do enzymes and ribosomes effect biological reactions
by lowering the activation energy needed for a reaction to begin
Are ribosomes and enzymes consumed during a reaction
no
What is an example of a catabolic reaction
cellular respiration
what is an example of an anabolic reaction
photosynthesis
Why do cells use enzymes, rather increase their temperature, to overcome the activation energy needed for a reaction to begin?
temperature increase can only push reactants to the transition site, enzymes can (1) position reactants together to facilitate bonding (2) strain bonds in reactants to make it easier to achieve transition state (3) change the local environment
Does an enzyme alter the ∆G value of a chemical reaction?
enzymes do not have an impact on ∆G
Can one type of enzyme bind to a large number of different substrate types?
No, an enzyme is made to bond to one specific substrate.
What happens when an enzyme is saturated in a solution with substrate
the speed of the reaction will plateau
Is the inhibition of an enzyme always a reversible event?
It is not ALWAYS reversible but it is pretty common
Can increasing substrate levels “overcome” both competitive and noncompetitive inhibition? Why or why not?
Increasing substrate levels can over come competitive inhibitor because it becomes more likely for the enzyme to react with the substrate. It will NOT be able to over come noncompetitive inhibition because this type of inhibitor changes shape and fits into the enzyme not allowing for anything to bind
What gave rise to the large diversity of enzymes that we observe today?
evolutionary processes acting upon random mutations
What is an example of kinetic energy
the energy of running water
what is an example of potential energy
water behind a dam because of its altitude above sea level
If a reaction is able to proceed spontaneously (after inertia is overcome), will it result in a higher or lower amount of entropy being present?
lower
In order for a reaction to be spontaneous (after inertia is overcome), does the value of ∆G need to be positive or negative?
negative
How might an enzyme strain substrates in order to make them more likely to undergo a chemical reaction
temporarily gripping of substrates due to change in shape
Why do temperature and pH affect the function of enzymes?
at high temperatures, enzymes can function at a faster rate, but if it gets too high then it can cause the enzyme to denature
Would all allosteric regulation be classified as noncompetitive inhibition?
Practically all of them, there are a few unique cases in which this would be untrue
What are some of the ways in which metabolic pathways are regulated in living systems
feedback inhibition