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metabolism
all the chemical reactions that take place in cells
anabolic reactions
build molecules and require energy to occur
catabolic reactions
break down molecules and release energy
metabolic pathway
consists of many chemical reactions that require energy transformations
what is each step of a metabolic pathway?
a separate chemical reaction catalyzed by a specific enzyme
what is the relationship between each kind of metabolism
every kind of metabolism is connected
potential energy
energy stored due to an objects position, structure, or arrangement
kinetic energy
energy an object has because of its movement
thermodynamics
study of energy and energy transformations
system
matter being studied in thermodynamics
surroundings
everything outside the matter being studied in thermodynamics
open system
exchanges both energy and matter with its surroundings
what is an example of an open system?
humans
closed system
exchanges only energy with its surroundings
isolated system
exchanges neither matter nor energy with its surroundings
1st Law of Thermodynamics
states that energy can’t be created or destroyed
2nd Law of Thermodynamics
states that when energy is transfered or transformed, some energy is lost as heat
entropy
disorder
do cells have high or low entropy
low (they are highly organized, so they have low disorder and therefore low entropy)
what is the relationship between order and entropy?
as order increases, entropy decreases
Gibbs free energy (G)
energy from a chemical reaction available to do work after accounting for entropy
delta G
energy of the final state - energy of the initial state
what is the delta G for endergonic reactions
positive
what is the delta G for exergonic reactions?
negative
what kind of reactions are exergonic?
catabolic
what kinds of reactions are endergonic?
anabolic
are monomers or polymers more stable
polymers
what happens when ATP is dephsophorylated?
water is absorbed and energy is released
what happens when ATP is phosphorylated
energy is absorbed and water is released
phosphorylation
when a phosphate group is added
dephosphoralation
when a phosphate group is removed
which reactions are spontaneous/non-spontaneous
endergonic is nonspontaneous, exergonic is spontaneous
which reactions require/release energy
endergonic requires energy, exergonic releases energy
which reactions result in an increase/decrease in stability?
endergonic increases stability, exergonic decreases stability
which reactions require activation energy
endergonic and exergonic
which phosphate group on ATP is the closest to ribose? the middle? the farthest?
closest is Alpha, middle is beta, farthest is omega
is ATP stable or unstable? How is energy stored as a result
ATP is unstable, so energy is stored in more stable forms (like carbs and fats) so ATP does not disassociate and waste energy when its not needed
enzyme
molecule (typically protein) that catalyzes biochemical reactions
active site
region of enzyme where substrate binds and reaction occurs
allosteric site
different site on an enzyme where another molecule can bind and alter how the enzyme works
substrate
specific molecule an enzyme acts on; can be multiple depending on the reaction
how do enzymes catalyze biochemical reactions?
by lowering the activation energy
what do enzymes not do?
change the free energy of reactants or products, change delta G, change if a reaction is endergonic or exergonic, don’t get used up
what regulates which reactions occur and at what rate they occur in metabolic pathways?
enzymes
what are the environmental factors that impact enzyme activity?
pH, temperature, salt concentration
what are the physical location factors that impact enzyme activity?
which organism, tissue, or area of the cell the enzyme is in
regulatory molecules/cofactors/coenzymes
molecules that affect enzyme activity
examples of coenzymes
Fe2+, Mg2+, NAD+, FAD
inducers
regulatory molecules that increase enzyme activity by binding to the allosteric site
competitive inhibition
when an inhibitor binds to the active site to prevent the substrate from binding to the enzyme
noncompetitive/allosteric inhibition
when the inhibitor binds to the allosteric site to prevent the substrate from binding to the enzyme
allosteric regulation
when a molecule binds to the allosteric site to control the affinity of the enzyme for the substrate
what is the difference between a competitive inhibitor and a noncompetitive inhibitor
a competitive inhibitor temporarily decreases the rate of reaction, while a non-competitive inhibitor permanently decreases the rate of reaction