exam 3 Flashcards
metabolism
emergent property of life tat arises from orderly interactions between molecules
made of chemical reactions arranged as intersection metabolic pathways
metabolic pathway
a specific molecule is altered in a series of defined steps, resulting in a product
each step of the pathway is catalyzed by a specific enzyme
catabolic pathways
release energy by breaking down complex molecules into simpler ones
cellular respiration
anabolic pathways
consume energy to build complicated molecules from simpler ones
photosynthesis
bioenergetics
study of how energy flows through living organisms
energy
capacity to cause change
kinetic energy
energy associated with the relative motion of objects
thermal energy
kinetic energy associated with the random movement of atoms or molecules
heat
heat
transfer from one object to another with thermal energy
potential energy
energy that is not kinetic
it is energy that matter posesses because of location or structure
chemical energy
potential energy available for release in a chemical reaction
thermodynamics
the studyi of the energy transformations that occur in a collection of matter
isolated system
unable to exchange either energy or matter with suroundings
open system
energy and matter can be transferred between the system and its surroundings
first law of thermodynamics
energy can be transferred and transformed, but it cannot be created or destroyed
also known as principle of conservation of energy
second law of thermodynamics
every energy transfer or transformation increases the entropy of the universe
entropy
measure of disorder, randomness
spontaneous process
a process that can occur without an input of energy
free energy
portion of a system’s energy that can perform work when temperature and pressure are uniform throughout the system, as in a living cell
exergonic reaction
proceeds with a net release of free energy
change in G is negative because the chemical mixture loses free energy
endergonic reaction
one that absorbs free energy from its surroundings
because this kind of reaction essentially stores free energy in molecules the change in G is positive
equillibrium
term used to describe a state of maximum stability
energy coupling
the use of an exergonic process to drive an endergonic one
atp is responsible for mediating most energy coupling in cells
adenosine triphosphate
contains a sugar ribose, with the nitrogenous base adenine and a chain of 3 phosphate groups bonded to it
in addition to its role in energy coupling, ATP is also one of the nucleoside triphosphates used to make RNA
phosphorylated intermediate
the recipient with the phosphate group covalently bonded to the ATP
enzyme
macromolecule that acts like a catalyst
catalyst
chemical agent that speeds up a reaction without being consumed by the reaction
activation energy
the intial investment of energy for starting a reaction
abbreviated Ea
substrate
the reactant an enzyme acts on is referred to as this
enzyme-substrate complex
when the enzyme binds to the substrate
induced fit
the shape change of an enzyme to make an active site fit even more snugly around the substrate
cofators
nonprotein helpers for catalytic activity
may be bound tightly to the enzyme as permanent residents, or they may bind loosely and reversibly along with the substrate
coenzyme
cofactors that are organic
vitamins are coenzymes
competitive inhibitors
reduce productivity of an enzyme by blocking substrates from entering active sites
noncompetitive inhibitors
do not directly compete with the substrate to bind to the enzyme at the active site
instead they impede enzymatic reactions by binding to another part of the enzyme
allosteric regulation
any case in which a protein’s function at one site is affected by the binding of a regulatory molecule to a seperate site
regulatory molecules
molecules that naturally regulate enzyme activity in a cell behave like reversible noncompetitive inhibitors
activator vs inhibitor
the binding of an activator to a regulatory site stabilizes the shape that has functional active sites, whereas the binding of an inhibitor stabilizes the inactive form of the enzyme
cooperativity
substrate molecule binding to one active site in a multi subunit enzyme triggers a shape change in all the subunits, thereby increasing catalytic activity and other active sites.
Amplifies the response of enzymes to subtrates
feedback inhibition
a metabolic pathway is switched off by the inhibitory binding of its end product to an enzyme that acts early in the pathway
fermentation
the partial degradation of sugars or other organic fuel that occurs without the use of oxygen