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Anabolic Pathway
pathways that consume energy to build complicated molecules from simpler compounds
Catabolic
pathways that release energy by breaking down complex molecules into simpler compounds
Cofactors
non-protein molecules that assist enzyme function; inorganic co-factors consist of metals; can be bound loosely or tightly; holoenzyme (enzyme with co-factor attached)
Non-competitive Inhibitors
binds to an area other than the active site (allosteric site), which changes the shape of the active site preventing substrates from binding
Competitive Inhibitors
reduce enzyme activity by blocking substrates from binding to the active site; inhibition can be reversed with increased substrate concentration; Competitive inhibitors “competes” with substrate
Activation energy
the minimum amount of energy required to start a chemical reaction. Enzymes lower the amount of energy needed for a reaction to occur.
1st Law of Thermodynamics
energy cannot be created or destroyed; energy can be transferred or transformed
ex. the chemical (potential) energy stored in the nut will be transformed into kinetic energy for the squirrel to climb the tree
Kinetic energy
energy associated with motion
Potential energy
stored energy
Free energy
energy that is available to do work at constant pressure and temperature
Exothermic
releases energy, typically heat, into the surroundings
Endothermic
absorbs energy, typically heat, from its surroundings
ATP (Adenosine Triphosphate)
molecule that organisms use as a source of energy to preform work
How is ATP used for energy?
ATP couples with exergonic reactions to endergonic reactions to power cellular works
Organisms obtain energy by breaking the bond between the 2nd and 3rd phosphate in a hydrolysis reaction
Phosphorylation: the released phosphate moves to another molecule to give energy
Temperature (effect on enzyme function)
the rate of enzyme activity increases with temperature (due to collision) up to a certain point. After a certain point the enzyme will denature
pH (effect on enzyme function)
being outside the normal pH range can cause hydrogen bonds in the enzyme to break, changing the shape of the concentration
Substrate Concentration (effect on enzyme function)
increased substrate concentration increases activity because more substrate molecules are available to bind to the enzyme’s active site
Salinity (effect on enzyme function)
disrupts the enzyme’s structure and function. Low salinity can cause charged amino acid side chains to attract each other, leading to denaturation and aggregation
Major Ideas about Lab
The effect of enzyme concentration, temperature, pH, and substrate concentration
Increased enzyme concentration increases rate of reaction