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What is an enzyme?
Proteins
Biological catalysts (to catalyze = “to speed up” a chem. reaction)
Enzymes make reactions occur more quickly by lowering the activation energy of a reaction
What is activation energy?
The minimum energy required for a chemical reaction to occur.
Do enzymes change the shape/function of the products/reactants?
No. Enzymes do not change the reactants of products of any chemical reaction - they just make the reaction happen faster
How do Enzymes function?
Enzymes bind to reactant molecules and hold them together so that chemical processes like bond-breaking and bond-forming can occur more readily
Enzymes lower the energy of the transition state
What is the transition state?
The unstable, short-lived point of a chemical reaction where energy is at it’s maximum
Enzyme Graph
graph
Enzymes aren’t changing the starting reactants or ending products
The transition state of a reaction is at the top of the energy “hill” - in the reaction w/ enzyme, the hill is smaller because enzymes lower the energy of the transition state
Endothermic Reactions
graph
absorbs heat/energy from their surroundings
temperature decreases
products have more energy because energy is being absorbed
Exothermic reactions
graph
release heat/energy to their surroundings
temperature increases
products have less energy because energy is being absorbed
HINT: “exo” → the reaction is releasing outside
What does enzyme function look like?
picture of enzyme substrate complex
Enzymes hold reactants together and stabilize them
to catalyze (speed up) a reaction, enzymes will bind to reactant molecules
these reactant molecules are the enzyme’s substrates
the part of the enzyme that the substrate(s) binds to is called the active site
Are enzymes specific or more general?
Enzymes are proteins made of amino acids:
amino acids found in the enzyme’s active site determine the “target molecules” of the enzyme - a.k.a. which substrates will fit into the enzyme, and which won’t
active sites have a specific size, shape, and chemical behavior, so some enzymes will only catalyze certain types of substrates that fit the active site
Lock-and-key Model - how do substrates fit into enzymes?
Image
substrate fits perfectly into the active site like a puzzle piece fitting together
now rejected by most scientists
Induced-fit - how do substrates fit into enzymes?
Image
enzyme changes shape slightly when it binds to its substrate - called “induced-fit”
active site conforms to the substrate shape
scientifically-approved
How do Enzymes lower the activation energy of reactions?
enzymes bring substrates together in the right orientation
favorable environmental environments
temporary covalent bonds with substrate molecules
enzymes are NOT altered by the substrates, and vice versa. They release the products and are ready for the next process of catalysis.
Why are enzymes sensitive to environmental changes?
enzymes have “optimal conditions” when the reaction occurs the fastest
active sites are sensitive to change because they are finely tuned to specific substrate(s)
Impact of temp. change on enzymes
increasing/decreasing the temperature outside of a manageable range can affect the chemical bonds in the active site, making them less suited to binding substrates
(ordinarily an increase of temperature would speed up the rate of the reaction, but too large of an increase would denature the protein)
temperature drops → reaction slows down
(large) temperature increase →protein denatures because bonds are breaking and shape is lost
Impact of pH change on enzymes
active sites have basic/acidic properties that are crucial for catalysis
enzymes work best at a certain pH range
extreme pH values → protein denatures because bonds are breaking and shape is lost
How can the reaction rate be further increased?
option 1: increase enzyme concentration
speeds up reaction until there are no longer any substrates for enzymes to bind to, and the reaction no longer speeds up
more enzymes = “more workers”
option 2: increase substrate concentration
speeds up reaction until all available enzymes are being used and the reaction will no longer speed up
more substrate = “more things to work on”
Why do living organisms needs energy?
energy is necessary for organisms to grow, reproduce, maintain structure, function, and homeostasis
cells use ATP - adenosine triphosphate - to power reactions
What is ATP?
image
a molecule that is the main energy source for all living cells
holds and transports energy within cells
releases energy when one of the phosphate bonds is broken through hydrolysis
What is “energy-coupling”?
use of exergonic reactions to drive endergonic reactions
2 biological reactions are coupled together and linked
ex. catabolic pathways release energy that is used to power anabolic pathways
image
What are endergonic reactions?
require input of energy
non-spontaneous
cannot occur naturally without input of energy
anabolic - builds complex molecules
What are exergonic reactions?
releases “free” energy
spontaneous
can occur without input of energy
What are metabolic pathways?
metabolism: sum of chemical reactions that occur throughout the body within each cell that provides the body with energy
responsible for both breaking down molecules to release energy (catabolic pathways) and building complex molecules from simpler ones (anabolic pathways)
Each step in a metabolic pathway is facilitated by a specific enzyme
A starting substrate is transformed step-by-step into a final product via a series of intermediate molecules.
What are anabolic pathways?
small molecules → larger, complex ones
uses energy
ex. synthesizing proteins from amino acids
What are catabolic pathways?
larger molecules → small molecules
energy is released in the form of ATP
ex. glycolysis, Krebs cycle
What is the first law of thermodynamics?
Law one: energy can be transformed and transferred but cannot be created or destroyed
ex. water in a series of cups can be moved around to a different cup but the total amount states the same
What is the second law of thermodynamics?
Law two: every energy transfer/transformation increases the entropy of the universe
What is entropy?
randomness in the way molecules are arranged
measure of “disorder”
systems move towards more entropy
What are the fundamental qualities of a good experiment?
1 independent variable
clear dependent variable
control group where conditions remain the same
multiple trials
experimental group
controlled variables
What are the positive and negative control groups?
Positive control:
produces the expected result
confirms the functionality of the experimental design
Negative control:
produces no result, or an expected negative result
confirms there are no false positives in the experiment or sources of error
proves there is no outside interference
ex. testing a denatured enzyme will not yield a result because the enzyme is non-functioning - tested to ensure there are no false positives