Lecture Exam 2 SG Flashcards
What is the term for the sum of all chemical reactions in an organism?
Chapter 5
Metabolism
For both catabolism and anabolism, describe the following: (a) is it used to build or break down
molecules, (b) does it use a hydrolysis or dehydration reaction, and (c) are the reactions exergonic or endergonic?
Catabolism: Break down, Hydrolysis, Exergonic
Anabolism: Build, Dehydration, Endergonic
Describe an endergonic vs. an exergonic reaction. Give an example of each.
Endergonic: Cold, Absorbs energy, Photosynthesis
Exergonic: Hot, Releases energy, Explosion
When a chemical bond forms, does this release or store energy?
This stores the energy which can be released by breaking the bond
Does an exergonic or an endergonic reaction require a high amount of potential energy for the reaction to occur? Why?
An exergonic reaction requires more PE than an endergonic reaction because energy must be released as opposed to endergonic reactions which absorb energy
What are the three types of metabolic pathway patterns? Give an example for each.
Linear: Starch hydrolysis
Branched: Glycolysis
Circular: Kreb’s cycle
Why are some organisms able to carry out certain metabolic processes and while other organisms
cannot? For example, yeast perform alcoholic fermentation and humans cannot. Why is the human body physiologically unable to perform alcoholic fermentation?
Metabolic pathways are determined by enzymes and enzymes are encoded by genes. If humans do not have the gene required to make enzymes that are needed for processes such as alcoholic fermentation we cannot perform these processes
Why is it necessary for all organisms to possess some form of metabolism? Which class of
macromolecule provides the most cellular energy?
It is important for all organims to posses some form of metabolism because metabolism allows us to store and release energy using organic molecules. If this was not the case organims would need to constantly eat to survive. Carbohydrates provide the most cellular energy as they can be oxidized.
Which part of ATP’s structure allows it to store potential energy? What happens to ATP when its
stored energy is released?
The phosphate component is where the energy is held. When energy is released from ATP it becomes ADP and Pi due to the loss of energy showing that a phosphate that had energy has been shed.
Define the following terms: collision theory, activation energy, and reaction rate.
Collision Theory: Atoms/ molecules must collide to be able to react
Activation Energy: Minimum amount of energy required to make a reaction occur
Reaction Rate: Number of Products over seconds
What are the ways that a reaction rate can be increased?
Increase heat, increase enzyme/substrate, increase pressure, aggitate
A(n) ______________ is a type of protein that accelerates the rate at which a chemical reaction takes place in an organism.
Enzyme
Enzymes are usually made of which type of macromolecule?
Polypeptides
Does a specific enzyme usually catalyze one specific reaction or many types of reactions?
An enzyme usually catalyzes a specific reaction
Lactose is the _________________ of the enzyme ___________________.
Substrate
Lactase
How do enzymes work?
The globular protein has an activation site where a substrate can attach and this will induce a reaction that lowers the energy required to make a reaction occur. once the chemical reaction has occured, the product will be released and the enzyme can catalyze the reaction once more
Name the region of the enzyme that binds to the substrate.
Active Site
Define the following parts of an enzyme: apoenzyme, cofactors, holoenzyme, active site, and allosteric site.
Apoenzyme: Protein component of enzyme
Cofactor: Non protein component of enzyme
Holoenzyme: Apoenzyme + Cofactor (fully functional)
Active site: Location where substrate binds
Allosteric site: Molecular on/off switch for enzyme
Name and describe two types of cofactors. What is the role of an enzyme cofactor?
Cofactors: The non protein portion that helps a reaction occur. Often play a role in stabilizing the enzyme or catalyzing the enzymatic action
Inorganic: Iron in heme, Mg, Cu
Organic (coenzymes): NAD+, NADP+, FAD, CoA
NAD+, NADP+, FAD are all electron carriers
Describe the mechanism of enzymatic action (4 steps)
- Substrate makes contact with binding site
- Enzyme and substrate form complex (induced fit)
- Substrate is transformed and released
- Enzyme remains unchanged and available for further reactions
List the factors that influence enzymatic activity. Briefly describe how each factor affects enzymatic
activity.
Temperature - Increased molecular motion as temp increases
Pressure - Less space means more molecules bumping increasing reaction rate
pH - If pH is not ideal, the denatured enzyme can stop functioning
Concentration - More substrate or enzyme can increase reaction rate unless one factor is limited by the other
Inhibitors - Some inhibitors can either compete with substrates or turn off enzymes resulting in decreased reaction rates
What is the difference between competitive and noncompetitive inhibition? Which type of inhibitor
can be reversed by increasing the substrate concentration? Which type of inhibitor has a structure that is similar to the normal substrate?
Competitive: Competes with substrate to block activation site
Noncompetitive: Binds to allosteric site resulting in enzymatic shape change which makes enzyme inactive
- Competitive
- Competitive
How does sulfanilamide inhibit the synthesis of folic acid? Why is this important?
Sulfadrug is a competitive inhibitor that is analogous with PABA. Because bacteria such as S. aureus or E. coli rely on making folate it will inhibit bacteria by competing for active sites
Describe feedback (end-product) inhibition and how it works.
- A pathway in which the end product inhibits enzyme activity
- Excess product binds to allosteric site on the first enzyme in the pathway deforming activation site and shutting pathway down
- As [end product] decreases activesites reform and pathway resumes