Proteins, Lipids, Carbs and Enzymes Flashcards
What is feedback inhibition?
When the product of a pathway prevents too much build of the product
Why is feedback inhibition important?
It provides a means of self-regulating the system.
What type of regulation control the conversation of threonine to isoleucine?
allosertic regulation. The final product of this reaction threonine is an allosteric inhibitor of the first enzyme.
Does the threonine deaminase have both an active and an allosteric site?
Yes, it does. The active site is where the substrate threonine binds. The allosteric site is where isoleucine binds to performs feedback inhibition
What are the two ways energy is created in a cell?
- ) Transfer of high energy electrons
2. ) Transfer of a phosphate group
What happens when a molecule loses an electron?
Oxidation
What happens when a molecule gains an electron?
reduction
Oxidation is endergonic or exergonic?
When something is oxidized the reaction that has occurred is exergonic
Is reduction endergonic of exergonic?
When somethings is reduced the reaction that had occurred is endergonic
What is the formula for glucose?
C6H12O6
Is ATP like rna or dna?
It is like DNA because of the OH on both point of the ribose
What is phosphorylation?
The addition of a phosphate group to a substate during to drive endergonic reactions.
What would causes irreversible changes to an enzyme?
They are often the result of changes to the protein’s primary structure.
What does pH alter the secondary and tertiary?
Changes in pH alter the hydrogen bonds.
How do polymers form?
Via condensation
How do polymers break apart?
Via hydrolysis
What is the shape of saccharides?
A linear ring formation
What stabilizes the secondary structure of proteins?
Polar interactions between the back bone. The R groups are not involved.
What stabilizes the tertiary structures of the protein?
interactions between the R groups. This is often called the 3-D protein
What bonds the quaternary structure of proteins?
relationship among the polypeptide chains are stabilized by r-group interactions, h bonds, ionic interactions
What must proteins have in order to have a quaternary structure?
More than one subunit
What is a peptide bond and why does it matter?
Holds the backbone of amino acids together.
peptide bond is a chemical bond formed between two molecules when the carboxyl group of one molecule reacts with the amino group of the other molecule, releasing a molecule of water (H2O). This is a dehydration synthesis reaction (also known as a condensation reaction), and usually occurs between amino acids.
What causes protein to denature?
Changes in environment and chemical interactions can alter protein shape.
Often a non-permanent change. Not at the primary level. It is al alteration in protein folding.
When proteins are broken down to amino acids in your stomach and small intestine, we would say that the protein has been:
Hydrolyzed