Enzymes Flashcards
What is an Enzyme?
Enzymes are proteins that help speed up metabolism, or the chemical reactions in our bodies.
It is a catalyst
What do enzymes consist of?
Amino acids- end in -ase, ex: amylase,maltase,sucrase
What is the function/goal of the enzyme?
To speed up the rate. RXN
What is activation energy?
The minimum amount of energy to start the rate RXN
What makes up an enzyme?
Weak hydrogen bonds, and amino acids
What does the substrate do?
It attaches to the enzymes active site
What are reactants?
a substance that takes part in and undergoes change during a reaction. On the left hand side.
What are products?
Products are the end result of the reaction and are written on the right-hand side of the equation.
What group do cofactors and coenzymes live in?
Prosthetic groups, they increase the rate of enzyme catalyzed reactions
What are coenzymes?
organic molecules that are needed to attach to certain enzymes to carry out the chemical reaction
How do coenzymes work?
They attach to the enzyme and allow substrate to bind and the reaction occurs.
What is an example of a coenzyme?
Vitamin B
What type of substance is cofactors classified as?
The are classified as metalion substances.
Example of cofactors?
Non-protein and organic ions. (lead)
What does hemoglobin do?
It is a protein that carries oxygen in blood cells.
What do inhibitors do?
Slows the rate of enzyme catalyzed reactions
Irreversible inhibitors
Forms a covalent bond with the enzyme at its active site therefore permanently blocking the subtrate.
Example of irreversible inhibitor?
Pb – lead —-> lead poisoning affects 3rd structure of the neurological protein.
Reversible inhibitor
Forms a temporary bond with the enzyme therefore slows the reaction rate while the inhibitor is bound to the substrate.
How can you overcome the effects of the reversible inhibitor?
By adding more substrate.
Example of rev. inhibitor ?
CO2 binds to hemoglobin
What does irreversible inhibitor do to the body?
It denatures the cells in the body
Competitive inhibitors
Inhibitors with a similar size and shape to a substarte.
What do Competitive inhibitors do?
They compete with the substrate to bind with the active site
Example of Competitive inhibitors?
Antibiotics —–> blocks enzymes needed for reproduction
What does the active site do?
Maintains homeostasis and binds with the catalyst
what is pH
measure of the concentration of hydrogen ions in a soloution
What is the optimum temperature for an enzyme to function and max rate?
37 C and 98.6 F
What happens if you go beyond pH opt.
Enzymes starts to denature and breaks R group.
More heat =________?
Denatures
Substrate concentration
There is a fixed amount of enzyme but increasing amount of substrate.
Enzyme concentration
There is a fixed amount of substrate but an increasing amount of enzyme
Allosteric site
site where the allosteric inhibitor binds to the enzyme
Allosteric inhibitor
Inhibitor that is non competitive, does not compete with substrate but binds to enzymes allosteric site.
What happens if body temp. goes beyond the optimum?
Enzymes starts to denature
Can enzymes that are denatured, renature?
Yes, only sometimes, not always possible
