Enzymes Flashcards
What is the purpose of Enzymes?
Catalyze, convert, combine substrates into products
How is affinity defined?
How well the substrate interacts with the binding site.
What does a stronger affinity indicate?
The less substrate is needed to achieve a given rate of reaction
Explain how enzymes affect the reactions
They do not change the overall energy of the reaction.
They accelerate the reaction, by lowering the activation energy or increasing the rate of the reaction
Explain Substrate concentration in high and low states
Too low of a substrate concentration, leads to a slower rx rate
Too High of a substrate concentration leads to substrates rx with different enzymes
What two things can affect the efficiency of the Rxn Rate?
Mutations, Cellulary regulatory molecules
How is the product effected when there is a high substrate?
High substrate causes increased production of the product and reaction slows when the product is too high
What are the two categories of cofactors?
Organic and Non-Organic
Organic: NADH, NADPH
Inorganic: Metal ions
What is PKU or Phenylketonuria?
Caused by the deficency of the enzyme phenylananine hydroxylase, which is required to covert phenylalnine to tyrosine
Define Rate
The speed at which an enzyme catalyzes a reaction
Define Enzyme Regulation
Via numerous factors is the effect to increase (activate) or decrease (inhibit) the rate
What is the difference between a Competitive inhibitor and non-competitive inhibitor?
Competitive Inhibitor fights for adherence to the active site before the substrate to decrease or eliminate activation
Non-Competitive Inhibitor attaches to someplace other than the active site cuasing a change confirmation that can either increase or decrease the rate
What to B-Lactam Antibodics do to demonstrate Competitive Inhibition>
They mimic the end amino acid sequence of unlinked peptidoglycogne and irreversibly bind to the active site to completively block final cross-linking reaction
Define Allosteric regulation
Involves the binding of an effector molecule to facilitate additional binding of the substrate (positive cooperatility) or inhibition of the substrate (negative cooperativity)
Why are Allosteric enzymes an exception to the M-M model?
Allosteric enzymes have more than two subunits and an active site
