Second Wave Flashcards
Maximal velocity of an enzyme-catalyzed reaction
Vmax
Substrate concentration at which the reaction velocity is equal to 1/2 Vmax
Michaelis constant
Rate independent of substrate concentration
Zero (constant rate)
Rate proportional to substrate concentration
First (half,half,half,half)
Structure of the inhibitor resembles the substrate
Competitive inhibition
Vmax is lowered
Non competitive inhibition
Km does not change
Non competitive inhibition
Affinity of enzyme to the substrate is decreased
Competitive inhibition
The inhibitor and the substrate bind at different sites on the enzyme
Non competitive inhibition
Malathion’s effect on acetylcholinesterase
Non competitive inhibition
Simvastatin’s effect on HMG-CoA reductase
Competitive inhibition
Rate of reaction in High substrate concentration
Increase
Rate of reaction in Low substrate concentration
Decrease
Rate of reaction in Low temperature
Decrease
Rate of reaction in High temperature
Increase
Rate of reaction in both high & low pH
It depends
In Nitrogen balance, State where intake is greater than excretion. There is net accumulation of proteins.
Positive
In Nitrogen balance, State where excretion is greater than intake. There is net breakdown of proteins.
Negative
Enzyme that catalyze the transfer of the amino group of AAs to glutamate
Aminotransferase
Oxidatively deaminates glutamate to liberate free ammonia (kidney & liver)
Glutamine Synthetase
Deaminates glutamine to glutamate in the kidney and intestines
Glutaminase
Compounds in which organisms excrete excess nitrogen
Ammonia, Uric acid & Urea “AUU”
Produces urea from free ammonia
Urea cycle
Location of urea cycle
Mitochondria & Cytoplasm (Liver only)
Reactants for Urea cycle
Ammonia, CO2 & Aspartate “ACA”
End product of urea cycle
Urea
Rate Limiting step for Urea Cycle
NH3+CO2 -> carbamoyl phosphate
Rate limiting enzyme for urea cycle
Carbamoyl Phosphate Synthase I
Three compounds that are immediate donors of the atoms of urea
Free ammonia, Aspartate & CO2 “FAC”