Test 2 Flashcards
First Law of Thermodynamics
Energy cannot be created nor
destroyed, but can be transformed
Second Law of Thermodynamics
Disorder always increases (+ ∆S)
∆H<0
Exothermic
∆H>0
endothermic
∆G<0
Exergonic
∆G>0
Endergonic
The higher the activation energy “hump” the _ the reaction
slower
provides alternative reaction pathway with lower activation energy
catalyst
_ increases the rate of a reaction
catalyst
Catalysts cannot do what
cannot change equilibrium position, cannot change Delta G or free energy of reaction
The higher G°‡ the _ the reaction
slower
catalyst lower_and speed up reaction
G°‡
G° equation
ΔG° = - RT ln Keq
what is zero order kinetics
rate does not depend on concentration of substrate
what is first order kinetics
rate depends on concentration of substrate
Michaelis-Menten equation
V0= (V max [S])/(KM + [S]). Vmax or Vm is the max velocity of the enzyme. KM is the steady-state constant or Michaelis constant
KM equation
KM= [S] at Vmax/2
at [S] , KM-> low V init
enzyme not very active
at [S] <KM-> high V init</KM->
enzyme more active
what is Km
substrate concentrate at 1/2 Vmax
what is Km
concentration of substrate at cellular concentration in most cases
Different substrates of the same enzyme have different?
Km
Low values of Km indicate ?
tighter binding affinity
Michaelis Menten cure can be transformed into ?
a straight line
what is a reversible inhibition
an inhibitor that binds to and dissociates from an enzyme form reaching equilibrium
what are the most common ways enzymes are regulated
cellular regulators, drugs
what are the types of reversible inhibition
competitive, non competitive
job of competitive inhibition
S competes with inhibitor I for active site on E ➔ either S or I binds to E ➔ more
substrate required to reach a given reaction velocity
job of noncompetitive inhibition
Inhibitor can bind to E or ES; S can bind to E or EIDifferent binding sites!