02. ENZYMES AND BIOENERGETICS Flashcards
protein catalysts that increase the velocity of a chemical reaction and are not consumed during the reaction they catalyze
enzymes
classes of enzymes
oxidoreductases transferases hydrolases lyases isomerases ligases
properties of enzymes
active site
efficient
specific
require cofactors
bind in a transient dissociable manner either to the enzyme or to a substrate
cofactor
serve as recyclable shuttles - or group transfer agents - that transport many substrats from their point of generation to their point of utilization
coenzyme
enzymes work by
lowering the free energy of activation
enzymes that follow michaelis-menten kinetics have a ________ curve
hyperbolic
____ Km has _____ substrate affinity
HIGH Km = LOW substrate affinity
LOW Km = HIGH substrate affinity
Above Km
zero order kinetics
rate not affected by [S]
Below Km
first order kinetics
rate directly proportional to [S]
increase in temperature =
increase in reaction rate
very high temperature =
decrease in reaction rate due to denaturation
reciprocal of the michaelis menten equation
lineweaver burk plot
lineweaver burk plot
used to calculate Km and Vmax
Competitive inhibition: mechanism reversal Km Vmax
Competitive inhibition: mechanism - competes for binding site reversal - increase [S] Km - increased Vmax - not changed
Non-competitive inhibition: mechanism reversal Km Vmax
Non-competitive inhibition: mechanism - bind somewhere else reversal - increase [E] Km - not changed Vmax - lowered
kinase
attach phosphatase
phosphokinase
remove phosphatase
ΔG
net loss of energy (exergonic)
spontaneous reaction
ΔG > 0
net gain of energy (endergonic)
not a spontaneous reaction
ΔG = 0
equilibrium
forward and backward reactions are equal
ΔG
standard free energy change
Enthalpy -
Entropy +
Spontaneous?
YES. Always
Enthalpy +
Entropy -
Spontaneous?
NO. Always
Enthalpy +
Entropy +
Spontaneous?
MAYBE, but only at high temperatures
Enthalpy -
Entropy -
Spontaneous?
MAYBE, but only at low temperatures
greatest quantitative source of high energy phosphate in aerobic organisms
oxidative phosphorylation
In glycolysis, ATP is generated in 2 steps
1,3 BPG + ADP -> 3PG + ATP (physphoglycerate kinase)
PEP + ADP -> pyruvate + ATP (pyruvate kinase)
in the citric acid cycle, ATP is generated in 1 step
syccinyl CoA + ADP > succinate + ATP (succinyl thiokinase)
2 electron carriers used in ETC
NAD
FAD
NAD is derived from which vitamin
niacin B3
FAD is derived from which vitamin
riboflavin B2