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Enzyme Kinetics
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steady-state kinetics
[ES] constant rate of formation=rate breakdown of [ES] complex
what does Km=
(k
2
+ K
-1
)/ k
1
Michaelis Menton Equation
V
o
= V
max
[S]/(K
m
+ [S])
K
cat
=
V
max
/[E
t
]
BiBi rxns
ordered bibi
random bibi
ping-pong mech
Types of Enzyme Inhibition
Reversible
-Competitive
-Uncompetitive
-Mixed
Irreversible
-Noncovalent
-Covalent
Competitive inhibitor
Inhibitor binds to the enzyme active site and prevents binding of S and vice versa
what is α?
1 + [I]/K
I
Michaelis-Menton Equation Competitive inhibition
Vo = Vmax [S]/(Kmα + [S])
A competitive inhibitor...
affects K
m
not V
max
Uncompetitive inhibition
I binds only to ES complex
An uncompetitive inhibitor ...
lowers V
max
and K
m
Michaelis-Menton Equation uncompetitive competition
Vo = Vmax [S]/(Km + [S]α')
Mixed Inhibition
Inhibitor binds to both the E and ES at a site distinct from where S binds
Michaelis-Menton Equation Mixed Inhibition
Vo = Vmax [S]/(Kmα + [S]α')
A mixed inihibitor
lowers Vmax
Apparent Vmax Competitive Inhibitor
V max
Apparent Km Competitive Inhibitor
αKm
Apparent Vmax Uncompetitive Inhibitor
Vmax/α'
Apparent Km Uncompetitive Inhibitor
Km/α'
Apparent Vmax Mixed Inhibitor
Vmax/α'
Apparent Km for Mixed Inhibition
αKm/α'
Irreversible Inhibition
Affects Km and Vmax
destroys enzyme
Noncovalent (transition state analogs)
Covalent modification (special classes)
Suicide Inactivators
Covalent irreversible inhibitor
Simplifying assumptions of MM treatment
K-2 insignificant
[P] insiginificant
V=k2[ES] but hard to measure k2 or [ES]
steady state assumption haldane
Pre-Steady State Kinetics
Single turnover
Rapid Mixing/sampling
typical enzyme in MM treatment
Rxn vs[S]
Saturation Kinetics
can be explained by ES
how to find Vmax and Km from reciprocal plot
slope=Km/Vmax
y-intercept=1/Vmax
x intercept=1/km
what does the dissociation constant equal
in MM Kd=Km=K-1/k1
lineweaver-burk equation
1/Vo=(km/vmax)(1/[S])+(1/vmax)
Author
Sheilaj
ID
335007
Card Set
Enzyme Kinetics
Description
stuff
Updated
2017-10-19T16:24:28Z
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