9 - Energetics and Dynamics Flashcards
structure of an enzyme?
sachride interacting residue
catalytic residue
extended binding cleft
steps of an ezyme reaction?
enzyme + substrate [binding] enzyme subtrate complex [catalysis] Enzyme-product complex [release] enzyme + product
understand an exergonic reaction and endergonic using Gibbs?
if G more than 0
- EXERGONIC
- energy is lost
if G less than 0
- ENDERGONIC
- energy not lost
coupling energonic and exergonic?
.
substrate factors that enzyme function depends on?
- localisation of sub
- orientation
- binding energy
what step is the slowest step in a reaction?
K2
step from enzyme substrate –> enzyme + product
- K2 = Kcat
what are the 3 assumptions of the michaelis-menten calc?
- Reverse reaction is neglible
- Only single Enzyme Substrate complex
- Assume subtrate is in much more excess than enzyme and [S] isn’t affected
understand initial rate and [S] graph?
.
what is the Vmax and the eq?
theoretical max where enzyme is fully saturated [limiting factor]
Vmax = Kcat [E]t
What is Vo
half the Vmax
cant be obtained as you don’t know the Vmax
so use m-m eq
michealis menten eq?
Vo = Vmax [S] / Km + [S]
(Vmax is also Kcat[E]t)
what is Km?
Michealis constant
[S] when reaction is 1/2 maximal
how to find Km?
line where Vo meets curve then down to [S]
what is Kcat?
Kcat is the slowest step so the K2 step
what does a
- high Kcat value mean
- small Km value mean
high Kcat
- rapid turnover
small Km
- high substrate affinity