chapter 7 Flashcards
kinetics
study of reaction rates
velocity
rate of substrate A becoming product
Decrease of substreate over increase in time
-D(A)/Dt
increase in product over increase in time
D(P)/DT
One substrate results in A=P
V=k(A)
first ordered reactions
Two substrates result in A+B=P
V = K(A)(B)
Second ordered reactions
What is michealis-menten equation and explain it
E+s=ES=E+P
E+s and E are reversible
Substrate in excess enzyme complexess with substrate, product formed
E+P is not reversibile
michelis constant
indicates the enzyme-substrate affinity
Vmax
describes the substrate concentration when enzyme is saturated
does substrate concentration affect reaction
nop ammount of enzymes do and as more substrates come the velocity platues
what does higher Km result in
a lower affinity
isoenzymes
different enzymes that can catalyze the same reaction
- it can be different kinteics (reaction rate)
- it can have different regulations
- it can be expressed in diferent tissues
sequential
2 substrates and 1 enzyme
double-displacement
an enzyme substitution in the middle
Alosteric enzymes
regulated enzymes taht allow for metabolism and metobolite flush and complex metabolic pathways
metabloism and enzymes
it is a sereis of metabolic reations, only some enzymes are controled
feedback inhibition
Once sufficient F has been reached the inhibotors are signaled to bind to the allosteric enzyme in E1
can inhibit one pathway and stimulate another and immedietly stops one pathway
V0/(s) is what sigmoidal or hyperbolic with alosteric enzymes and why
it is sigmoidal, which tells that it doesnt shoot up in reletive velocity in low S (substrate concetration).
Alosteric enzymes are quaternary structures, meaning they have reglotory binding sites meaning some are blocked.
what are the models of function and what do they do (summary)
concerted model- everything happens at once
seqeuntial model - everything is done step by step
Concerted model and what are the steps
- enzynme exists to two quaternary structers where they go into t-state(tense or R-state (relaxed)
- R-state has more enzymitic activity than T-state
- T-state goes into R-state once enzyme is binded
- All activities must be completed at the same state
sequential model
- Rstate more enzamatically active than the T state
- T-state more stable but goes into R state when binding
- T and R-state are hybrid
- binding at one site changes all the other sites aswell
what stabilizes T and R states
Inhibitor stabilizes t-state - deoxiginated
Activitors stabilize the R-state- oxyginators
