Enzyme Activity (kinetics And Inhibition)

Question 1

What is a transition state?

Answer 1

The high energy intermediate between substrate and product.

Question 2

What 3 factors can increase rate of reaction?

Answer 2

Temp=increases amount molecules with activation energy
Conc=increase the chance of Collisions
Enzyme=lowers Ea, to facilitate formation of transition state

Question 3

Why are enzymes important in medicine?

Answer 3

Can relate to inherited genetic disorders
Overactive can cause disease
Can be measured in some diagnosis
Can be inhibited by drugs

Question 4

How is an active site formed?

Answer 4

Rest of enzyme provides scaffold for it.
AAs scattered in primary seq, but close together in 3D structure
Excludes H2O that may interfere with reaction

Question 5

What does the Michealis-Menten Equation do?

Answer 5

Predicts that V0 (rate) to (S) will form a hyperbolic curve.

Question 6

What does Vmax stand for?

Answer 6

The maximum rate that can be reached when all active sites contain a substrate molecule

Question 7

What does Km stand for?

Answer 7

The concentration of Substrate at half Vmax

Question 8

How can we use KM values in affinity?

Answer 8

Km gives an indication of an enzymes affinity for a substrate.
A low Km suggests high affinity
A high Km suggests low affinity

Question 9

What is a Lineweaver-Burk plot?

Answer 9

A linear version of the Micheal is-me ten equation.
Can be used to estimate Km and Vmax values
The further left the x intercept the higher the affinity (low Km)
The lower the Y intercept the higher the Vmax