Question

1. Decribe the structure, function, and location of ATP synthase.

2. Explain why emzyme function is usually explained as a "lock and key" model. Then explain why this model is outdated/ inccorect.

3. compare and contrast an allosteric inhibitor and an allosteric activator.

Answer 1

ANSWER NO...1

It is located within the thylakoid membrane and the inner mitochondrial membrane, ATP synthase consists of two parts FO and F1.

It is made of c-ring and subunits a, two b, F6. F1 is made of α, β, γ, δ subunits.

Function of ATP synthase is it synthesize ATP from addition of ADP and inorganic phosphate (Pi) in the F1 part. This is possible due to a gradient of protons which cross the inner mitochondrial membrane from the intermembrane space into the matrix through the Fo portion of the enzyme.

ANSWER NO..

LOCK& KEY MECHANISM:-

*Given by Emil Fischer(1894)

According to this model both enzyme and substrate have specific shapes.

The shape of active site of enzyme is in such a way that it fit in the substrate

Compounds similar to substrate in inhabit enzyme activity, this supports template model .

This model explain the specificity of enzyme action lock and key model of enzyme action represent that a particular enzyme molecule interact with specific type of substrate molecule.

ANSWER NO..3

Allosteric inhibitors change the active site of the enzyme so that substrate binding capacity is reduced or prevented.

Allosteric activators modified the active site of the enzyme so that the affinity for the substrate increases. And enzymatic activity increases seceral fold.