Enzyme kinetics

Question 1

Enzymes

Answer 1

Proteins that stabilise the transition state of reaction intermediates thus decreasing activation energy = increases reaction rate. Affected by anything that alters its structure. Highly specific. Does not effect equilibrium.

Question 2

Oxidoreductases

Answer 2

1. transfer electrons (H atoms)

Question 3

Transferases

Answer 3

2. Group transfer of electrons

Question 4

Hydrolases

Answer 4

3. Hydrolysis reactions (transfer of functional groups to water)

Question 5

Lyases

Answer 5

4. Addition of groups to double bonds or formation of double bones by group removal.

Question 6

Isomerase

Answer 6

5. Transfer of groups within molecules to yield isomeric forms

Question 7

Ligases

Answer 7

6. formation or c-c c-s c-o c-n bonds by condensation reactions coupled to ATP cleavage.

Question 8

Allosteric regulation

Answer 8

Allosteric enzyme regulation occurs when binding of a ligand molecule (activator/repressor) at an allosteric site changes the shape of the enzyme.

Question 9

Allosteric regulator

Answer 9

Molecule that competes with the substrate for the active site.

Question 10

0th order

Answer 10

Rate = k (independent of [substrate] ) Ms-1

Question 11

1st order A—> product

Answer 11

Rate = k[s] (proportional to first power of [substrate] ) s-1

Question 12

2nd order A+B —> product

Answer 12

Rate = k[s1][s2] (proportional to first power of each reactants) M-1 s-1