Enzymes

Question 1

Enzymes

Answer 1

Protein Catalysts. Catalyze reactions. VERY specific, will even choose enantiomers of a molecule.

Question 2

V= (Vmax[S])/(Km + [S]) and km= (s)

Answer 2

V= (Vmax)/2

Question 3

Higher Km

Answer 3

Lower substrate binding

Question 4

Lower Km

Answer 4

Higher Substrate binding

Question 5

Vmax

Answer 5

Completely saturated with substrate

Question 6

Competetive Inhibition

Answer 6

compete for active site. Needs more substrate to reach Vmax. Max DOESN’T change, but Km INCREASES.

Question 7

Noncompetetive Inhibition

Answer 7

Binding can happen, but processing cannot. Max decreases, Km doesn’t change.

Question 8

Cooperaive enzyme binding

Answer 8

Hemoglobin is good example.

Question 9

Bohr Effect

Answer 9

Want O2 to bind well but not so well that to doesn’t let go.

Question 10

Most common enzyme regulation

Answer 10

allosteric regulation and phosphorylation

Question 11

allosteric regulation

Answer 11

bind to some place on protein other than active site, changing it shape. Turns protein on/off.

Question 12

phosphorylation (covalent)

Answer 12

add phosphate group, change conformation, activate/deactivate protein. Phosphotase dephosphorylates it. Kinase phosphorylates it. Has to happen on OH group (Serine, Thrynine, Tyrosine). Makes covalent bond.

Question 13

Zymogens

Answer 13

pepsin/chymotrysin. Made as an active protein, undergoes protyolitic cleavage in certain environment so it only does what it’s suppose to do when it’s suppose to do it.

Question 14

Cofactors

Answer 14

metal ion concentrations. organic coenzymes.

Question 15

Association with other peptides

Answer 15

another enzyme regulation