enzymes

Question 1

what is competitive inhibition?

Answer 1

inhibitors compete with the substrate for the active site of an enzyme

Question 2

non-competitive inhibition:

Answer 2

inhibitor binds to allosteric site of enzyme and modifies the active site so that the substrate cannot bind.

Question 3

increased KM?

Answer 3

worst substrate binding by active site of enzymes

Question 4

decreased KM?

Answer 4

better substrate binding by active site of enzymes

Question 5

what happens to the KM and Vmax in competitive inhibition?

Answer 5

KM increases and Vmax stays the same

Question 6

what happens to KM in non-competitive inhibition?

Answer 6

KM stays the same and Vmax decreases

Question 7

what is Vmax?

Answer 7

maximum reaction velocity

Question 8

small KM?

Answer 8

only need a little bit of substrate because enzyme function/ ability is high

Question 9

large KM?

Answer 9

need many substrates for reaction progression because enzymes availability/function is low

Question 10

catalyst:

Answer 10

lower activation energy to speed up reactions

Question 11

activation energy:

Answer 11

amount of energy a chemical reaction requires to progress

Question 12

most enzymes are:

Answer 12

proteins

Question 13

enzymes specificity constant:

Answer 13

measures how efficient an enzyme is in converting substrate to product

Question 14

high specificity constant:

Answer 14

enzyme’s active site will have high affinity and enzyme is highly efficient.

Question 15

induced fit theory:

Answer 15

enzymes active site changes shape slightly when substrate binds. allows for a better and tighter fit of substrate.