2.4 lecture Flashcards

1
Q

What do enzymes do?

A

-They act as catalysts and lower activation energy
-equilibrium is reached faster

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
2
Q

What don’t enzymes do?

A

-does not change equilibrium points for reactions
-does not shift equilibrium toward more product

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
3
Q

Mechanisms enzymes use to lower activation energy?

A

1.catalytically active groups (polar/charged)
2.properly aligning groups
3.more weak intermolecular reactions are formed between enzyme and transition state

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
4
Q

Proteases

A

Cleave peptide bonds in the backbone of proteins

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
5
Q

Chymotrypsin structure

A
  • 2 anti parallel beta barrel domains that sandwich together
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
6
Q

What are the structural requirements for chymotrypsin activity

A
  1. catalytic triad
  2. oxyanion hole
  3. substrate binding pocket
  4. specificity pocket
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
7
Q

catalytic triad

A
  1. Serine (Ser)
  2. Histidine (His)
  3. Aspartate (Asp)
How well did you know this?
1
Not at all
2
3
4
5
Perfectly
8
Q

Serine 95: catalytic triad

A

forms alkoxide ion that acts as a nucleophile and covalently bonds w/ the substrate

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
9
Q

Histidine 57: catalytic triad

A

acts as a general base to ionize the serine side chain and turns it into nucleophilic alkoxide

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
10
Q

Aspartate 102: catalytic triad

A

Stabilizes the positively charged histidine

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
11
Q

Oxyanion hole

A

formation of tetrahedral state

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
12
Q

Substrate binding pocket

A

binds peptide chains regardless of amino acid content

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
13
Q

Specificity pocket: Chymotrypsin

A

cuts after a bulky residue (F,Y,W)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
14
Q

Specificity pocket: Trypsin

A

cuts after a positively charged residue (K, R)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
15
Q

Specificity pocket: Elastase

A

cuts after small hydrophobic amino acids (A, V, G)

How well did you know this?
1
Not at all
2
3
4
5
Perfectly
16
Q

Transition state

A

Transient and unstable

17
Q

Characteristics of enzyme inhibitors that are drugs

A
  1. they are substrate/transition state mimics
  2. They are more stable than the transition state
  3. They block the enzyme activity site
18
Q

Ornithine decarboxylase

A

-produce polyamines
-anti-trypanosome drugs

19
Q

Where does HIV protease cut?

A

between F and P

20
Q

Protease inhibitors from plants

A

PIN I and PIN II
-inhibits serine proteinases