Chapter 8: Mechanisms and Inhibitors (Test 2) Flashcards
1
Q
- Chymotrypsin is has best specificity with
A
- Phenylalanine
- Tryptopan
- Tyrosin
2
Q
What is required for chymotrypsin activity?
A
- Serine 195
3
Q
What is chymotrypsin?
A
- A proteolytic enzyme that hydrolyzes peptide bonds selectively on the carboxyl side of large hydrophobic amino acids?
4
Q
Which organ secretes chymotrypsin?
A
- The pancreas
5
Q
What is diisopropylphosphofluoridate (DIFP)?
A
- The group-specific reagent that modifies only serine 195, one of 28 serine residues in chymotrypsin, and inhibits the enzyme
6
Q
What is a chromogenic substrate for chymotrypsin?
A
- N-Acetyl-L-phenylalanine p-nitrophenyl (ester)
7
Q
What comprises the catalytic triad that includes serine?
A
- Serine
- Histidine
- Aspartic Acid
8
Q
What are common catalytic strategies?
A
- Covalent catalysis
- General acid-base catalysis
- Metal ion catalysis
- Catalysis by approximation and orientation
9
Q
What is covalent catalysis?
A
- The active site contains a nucleophile that is briefly covalently modified
10
Q
What is general acid-base catalysis?
A
- A molecule other than water donates or accepts a proton
11
Q
What is metal ion catalysis?
A
- Metal ions function in a number of ways including serving as an electrophilic catalyst
12
Q
What is catalysis by approximation and orientation?
A
- The enzyme brings two substrates together in an orientation that facilitates catalysis
13
Q
What are the three common types of reversible inhibition?
A
- Competitive inhibition
- Uncompetitive inhibition
- Noncompetitive inhibition
14
Q
What is competitive inhibition?
A
- The inhibitor is structurally similar to the substrate and can bind to the active site, preventing the actual substrate from binding
- Can be overcome with a high concentration of substrate
- Vmax is unchanged, but Km is increased
15
Q
What is uncompetitive inhibition?
A
- The inhibitor binds only to the-substrate complex
- Vmax and Km are decreased
- Cannot be overcome
16
Q
What is noncompetitive inhibition?
A
- The inhibitor binds either the enzyme or the enzyme-substrate complex
- Vmax is decreases, Km is unchanged
- Cannot be overcome