Biochem - Enzyme and Kinetics [1] Flashcards
(30 cards)
1
Q
- A competitive inhibitor of an enzyme is usually
A
- Structurally similar to the substrate
2
Q
- Linear inhibition is sometimes called as
A
- Partial inhibition
3
Q
- The types of inhibition pattern based on Michaelis Menten equation are
A
- All of the above
4
Q
- The effect of non-competitive inhibition on a Lineweaver-Burk Plot is that
A
- It can change the y-intercept
5
Q
- The rate-determining step of Michaelis Menten kinetics is
A
- The complex dissociation step to produce product
6
Q
- In competitive inhibition a factor is obtained from the measurement of
A
- KMKM
7
Q
- Which of these proteases is not a cysteine active site protease?
A
- Cathepsin D
8
Q
- Given an enzyme with aKm=10 mMKm=10mMandVmax=100 mmol/minVmax=100mmol/min. If [S] = 100 m M, which of the following will be true?
A
- A 10-fold increase in Vmax would increase velocity 10-fold
9
Q
- The conformational change in an enzyme after the substrate is bound that allows the chemical reaction to proceed, can be explained by
A
- Induced fit
10
Q
- The active site of an enzyme remains
A
- At the center of globular proteins
11
Q
- Which category of enzymes belongs to class two in the international classification?
A
- Ligases
12
Q
- The Woolf-Augusteinsson-Hofstee plot of v versus v[S] and the Eadie-Scatchard plot of v[S] versus v do not involve reciprocals of v therefore are considered to be more reliable when the error in v is
A
- Significant
13
Q
- The relationship betweenKeq,KmKeq,KmandVmaxVmaxis known as
A
- Haldane equation
14
Q
- The reciprocal equation for non-competitive inhibition can be arranged to the equation for the
A
- Dixon plot
15
Q
- Which of the following statements is true for enzymatically catalyzed reaction?
A
- The activation energy of the reaction is lowered so that a larger proportion of the substrate qualifies to overcome it
16
Q
- Which of the following common drugs is not a specific enzyme inhibitor?
A
- Iodine
17
Q
- The enzyme inhibition can occur by
A
- Both (a) and (b)
18
Q
- In a Lineweaver-Burk Plot, competitive inhibitor shows which of the following effect?
A
- It has no effect on the slope
19
Q
- Which of the following statements is not true?
A
- Enzymes only function when they are in intact cells
20
Q
- Non-competitive inhibitor of an enzyme catalyzed reaction
A
- Decreases Vmax
21
Q
- An enzyme and a reactant molecule maintain relationship as
A
- A temporary association
22
Q
- An enzyme is assayed at an initial substrate concentration of 2 x 10-5M. In 6-minute, half of the substrate is used. The Km for the substrate is 2 x 10-3M. The value of k in minute is
A
- 0.115
23
Q
- The plot commonly used for determining the value of Vmax is
A
- Lineweaver Burk plot
24
Q
- Quasi steady state is also known as
A
- Briggs-Haldane approach
25
25. Which of these enzymes contains a Zinc (Zn) ion?
25. Carboxypeptidase A
26
26. A noncompetitive inhibitor of an enzyme-catalyzed reaction
26. Increases KMKM and reduces VmaxVmax
27
27. An allosteric inhibitor of an enzyme usually
27. Participates in feedback regulation
28
28. Which of the following activity is possible by transferases?
28. Transfer of methyl groups
29
29. A classical uncompetitive inhibitor is a compound that binds
29. Reversibly to the enzyme substrate complex yielding an inactive ESI complex
30
30. Which graphical method is used to determine an enzyme degree of cooperativity?
30. Hill plot
