Biochem - Enzyme and Kinetics [1] Flashcards
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
Q
- Which of these enzymes contains a Zinc (Zn) ion?
A
- Carboxypeptidase A
26
Q
- A noncompetitive inhibitor of an enzyme-catalyzed reaction
A
- IncreasesKMKMand reducesVmaxVmax
27
Q
- An allosteric inhibitor of an enzyme usually
A
- Participates in feedback regulation
28
Q
- Which of the following activity is possible by transferases?
A
- Transfer of methyl groups
29
Q
- A classical uncompetitive inhibitor is a compound that binds
A
- Reversibly to the enzyme substrate complex yielding an inactive ESI complex
30
Q
- Which graphical method is used to determine an enzyme degree of cooperativity?
A
- Hill plot
