1. what is the Vmax of the
enzyme described in the equation?
2. what is the Km of the enzyme described in the equation?
Please rate high.
1. what is the Vmax of the enzyme described in the equation? 2. what is the...
The kinetics of enzyme catalyzed reactions can be described the Michaelis-Menten equation and the Eadie-Hofstee equation as shown below: V0 = (-Km) V0 / [S] + Vmax a). Please derive the Eadie-Hofstee equation starting from the Michaelis-Menten equation. b). The Vmax and Km of the enzyme catalyzed reaction can be derived from a plot of V0 versus V0/[S]. Please draw one of these plots and explain how do you use it to derive Vmax and Km. c). Please draw a...
- Vmax is a kinetic property associated with an enzyme. Describe what occurs when an enzyme reaches its Vmax. - Km is also another intrinsic property of an enzyme. Practically, what does the Km tell about how an enzyme interacts with its substrate?
1. Show, using the Michaelis-Menten equation, that when [S] >>> Km, vo = Vmax. Show, using the M-M equation that when [S] <<<Km, vo =[S][Et]kcat/Km. 2. What is Vmax? Provide both a mathematical and written description of Vmax? How can Vmax be experimentally altered? How can we use Vmax to determine the turnover number (kcat) of an enzyme-catalyzed reaction? What is the major challenge of determining Vmax from an Michaelis-Menten plot?
b. For an enzyme that displays Michaelis-Menten kinetics, what is the initial velocity as a function of Vmax when: a. [S] Km b. S] 0.1 Km c. [S] 50Km c. What will be the initial velocity (yo) for an enzyme that has Km 2.5 [S]? Your answer will be a fraction of Vmax a.
16. At right is a graph obtained from a series of enzyme kinetics assays. The Vmax for this enzyme and substrate is 4.5 uM/s. 5 4.5 4 a) What is the KM? KM: v. (mM/s) 3.5 3 2.5 2 1.5 1 0.5 b) If a pure non-competitive inhibitor was added to the assays, what would the resulting kinetics curve be like? Give a Km and Vmax in the presence of the inhibitor (write them below) and draw an appropriate curve...
1. an enzyme is observed to approach an initial velocity of
0.1M/s as more and more [S] is added to the reaction. additionally
when V0 is equal to 0.05 M/s [S] is equal to 0.6 M. based on this
information what is Vmax and Km?
2. If a psrticular enzyme has a Vmax of 0.4 M/s, and a Km of
20 mM, what is V0 wjen [S] = 0.8 M?
3. We have discussed which amino acids chymotrypsin cleaves
at,...
The next 3 questions are related. The results of an enzyme analysis are: KM=1.1x10-5 M; VMAX=47.6 μM/min. What is the Lineweaver Burk plot equation (recall: y=1/Keq and x=1/[S])?
2.) a. Given the following equation and using the Lineweaver-Burk equation find the Vmax and Km O y=7x+2.5 for enzyme A (in mM and s). b. Suppose you want to compare similar enzymes A (above Kcat=500) with enzyme B (Km=2.0, Kcat=450) to find out which enzyme has a higher catalytic efficiency; which enzyme has the higher catalytic efficiency?
21. For the L-8 graph below, what is the Km and Vmax for this enzyme? ◆ Series! Linear (Series1) y=1229·4x + 2.9701 ﹁ -0.005 0.005 L-DOPA]
16. At right is a graph obtained from a series of enzyme kinetics assays. The Vmax for this enzyme and substrate is 4.5 uM/s. a) What is the KM? 5 4.5 4 3.5 3 2.5 2 KM: 3mm V. (mM/s) 1.5 1 b) If a pure non-competitive inhibitor was added to the assays, what would the resulting kinetics curve be like? Give a Km and Vmax in the presence of the inhibitor (write them below) and draw an appropriate curve...