Interpret clearly and explain the information presented in this graph
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Interpret clearly and explain the information presented in this graph
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- A hypothetical enzyme that follows Michaelis-Menten kinetics functions has a substrate concentration 50mM at 50% of Vmax. Find the substrate concentration when the velocity of reaction is equal to 75% of Vmax.Define the following terms:a. catalystb. transition statec. substrated. activation energye. active site2. Define the follWhen substrate [S] = Km, the velocity of an enzyme catalyzed reaction is about: * 0.1 Vmax. 0.2 Vmax. 0.5 Vmax. 0.9 Vmax
- Consider the enzyme, ATCase. All are true except: It's K effectors are ATP and CTP It is a K system enzyme. Plots of V versus [S] are sigmoidal Plots of 1/V versus 1/[S] are sigmoidal.Pls help ASAP, thank you! "Regulation of metabolic pathways most typically occurs at enzyme steps that are"An enzyme-catalyzed reaction has a Km of 4 mM and a Vmax of 5x10-3 uM/s. What is the reaction velocity when the substrate concentration is: 5 mM 4 mM
- If an enzyme catalyzed reaction has a KM of 5mM and a Vmax of 60 nm/sec, the substrate concentration at 30 nM/sec is? Thank you.Another member of your research group studied the kinetics of theGAPDH from the organism. They also determined if the GAPDH fromthe organism is also inhibited by the known inhibitor of GAPDH fromhumans. From the following data, determine the KM (Michaelis-Menten Constant) and the Vmax(maximum velocity) of the enzyme without and with the inhibitor.An enzymatic reaction follows M-M kinetics with Vmax= 2.5 mol m-3s-1and Km = 5 mM.Calculate the time required for 50% conversion of the substrate in a batch reactor if theinitial substrate concentration is0.2 M.Show your calculation steps.
- Velocity (mmol/minute) [S], (mM) No inhibitor Inhibitor 3 10.4 4.1 5 14.5 6.4 10 22.5 11.3 30 33.8 22.6 90 40.5 33.8 The kinetics of an enzyme are measured as a function of substrate in the presence and the in absence of 2mM inhibitor (I). What are the values of Vmax and KM in the absence of inhibitor? In its presence? In its presence? What is the type of inhibition?Here’s a kinetic model for some enzyme E acting on substrate S. The last step (EP → E) is rate determining. Write an equation for the rate of the reaction. And write an equation for the total amount of enzyme in this system.The equil ibrium constant for the attachment of a substrate to the active site of an enzyme was measured as 200.In a separate experiment, the rate constant for the secondorder attachment was found to be 1.5 x 108 dm3 mol-1 s- 1.What is the rate constant for the loss of the unreacted substrate from the active site?