Question

During an experimental workup you determine that k2 = 1200 s-1 . When you set [ET]...

During an experimental workup you determine that k2 = 1200 s-1 . When you set [ET] = 10 nM and [S] = 40 μM, you observe Vo progressing at 9.6 μM s-1 . For this reaction, what is KM?

0 0
Add a comment Improve this question Transcribed image text
Answer #1

Solution Given ) K = 12006-1 [ET] = 10nM [s] - 40nM Vo = 9.6uM5 To find kmi Firest of all we need to find max. max = K₂ [ET]the enzymatic reaction related formulas have been used to solve the above question.

Add a comment
Know the answer?
Add Answer to:
During an experimental workup you determine that k2 = 1200 s-1 . When you set [ET]...
Your Answer:

Post as a guest

Your Name:

What's your source?

Earn Coins

Coins can be redeemed for fabulous gifts.

Not the answer you're looking for? Ask your own homework help question. Our experts will answer your question WITHIN MINUTES for Free.
Similar Homework Help Questions
  • During an experimental workup you determine that k2 = 1200 s-1 . When you set [ET]...

    During an experimental workup you determine that k2 = 1200 s-1 . When you set [ET] = 10 nM and [S] = 40 μM, you observe Vo progressing at 9.6 μM s-1 . For this reaction, what is KM?

  • Can someone help me walk through this problem step by step please! Am i going to use V= Kcat/Km [S] [Et] ??? Help me sol...

    Can someone help me walk through this problem step by step please! Am i going to use V= Kcat/Km [S] [Et] ??? Help me solve it step by step Consider the following enzymatic reaction: SP The enzyme has a kcat of 600 s-1. When [Et]=20 nM and [S]=40 uM, the reaction velocity is 9.6 uM/s-1. What is the Km for this enzyme?

  • D-Lactose is the substrate for B-galactosidase. Given Vo = kcat [Et] [S]/km + [S], calculate [S],...

    D-Lactose is the substrate for B-galactosidase. Given Vo = kcat [Et] [S]/km + [S], calculate [S], when Km = 4.0 nM, V. = 10.5 M s', kcat = 500 s, and [Et] = 40 uM Calculate the catalytic efficiency. Below is a double-reciprocal plot for an enzyme reaction in the absence and presence of of inhibitor. Give the equation for the line. Calculate Vmax and Km for the enzyme and enzyme plus inhibitor. Which type of inhibition is apparent. 0.10...

  • 1. Show, using the Michaelis-Menten equation, that when [S] >>> Km, vo = Vmax. Show, using...

    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?

  • 10.What type of inhibitor is this? How do you know? (2) 11.For your assigned inhibitor 1,...

    10.What type of inhibitor is this? How do you know? (2) 11.For your assigned inhibitor 1, what are the apparent Km & Vmax? (NOTE: apparent Km& Vmax are just the Km & Vmax in presence of inhibitor, at a given concentration.) (2) Kinetics experiments were performed on PGI. Enzyme activity (initial velocity, Vo) was measured at varying concentrations of Glucose-6-phosphate (G6P). The enzyme concentration used in all experiments was 1.5 μM. 12.What will be the reaction rate with 0.500 mM...

  • Question 1 (2 points, 1 point for each correct answer) A research group discovered a new...

    Question 1 (2 points, 1 point for each correct answer) A research group discovered a new enzyme happyase that catalyzes chemical reaction SAD STUDENT HAPPY STUDENT Researchers characterized this enzyme and found that at [E,-10 nM this enzyme has Vmax at 2.5 μM/s. It was also experimentally measured that at [SAD STUDENT)-0.05 mM this enzyme has Vo -500 nM/s. What are the kat and Km of the happyase enzyme? Make sure to write down units of measure! Answers: keat- Question...

  • A Rī thermistor whose temperature coefficient is a = -0.02 per degree ( with a=(1/RI)dR,/dt et...

    A Rī thermistor whose temperature coefficient is a = -0.02 per degree ( with a=(1/RI)dR,/dt et R1 = 5.2 K2 at 20°C ) is placed in the circuit of the following figure, circuit comprising an ideal OP-AMP supplied with + 10 V. Vo L R2 I vol TTT TT TIL 1) What is the output s of the circuit at 20 ° C worth? 2) Determine the RT expression used to toggle the output of the circuit. 3) What is...

  • For her undergraduate project, Jessica studied an enzyme that catalyzes the reaction A↽−−⇀B. For substrate A,...

    For her undergraduate project, Jessica studied an enzyme that catalyzes the reaction A↽−−⇀B. For substrate A, she determined that ?m=2.5 μM and ?cat=35 min−1. Jessica graduated and her project has been passed on to you. Unfortunately, Jessica was so busy that she sometimes forgot to record all of the details of an assay in her lab notebook. Your mentor suggests that you try to back calculate some of the missing concentration values. Assume that the enzyme follows Michaelis–Menten kinetics. 1)...

  • To determine the kinetic characteristics of an enzyme you used 1 nmol/L of enzyme in a...

    To determine the kinetic characteristics of an enzyme you used 1 nmol/L of enzyme in a series of assays where you measured the rate of reactions as you varied the concentration of substrate in each assay (Table A). Estimate from a Michaelis-Menten plot approximate values for Vmax, KM, Kcat, and the specificity constant for this enzyme and substrate. (The only information that is given is this paragraph and the table below). Table 1: [S] (μM) v (μmol/L/min) 0 0 5...

ADVERTISEMENT
Free Homework Help App
Download From Google Play
Scan Your Homework
to Get Instant Free Answers
Need Online Homework Help?
Ask a Question
Get Answers For Free
Most questions answered within 3 hours.
ADVERTISEMENT
ADVERTISEMENT
ADVERTISEMENT