Add Structures for your Answers &&& Write one controlling rate limiting enzyme from any pathway or cycle and clarify the following: a- The whole reaction b- The exact mechanism
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- 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.1a-Enzymes serve as catalysts for chemical reactions. What does this mean? Select all that apply. Select one or more: a. Enzymes make reactions more likely to occur. b. Enzymes increase the activation energy. c. Enzymes decrease the free energy (?G) of a reactio d. Enzymes increase the free energy (?G) of a reaction. 1b-When ATP is hydrolysed: Select one: a. The energy will be released as heat if the reaction is not coupled to a substrate, b. The potential energy associated with the resulting ADP molecule increases. c. The terminal phosphate is transferred to a substrate, lowering the potential energy of the substrate d. Water is formed and released as a reaction product.The Michaelis‑Menten equation models the hyperbolic relationship between [S] and the initial reaction rate ?0V0 for an enzyme‑catalyzed, single‑substrate reaction E+S↽−−⇀ES⟶E+PE+S↽−−⇀ES⟶E+P. The model can be more readily understood when comparing three conditions: [S]<<?m[S]<<Km, [S]=?m[S]=Km, and [S]>>?m[S]>>Km. Match each statement with the condition that it describes. Note that "rate" refers to initial velocity ?0V0 where steady state conditions are assumed. [Etotal][Etotal] refers to the total enzyme concentration and [Efree][Efree] refers to the concentration of free enzyme.
- a. What is the Vmax of this enzyme WITHOUT inhibitor? Please show your work. b. What is the Km of this enzyme WITHOUT inhibitor? Please show your work. c. The specificity constant of enzyme X is 8 x 10^7 /(M * seconds) What is the kcat of enzyme X WITHOUT inhibitor? Please show your work d. What was the concentration of enzyme used for measuring the kinetics of enzyme X WITHOUT inhibitor? Please show your workCan Please Help Me: Bio- Chemistry 60 minutes only the given time. Wish you could help me. I will give UPVOTE and GOOD FEEDBACK. QUESTION/// Suppose two enzymes in different reaction pathways have the same substrate but have different level of affinities to it. At low [S], how will you differentiate the activities of the 2 enzymes? ///QUESTIONDESIGN YOUR ENZYME AND SHOW THE REACTION! To trap glucose in a cell, the following reaction is catalyzed by the HEXOKINASE enzyme: GLUCOSE (G) + ATP -> GLUCOSE-6-Phosphate (G6P) + ADP Diagram and label the steps in the catalytic cycle of this reaction in the presence of the hexokinase enzyme. Show the steps of how the REACTANTS are converted to PRODUCTS (you can use shapes to represent the different molecules) From what you know about the structure and polarity of the reactants, predict the amino acid R groups that might be in the ACTIVE SITE
- How can you find Kcat if you are only given Vmax, Km and [E] ? I tried using Kcat=Vmax/[E] but that didn't work. How do you know if [E] is the same as [E]total, and if it isn't how do you find it from this information: The Vmax for a particular enzyme is 10 nmols/L/s. The Km for its substrate is 5 microM. If the enzyme concentration is 10 nM, what is the kcat? a.80 nmoles/L/s b.8000 nmoles/L/s c.2 nmoles/L/s d.50 nmoles/L/s1B. please help me in detail. Draw a graph of free energy G (y-axis) vs reaction progress (x-axis) that illustrates what the kinase is doing in terms of the free energy by showing (i) the substrate (also label what the substrate is [it’s name]), (ii) the products (also give the name of the products), (iii) draw and label the uncatalyzed and catalyzed reactions, and be sure that the parts of the graph are properly labeled..NO AI GENERATED RESPONSE I NEED EXPERTS!! using results for experiment below conduct 1 graph of the different factors vs rate of enzyme activity. * *NO FUNNEL GRAPHS ACTUAL GRAPH WITH GOOD TITLE , AND MAKE SURE IT LOOKS LIKE THE IMAGE I PLACED BELOW** important info: experiment procedure: The experiment began by preparing a hot water bath by boiling water and an ice water bath using ice in a 400 mL beaker. In the control group, 2 mL of 3% H2O2 was placed in a test tube and a pinch of MnO2 was added. The rate of this reaction was assigned as 5, and the production of bubbles in millimeters (mm) was noted. The reaction was considered complete when no more bubbles were produced. Another control group was set up by placing 2 mL of 3% H2O2 in a test tube and adding a pinch of sand, with the rate of reaction assigned as 0. To investigate the difference between plant and animal catalase, 2 mL of H2O2 was added to a test tube and a small piece of fresh liver was added. The rate of…
- Can Please Help Me: Bio- Chemistry 60 minutes only the given time. Wish you could help me. I will give UPVOTE and GOOD FEEDBACK. QUESTION/// Suppose two enzymes in different reaction pathways have the same substrate but have different level of affinities to it. At low [S], what will happen to the 2 reaction pathways? ///QUESTIONIt's a three part question based on the chart provided asking: a) Which of these enzymes has the weakest binding of substrate? (I chose fumarase since it has lowest Km but that was wrong so I don't understand) b) Which enzyme has the fastest conversion of ES? (I would assume this means highest Kcat value, so should be catalase) c) Which enzyme is most closely catalytically perfect? (I'm assuming this means highest Kcat/Km ratio, so I was thinking Crotonase, although I don't know what classifies an enzymes as 'catalytically perfect', please explain)an enzyme acts on a substrate X. The enzyme exists in four different forms, with different catalytic efficiencies. The table shows the kcatand KM values for each form of the enzyme. If the concentration of substrate X in a solution is 5 µM, which of the four forms of the enzyme is the most efficient? Form of Enzyme kcat (s-1) KM (µM) A 50 10 B 50 1 C 100 4 D 1000 100 a. Form A b. Form B c. Form D d. Form C