Given below are five Km values for the binding of substrates to a particular enzyme. Which substrate ?has the strongest affinity to the enzyme
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Q: What is the impact of the lower value km 0.01 on the affinity of enzyme for substrate?
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Q: A plot of 1/Vo versus 1/[S], called Lineweaver-Burk or double-reciprocal plot, is a useful tool for…
A: Lineweaver-Burk plot is also known as the double reciprocal plot. Plot between the reciprocal of…
Q: What is the impact of the lower value Vmax on the affinity for enzyme for substrate? And what is…
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Q: 1² L-^ 0.1 + ||| -4-2 |||| 24 [S]-1, (mM-1) 1, The value of Km for the enzyme depicted by curve A is…
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Q: Vo with Vo without [Substrate, µM] DEDS DEDS (µM/min) (µM/min) 3.333 0.774 1.196
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Q: Under what circumstances may we believe that KM represents the substrate-enzyme binding affinity?
A: Enzymes are proteins that produce a substrate-enzyme complex by binding to the substrate. The…
Q: When is it reasonable to suppose that KM reflects the substrate-enzyme binding affinity?
A: According to Michaelis-Menten Kinetics, when the rate or velocity of an enzyme catalyzed reaction…
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A: Note : Hi ! Thank you for the question. We are authorized to answer one question at a time. Since…
Q: Consider the Michaelis-Menten equation, below: Vmar S V. k + [S] %3D What is the relationship…
A: [S] : Substrate concentration V= Vmax[S]/(Km+[S]) Vmax: Maximum velocity Km: [S] at which V is…
Q: Uncompetitive Mixed +Inh +Inh AInh Tnh Anh Anh [S] [S] a. How does the value of Vmax for the enzyme…
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Q: The accompanying figure shows three Lineweaver–Burk plots for enzymereactions that have been carried…
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Q: If the higher value of KM resulting in the new plot ( red curb ) is due to the presence of an enzyme…
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Q: The following data were collected in the study of a new enzyme and an inhibitor of the new enzyme:
A: The Michaelis–Menten equation is the rate equation for a one-substrate enzyme-catalyzed reaction.…
Q: What is the impact of the higher value of Km on the affinity of the enzyme for the substrate?
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A: Introduction Km gives the relative measure of the affinity of a substrate for an enzyme or how…
Q: Consider this intermediate in the derivation of the Michaelis-Menten equation. [E] [S] k-1 + k2 [ES|…
A: Km : The concentration of substrate at which enzyme achieves half Vmax-maximum velocity
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- The table presents the rates of reaction at specific substrateconcentrations for an enzyme that displays classicalMichaelis-Menten kinetics. Two sets of inhibitor data arealso included. Determine the Km and Vmax for the uninhibitedenzyme.Also please explain why you chose the column based on the column and the protein propertiesPepsin, a peptidase that hydrolyzes proteins, functions in the stomach at an optimum pH of 1.5–2.0. How is the rate of a pepsin-catalyzed reaction affected by each of thefollowing conditions? increasing the concentration ofproteins changing the pH to0 running the reaction at 0°C using lesspepsin
- The following data were obtained in a study of an enzyme that is known to follow the Michaelis-Menten kinetics. Approximately, what is the value of Km tor this enzyme? Substrate added, umol/L Vo uM/sec 48 97 175 187 192 197 2 16 100 1000 198 OA 1 uM O8.2 pM OC 4 uM. OD. 8 uM OE 16 IM OF 1000 uM OG 97 uM/sec OH 175 UM/secUnder what conditions does Km represent the true binding affinity (i.e. Kd) of the substrate to the enzyme? 1. when kcat << k-1 2. when k-1 >> k1 3. when k1 >> kcat 4. when k1 = k-1An enzymatic reaction with KM = 4.4 x 10-5 M, is carried out in 400 μL of of solution containing 0.20 nmoles of enzyme. It is observed that Vmax = 6.6 x 10-3 M/s. What is the kcat value for the enzyme? (HINT: Keep an eye on the units)!!! a. 1.50 x 102 s-1 b. 7.56 x 10-5 min-1 c. 1.32 x 104 s-1 d. 3.3 x 106 s-1
- 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.Carbonic anhydrase catalyzes the hydration of CO. CO2 + H2O ¬ H½CO3 The Km of this enzyme for CO, is 1.20×104 µ.M. When [CO,] = 3.60×104 µM, the rate of reaction was 4.50 umol·mL! sec-1 a What is Vmax for this enzyme? umol·mL-!sec-!you are trying to come up with a drug to inhibit the activity of an enzyme thuogth to have a role in a liver disease. in the lab the enzyme was shown to have a Km of 1x10-6 M and Vmax of 0.1 micromoles/min.mg measruing at room temperature. you developed a mixed non-competitve inhibitor with a ki=0.4x10-6M and a Ki` pf 0/2 x 10-5 What will be the apparent Km in the presence of 1.0x10-6 M?
- 1)Catalase a. Is catalase activity endothermic or exothermic? b. What classification of enzyme is catalase? c. Give the Enzyme Commission (E.C.) number of catalase. d. Is catalase reusable? answer all and don't copy from other sources I will downvote for sureThis is a visible spectra between 390-590 nm obtained during the protein separation process of haemoglobin and cytochrome c using CM Sephadex chromatography. I'd like the results shown on the image interpreted. Look for characteristic peaks or patterns that correspond to the absorption properties of these proteins in the visible range.Consider the Michaelis-Menten enzymes below and answer the following questions. Kcat (s') 9.5*105 1.4*10* 2.5*102 1.0*107 5.0*10 8.0*10² Enzyme Km (M) A В a. Which enzyme has the highest affinity substrate? How do you know? b. Which enzyme can convert the most substrate to product in a given period of time? How do you know? c. Which enzyme has the highest catalytic efficiency? How do you know?