Given the line-weaver Burke plot below for Enzyme Y, identify the Vmax for Enzyme Y. -10 30 1/v 1/[S] 5 10 Enter the numerical value for Vmax only, no letters or symbols. Round answer to 2 significant figures.
Q: In a reaction system, the concentrations of Enzyme-Substrate complex [ES], free enzyme [E] and free…
A: For a reversible reaction, the ratio of the product concentration to the reactant concentration at…
Q: Amino acids- Draw out the amino acid structure for one amino acid from the list of 20. Label all…
A: Amino acids are the building blocks of proteins that are made up of an amino group and a carboxylic…
Q: Suppose you prepared one additional tube of albumin unknown and got an absorbance value of 1.99.…
A: For protein estimation,A standard curve must be constructed before the concentration of an unknown…
Q: serine proteases act via a two-step catalytic mechanism. However, as a critical scientist, you may…
A: Serine proteases are protein cleaving enzymes that have Serine, Histidine and Aspartate (the…
Q: GQ5
A: The question is asking about the stage of cell division in which sister chromatids separate. Sister…
Q: 7. What is the driving force that promotes secondary structure formation of alpha helices and beta…
A: Two types of secondary structures are abundant in protein: alpha helix and beta sheets.The alpha…
Q: Question 3
A: The question is asking about the structure of DNA and what parts of the DNA strands are connected by…
Q: What is the purpose of adding hydroquinone? What is the purpose of washing the egg homogenate with…
A: Lipids are the important biomolecules which are soluble in fats and insoluble in water. Hence they…
Q: 48. The USP (United States Pharmacopoeia) has established a maximum limit of +3/ml eluate. i. 0.15…
A: The United States Pharmacopeia (USP) is a nonprofit organization that sets standards for the…
Q: Consider the malate dehydrogenase reaction from the citric acid cycle. Given the listed…
A: The free energy change for the malate dehydrogenase reaction of the TCA cycle is ≈21.122…
Q: Which of the following statements regarding Michaelis-Menten kinetics is TRUE? The ES complex can…
A: According to Michaelis Menten the MM) equation, the rate and velocity of enzyme catalyzed reaction…
Q: Genetics Question 16
A: The question is asking whether the number of chromosomes in the daughter cells produced at the end…
Q: If you transferred 15 mL of an undiluted sample into 35 mL of diluting fluid, what dilution have you…
A: Two similar expressions of the variation in concentration that occurs in a liquid material after…
Q: Question 3
A: The objective of the question is to determine the number of chromatids in fruit flies at the…
Q: Genetics Q5
A: The term 'semiconservative DNA replication' refers to the process by which DNA replicates itself.…
Q: Question 4
A: The objective of the question is to identify the origin of spindle growth during cell division.
Q: Tt O 8. What are the driving forces that promotes tertiary -3D and quaternary -4D structure…
A: Proteins are the biological macromolecules. They show great diversity in their structure and…
Q: Construct the two enantiomeric forms/structure of the following monosaccharides and designate the…
A: Monosaccharides are the simplest form of carbohydrates, often referred to as simple sugars. They…
Q: 16. A quantitative study of the interaction of a protein with its ligand yielded the following…
A: I cannot plot the graph as that would be doing your homework.Determine KD:From the graph, read the…
Q: Please describe what is a peptide bond? What is the significance of the amino terminus versus the…
A: Proteins are biomolecules which show great diversity in their structure and functions with Amino…
Q: 1. Draw an approximate titration curve of the following amino acid. Label the approximate…
A: The titration curve is a plot that tracks the behavior of amino acids under the influence of…
Q: Several general characteristics of metabolic reactions or reaction pathways are listed. Classify…
A: Metabolism is the sum total of all chemical reactions taking place in an organism. It can be…
Q: Question 1
A: The objective of the question is to match the descriptions of the Y chromosome during different…
Q: Cooperativity yields a sigmoidal kinetic curve. Which of the following is TRUE?
A: Co-operativity can be described as a phenomenon where the enzyme shape changes with the substrate…
Q: 24. Hexokinase catalyzes the phosphorylation of glucose from ATP, yielding glucose-6-P and ADP. The…
A: The objective of the question is to calculate the standard-state free energy change and equilibrium…
Q: What is the target for the following compound? O Muscarinic receptor O Acetylcholinesterase enzyme O…
A: Acetylcholine is a neurotransmitter. Many enzymes and proteins involved in the metabolism and…
Q: 1. ATP ACCOUNTING, Provide what is being asked for. Show all relevant calculations and summarize…
A: Fatty acids are organic compounds determined by a long hydrocarbon chain having a carboxylic group…
Q: Free energy diagrams are super fun to draw! Draw a set of free energy diagrams that show the…
A: Free energy diagrams have free energy (G) in Y-axis and reaction coordinate in X-axis. These can…
Q: Assume that an enzyme-catalyzed reaction follows the scheme shown: E + S ES E + P k₁ = 1 x 10%/M-s…
A: Michaelis Menten postulated that free enzyme reacts with the substrate reversibly to form an…
Q: Using the image provided, answer the two questions:- Based on their fat content, which is the…
A: The objective of the question is to determine the healthier option between Margarine A and Margarine…
Q: Describe the mechanism behind the hydrophobic effect. Support your description with one drawing.
A: The hydrophobic effect is the tendency of nonpolar molecules to aggregate in aqueous solutions. This…
Q: The Michaelis-Menten rate equation for reversible mixed inhibition is written as Vo = Vmax [S] aKm +…
A: Hence solved.Km=[S][αV0Vmax−1]Explanation:Determine the rate constant's expression, r.First, in…
Q: What is the major function of cholesterol esters? O Make cholesterol more hydrophobic so they can be…
A: Cholesterol esters are chemical compounds formed by the esterification of cholesterol molecules with…
Q: Question 5
A: The question is asking whether a mouse would die if it was injected with a mixture of heat-treated S…
Q: pindle The cell above is in a) Meiosis 2 b) Meiosis 1 c) Mitosis ****
A: Given cell is in metaphase stage. It is a mitosis cell division.
Q: The 4 kinase steps in glycolysis are catalyzed by hexokinase, phosphofructokinase, phosphoglycerate…
A: Glycolysis is a metabolic pathway, in which "Glucose" (six carbon sugar molecule) is broken down…
Q: imagine that you are running a sample on a TLC plate that is comprised of aspartate and isoleucine.…
A: The working principle of thin-layer chromatography is the same as column chromatography.A small…
Q: You are engineering a new vector that contains a screenable marker that can be used for blue/white…
A: Three important points to remember about the blue-white test: a special substrate is used which is…
Q: Genetics Question 17
A: The question is asking whether the number of sister chromatids in a cell at metaphase of meiosis 1…
Q: [AktivGrid] Draw the product of the reaction of isocitrate catalyzed by isocitrate dehydrogenase in…
A: Kreb cycleKreb cycle or citric acid cycle or tricarboxylic acid cycle (TCA) is a sequence of…
Q: (e) What kind of inhibitor is it likely to be? Plot the data in Lineweaver-Burk plot form to support…
A: For a one-substrate enzyme-catalyzed reaction, the Michaelis-Menton equation shows the quantitative…
Q: QUESTION 2 10 11 12 Glucose Pyruvic acid 2 ATP Lactic acid 13 36 ADP 36P 36 ATP Match the FOLLOWING:…
A: Answered the question.
Q: Write out each of the eight chemical reactions of the citric acid cycle. Draw the structures of the…
A: Citric acid cycle is also called as tricarboxylic acid cycle or Krebs cycle. This is the second…
Q: In a uni uni enzyme reaction, what is the substrate concentration relative to Km when an enzyme…
A: For a one-substrate enzyme-catalyzed reaction, the Michaelis-Menton equation shows the quantitative…
Q: Name the protein structural element shown in yellow in the figure:
A: Proteins can be defined as large biomolecules. They comprise of one or more chains of amino acids.…
Q: This is the three-letter code for the amino acid that is the most geometrically constricted amino…
A: Amino Acids are the organic compounds that combine to form proteins, hence they are referred to as…
Q: 111: 900 Page 3 (b) Construct an energy-level diagram of 2-pentene showing the relative energy…
A: Already done Explanation:Step 1: Step 2: Step 3: Step 4:
Q: Please draw out mechanism The formation of fructose 1, 6- biphophste from dihydroxyacetome phospahte…
A: Glycolysis:The metabolic process known as glycolysis, which in most organisms takes place in the…
Q: Which of these situations would produce a Hill plot with a Hill coefficient less than 1? A purified…
A: A Hill plot is used to establish the cooperativity of ligand binding to a protein.NH (Hill…
Q: Which of the sugars below are diastereomers of compound I? CHO H+ OH H-+OH H+OH CH₂OH I CHO H-OH…
A: Stereoisomers are the type of isomers in which the chemical formula of the molecules as well as the…
![Given the line-weaver Burke plot below for Enzyme Y, identify the Vmax for Enzyme Y.
-10
30
1/v
1/[S]
5
10
Enter the numerical value for Vmax only, no letters or symbols. Round answer to 2 significant figures.](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2F0929a000-131e-4378-97de-16d36c27aaaf%2F7bf32a84-8a05-476b-971f-ed71960d5f6a%2Fc2hfahl_processed.png&w=3840&q=75)
Step by step
Solved in 1 steps
- What is the medical diagnostic value associated with the presence of the following enzyme in the bloodstream? ALTIf 287.9 umol of enzyme X has a Vmax = 47.8 mmol/sec, what is the value of kcat %3D sec-1? Please report answer with 1 decimal place. Please do not report units. Your Answer: Answer units MacBook Air 888 F5 F4 F3 F2 %23 %24 %24If a data from an enzyme experiment is plotted as a Lineweaver - Burk plot, and the Vmax is 0.02 sec/mol, and x-intercept is -2.5 mM-1, then what is the KM value?
- An enzyme-catalyzed reaction has a KM of 20.0 mmol L-1 and Vmax of 17.0 pmol s-1. When a mixed inhibitor is added, the apparent KM is 50.0 mmol L-1 and the apparent Vmax is 5.20 pmol s-1. Calculate α.Please note the following Lineweaver-Burk plot for the enzyme Virbraniumase reacting with a substrate: -0.4 . 1/V 5 4 3 2 -0.2 0 0.2 y = 5.2781x + 1.3338 R² = 0.9967 0.4 0.6 0.8 1/[S] 1 Based on the information provided, what is the Vmax for this reaction?What is the likely keq for an enzyme that has a deltaG =-18.3kj/mol?
- During the early stages of an enzyme purification protocol, when cells have been lysed but cytosolic components have not been separated, the reaction velocity-versus-substrate concentration is sigmoidal. As you continue to purify the enzyme, the curve shifts to the right. Explain your results. This is an allosteric enzyme and you must use a Lineweaver-Burk plot to determine KM and Vmax correctly. This is an enzyme that displays Michaelis-Menten kinetics and you purify away an inhibitor. This is an allosteric enzyme and during purification you purify away an activator. This is an allosteric enzyme displaying a double-displacement mechanism and during purification you purify away one of the substrates: This is an enzyme that displays Michaelis-Menten kinetics, and you must use a Lineweaver-Burk plot to determine KM and Vmax correctly.Most of the enzyme reactions followed the mathematical kinetic plots suggested by Michaelis-Menten plots: Give the Michaelis-Menten equation of an enzyme reaction and draw the Michaelis-Menten plot of [S] versus V0.Although graphical methods are available for accurate determination of the Vmax and Km of an enzyme-catalyzed reaction, sometimes these quantities can be quickly estimated by inspecting values of V0 at increasing [S]. Estimate the Vmax and Km of the enzyme-catalyzed reaction for which the following data were obtained:
- A purified protein sample was used in a reaction, resulting in an activity of 696.7 nmol min-1. The reaction volume was 145.0 µL and the final volume before loading the plate was 1,050 µL. The total reaction time was 4.25 min. The amount of protein used in the reaction was 4.270 µg. Calculate the specific activity of the sample (in nmol min-1 µg-1).A biochemist is trying to determine the type of proteases they have isolated from walrus blubber. The three proteases and their relative activities in the presence of the indicated non-specific irreversible inhibitors are shown in the table below: Protease a Protease B Protease y Given this data, please answer the following question: The catalytic site of Protease ß contains an important: C R H + lodoacetate Normal Activity Normal Activity No Activity U + Tetranitromethane Normal Activity No Activity Normal ActivityFrom a kinetics experiment, the Vmax was determined to be 450µM∙min-1. For the kinetic assay, 0.1mL of a 0.05mg/mL solution of enzyme was used, and the enzyme has a molecular weight of 125,000 g/mole. Assume a reaction volume of 700µL. Calculate the kcat (in sec-1) for the enzyme.
