The initial rate (v0) data as a function of substrate concentration [S] for an enzyme (Enzyme1) that obeys Michaelis-Menten kinetics are shown in the table below. The total enzyme concentration is 2.5 nM.
Q: Utilising the provided class data generate the following graphs: I) Michaelis Menten; II)…
A: Enzymes kinetics - is the study of the reaction rate of enzyme catalyzed reactions. The reaction…
Q: The 4 graphs above represent the change in enzyme kinetics with the individual addition of different…
A: Enzymes kinetics - is the study of the reaction rate of enzyme catalyzed reactions. The reaction…
Q: Lysozyme is an enzyme that hydrolyzes bacterial cell wall…
A: Lysozymes are antibacterial agents that have the ability to hydrolyze the cell wall of bacteria. The…
Q: - Draw the graph A340 = f(t). Comment the shape of the curve Calculate alanine, LDH, NADH and…
A: If a particular reaction brings about a measurable change (like the generation or consumption of a…
Q: Explain this krebs cycle
A: Cellular respiration is a collection of three metabolic pathways that generate ATP by the oxidation…
Q: Question 7 Consider the structure of Baclofen, a GABA derivative used to treat cerebral palsy, drawn…
A: Baclofen is a chlorophenyl derivative of gamma-aminobutyric acid (GABA) derivative and it is a…
Q: Draw a schematic diagram illustrate the interactions made between the key components of total and…
A: Ligand and protein binding is vital phenomenon in our body for enzyme-substrates, enzyme-inhibitors,…
Q: 1- Describe any errors in your technique. How could you improve upon your technique in order to get…
A: Spectroscopy is used to determine the concentration of a substance. This technique is dependent on…
Q: Which one of the following statements about coenzyme Q is not true? a. coenzyme Q is lipid-soluble…
A: Coenzyme Q or ubiquinone or CoQ is an electron carrier that accepts electrons from NADH and FADH2,…
Q: What makes RNA a ribozyme? Why are DNA enzymes absent?
A: Enzymes are biomolecules which can catalyze the biochemical reactions. These can be proteins, RNA or…
Q: Briefly comment on the differences of using a fixed-time assay versus a kinetic assay to measure…
A: Fixed-time and kinetic assays are two common methods to measure enzyme activity. In a fixed-time…
Q: list the primary energy system out of these 3 (only pick 1) (TP-PC System, Glycolysis & Citric Acid…
A: Food is the composition of carbohydrates, fats and proteins. On digestion these macromolecules are…
Q: 7. Why is the doorway step needed to link glycolysis and the Krebs Cycle?
A: Glycolysis takes place inside the cytoplasm. Mitochondria is the site for kreb's cycle. Since both…
Q: What is Monoamine neurotransmitter, Amino-acid neurotransmitter, and neuropeptides?
A: Amino acids are a type of biomolecule that is involved in several biological and chemical functions…
Q: 3.) As mentioned in the March1 outline a critical step in the glycolysis metabolic pathway…
A: Triose phosphate isomerase catalyzes the interconversion between Dihydroxyacetone phosphate (DHAP)…
Q: 8. Glucose-6-phosphate dehydrogenase catalyzes the same reaction shown in problem 7 in yeast. The KM…
A: In enzyme kinetics: Km (Michaelis-Menten constant) is a measure of how tightly an enzyme binds to…
Q: 1) Why is the GPCR referred to as a GEF? What would occur in G protein signalling if the Ga subunit…
A: This answer explains the concept of G protein-coupled receptors (GPCRs) and their role as guanine…
Q: 1.a)Which one of the following vitamins is fat-soluble? Vitamin B12 Vitamin D Vitamin B1 Vitamin B3…
A: Introduction Vitamins are the organic substances which is required for our growth and development.…
Q: A higher concentration of NADH in the liver is associated with an increase in gluconeogenesis. Your…
A: NADH (nicotinamide adenine dinucleotide) is a coenzyme that plays a critical role in many cellular…
Q: Genetic disorders of urea synthesis
A: As a result of our metabolism, amino-acid metabolism specifically, a lot of ammonia is produced in…
Q: 1. If Ser 80 was replaced with Arg what kind is the change in the bond type between these two…
A: the stability of an amino acid is influenced by the specific interactions it forms with other amino…
Q: Before we finish this part of the Activity, you’re going to begin summarizing what you’ve learned…
A: Functional Group: A functional group is a reactive portion of a molecule that is responsible for the…
Q: Using the cultured cells used in this experiment and described in the introduction, how would you…
A: When increasing amounts of the labelled ligand are added to the cells, the amount of binding will…
Q: What kind of protein is casein? POST-LABORATORY QUESTIONS: What is the isoelectric point of casein?…
A: Since you have posted a question with multiple sub parts, we will provide the solution only to the…
Q: For what chemical group is Millon's reagent a test? Write the formula and the name of the amino acid…
A: A biochemical test is a laboratory procedure for identifying or quantifying specific molecules or…
Q: A carboxypeptidase is a metalloenyme (its active site contains one or more metal ions essential for…
A: An active site of an enzyme is a three dimensional structure that occurs within the enzyme. An…
Q: 28) Which of the following hormones does NOT stimulate production of BPG? a) Epinephrine b)…
A: Hormonal control is the use of hormones to regulate physiological processes in the body. Hormones…
Q: Can you show in a diagram how sulfur is cycled (Sulfur cycle) in a water column (Winogradsky…
A: Winogradsky column is an artificial ecosystem made in a transparent plastic or glass column to…
Q: If 10x TBE contains 0.89 M Tris-borate, 0.89 M Boric acid, and 0.02 M EDTA, what is the Molar…
A: Molar concentration is a measure of the amount of a substance in a given volume of solution. It is…
Q: Q1 Acety CoA 3. ATP Acy CoA ADP Ace Co Acetoacety CoA FAD L-Glycer 3-phosphate FACH 1,0 ATP NAD…
A:
Q: What does it mean for an amino acid to be polar? Please explain what qualities about an amino acid…
A: Proteins are folded polypeptides. A polypeptide is a polymer of amino acid residues linked via a…
Q: In no more than 100 describing a negative control that you might perform along side your dna…
A: In a DNA purification experiment, a negative control is the use of a blank sample, such as a sterile…
Q: Lysozyme is an enzyme that hydrolyzes bacterial cell wall…
A: Lysozymes are antibacterial agents that have the ability to hydrolyze the cell wall of bacteria. The…
Q: cetyl CoA is carboxylated to malonyl CoA during fatty acid biosynthesis: a) for thermodynamic…
A: Acetyl-CoA carboxylases enzyme catalyzes the acetyl-CoA carboxylation and produced malonyl-CoA.…
Q: A polar functional group that forms disulfide bridges and stabilizes protein tertiary structure is A…
A: The sequence of amino acids in the polypeptide chain is referred to as the fundamental structure of…
Q: Explain why people with a hereditary deficiency of carnitine acyltransferase II have muscle…
A: Carnitine acyltransferase II (CAT II) is an enzyme that is involved in the transport of long-chain…
Q: Consider the following experimental data from another experiment: [S] 1.5 2.00 2.50 5.00 10.00 V (No…
A: Parameters such as Km and Vmax are used for comparing enzyme activities. If we know the initial rate…
Q: Answer Bank Glyceraldehyde 3-phosphate + P¡ + NAD+ →→→ 1,3-bis 3-Phosphoglycerate →→→…
A: Glycolysis is the first phase in aerobic cellular respiration. It is the step during which one…
Q: Standard redox potentials E' for some common compounds in biochemistry: Eo' (Volt) + 0,81 12 O2 + 2…
A: If the Gibbs free is negative for a reaction then the process is said to be spontaneous. A positive…
Q: 1) Use the Leontis-Westhof base pair classification to identify the interaction occurring between…
A: Leontis-Westhof base pair classification is a system that categorizes RNA base pairs based on the…
Q: 22. Explain why how the shape of an enzyme is related to the function. 23. How is the synthesis of…
A: Proteins have certain chemical characteristics, and enzymes are proteins. Tertiary or quaternary…
Q: 1. What do the drops of NaOH indicate in terms of metabolic output (Hint: what causes carbon dioxide…
A: Aerobic respiration is a metabolic process that requires oxygen and produces ATP, a molecule that…
Q: Pompe disease is due to a deficiency in lysosomal α-1,4-glucosidase, also called acid maltase.…
A: Pompe disease was named after Johann Pompe who identified the disease in 1932. It is a lysosomal…
Q: Acetyl-CoA carboxylase is the principal regulation point in the biosynthesis of fatty acids. Some of…
A: Acetyl-CoA carboxylase (EC 6.4.1.2) is a biotin-dependent enzyme. It is responsible for the…
Q: Can someone please show your work for tracking the radiolabel: draw structures indicating position…
A: The given structure is a polysaccharide - starch (amylose) with alpha 1,4 glycosidic bond. It…
Q: For lipids to be able to travel in the blood, they must first be packaged into lipoproteins.…
A: There are five major groups of lipoproteins that circulates lipids in the body. They are…
Q: Table 1. Results of the Shrinkage Assay. Enter your assessment of the shrinkage of cell at the times…
A: A line graph represents the trend of the data on basis of differnt times. The y-axis usually shows…
Q: For the PDHC, generally what goes on in each active site, what is the role of lipoamide, and what…
A: The PDHC is an enzyme complex that undertakes the oxidative decarboxylation of pyruvate (i.e. both…
Q: Given the amino acid chain below, get the (a) translation strand, (b) transcription strand strand,…
A: DNA is double stranded. There one strand is the template strand and the other is non-template. From…
Q: Match the following sugars with their corresponding descriptions. A Esculin Arabinose aldonitol G.…
A: Sugars are 'sweet-tasting' carbohydrates. Depending on their type, they can be either (a)…
Trending now
This is a popular solution!
Step by step
Solved in 2 steps with 1 images
- Utilising the provided class data generate the following graphs: I) Michaelis Menten; II) Lineweaver-Burk; and III) Hanes-Woolf. Ensure that you clearly label each graph,and add the relevant trendlines with equations. Table 1: Class data demonstrating the Absorbance at 700nm obtained for the alkaline phosphatase enzyme reaction Table 1 tube Abs700mm 1 0.000 2 0.060 2 0.090 4 0.140 5 0.190 6 0.250 7 0.290 The equipment we used are • 20mM Tris Buffer pH 8.5 • 33mM MgCl2 • Alkaline Phosphatase (2mg/ml) in 20mM Tris Buffer pH 8.5 • 4mM Glucose-1-phosphate • Acid Molybdate pH 5.0 • Reducing Agent • Distilled Water • Glass Test tubes • Tube Rack • Cuvette • Pipettes and Tips • Water bath set to 37oC The method we used is Method/Protocol: 1. Read the protocol in its entirety before starting. Take note of any additional information that appears in subsequent steps that may influence how previous steps are performed. 2. Using glass tubes, generate the reactions mixtures…calculate the reaction velocity at saturating substrate concentrations. Your numerical answer is assumed to be in units of M sec-1. [S] = 100 mM k1 = 10 sec-1 k2 = 3000 sec-1 k-1 = 20 sec-1 [E]T = 1 \muμMLineweaver-Burk plots of enzyme kinetics for the reaction, S <-> P, has the following features: 1/v is zero when 1/[S] equals -40 liter mole^-1; 1/[S] is zero when 1/v equals 2.0 x 10^5 min mole^-1. What are the Vmax and Km? Vmax = 5 umol min^-1, Km = 2.5 mM? Vmax = 5 mmol min^-1, Km = 25 M? Vmax = 5 umol min^-1, Km = 25 mM? Vmax = 5 mol min^-1, Km = 2.5 mM? Vmax = 5 mol min^-1, Km = 25 mM?
- . The optimal conditions for salivary lysozyme (hydrolyzing glycoproteins of bacterial wall) are 37 C - temperature and pH is 5.2. Explain the decrease in this enzyme activity if the temperature will rise up to 60 °C and pH will be changed to 8.0. To answer the question: a) draw the graph of the velocity dependency on temperature and pH; b) calculate the relative enzyme activity if 10 mg of lysozyme catalyzes the formation of 5 uM of the product per 2 minutes. Concidor NH3: 5.An enzyme catalyzes a reaction at a velocity of 20 μmol/min when the concentration of substrate (S)is 0.01 M. The Km for this substrate is 1 × 10-5 M. Assuming that Michaelis-Menten kinetics arefollowed, what will the reaction velocity be when the concentration of S is 1 ×10-6 M?The rates at various substrate concentrations for an enzyme-catalysed reaction (b) are recorded as follows: 2.5 5.0 10.0 15.0 (S]/10 M 2.2 3.8 5.9 7.1 Vo/ M min Assuming the reaction obeys Michaelis-Menten kinetics, calculate the following values by using Lineweaver-Burk plot () maximum rate, Vmax- (i) Michaelis constant, Km- (ii) turnover number, kz.
- The steady-state kinetics of an enzyme are studied in the absence and presence of an inhibitor (inhibitor A). The initial rate is given as a function of substrate concentration in the following table: v[(mmol/L)min- [S] (mmol/L) No inhibitor Inhibitor A 1.25 1.72 0.98 1.67 2.04 1.17 2.50 2.63 1.47 5.00 3.33 1.96 10.00 4.17 2.38 (a) What kind of inhibition (competitive, uncompetitive, or mixed) is involved? (b) Determine Vmax and Ky in the absence and presence of inhibitor.An enzyme that follows Michaelis-Menten kinetics has a KM value of 3.00 µM and a keat value of 181 s1. At an initial enzyme concentration of 0.0100 µM, the initial reaction velocity was found to be 1.07 x 10-0 µM/s. What was the initial concentration of the substrate, S, used in the reaction ? Express your answer in micromolar to three significant figures. > View Available Hint(s) ? [S] !! µM SubmitThe turnover number for an enzyme is known to be 5000min-1. Given the following set of data, Substrate concentration(mM) 1, 2, 4, 6, 100, 1,000 Initial Rate(micromol/min) 167, 250, 334, 376, 498, 499 a) What is the Km of the enzyme for the substrate? (do this without using a calculator) b) What is the total amount of enzyme present in the assay?
- Calculate the Km of the enzyme with these parameters. kcat = 130s^-1 Vo = 3.0 μMs-1 S = 10 μM Et = 0.09 µMAn enzyme catalyzes a reaction at a velocity of 20 micromole/min when the concentration of substrate (S) is 0.01 M. The Km for this 1 X 10^-5 M. Assuming that Michaelis-Menten Kinetics are followed, what will the reaction velocity be when the concentration of S is 1.0 X 10^-6 M?For an enzyme that displays Michaelis-Menton kinetics, what is thereaction velocity, V (as a percentage of V max , observed at the followingvalues?[S] = K M[S] = 0.5K M[S] = 0.1K M[S] = 2K M[S] = 10K M