Case Study: Enzyme Kinetics Data for new statin drug (inhibits HMG CoA reductase): 1 Substrate (UM) ● 0.5 1.0 1.5 2.5 3.5 || Rate of reaction (mm/min) 23.5 32.2 36.9 41.8 44 • What are the Kms of the uninhibited and inhibited reactions? ||| Rate of reaction in presence of 5.0 nM statin Using the above date, create a double-reciprocal (Lineweaver Burk) plot. What type of inhibition is shown by the new statin? What are the Vmax of the uninhibited and inhibited reactions? 16.67 25.25 30.49 37.04 38.91
Q: An enzyme catalyzes a reaction with a Km of 6.50 mM and a V of 4.45 mMs. Calculate the reaction…
A: The Michaelis-Menten equation to calculate the reaction velocity of enzymatic catalytic reaction is…
Q: Which of the following is/are true regarding SDS-PAGE (there may be more than one correct answer,…
A: SDS-PAGE is the abbreviation for Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis.It is a…
Q: You have isolated a new protease that cleaves peptide bonds on the carboxyl side of Asp and Glu.…
A: In the realm of enzymology, understanding the specificity of proteases is crucial for unraveling…
Q: 10. In an abnormal hemoglobin variant known as Hemoglobin-Kariya, the lysine residues at position 40…
A: Since you have posted multiple questions, we will provide the solution only to the first question as…
Q: Which of the following amino acids or types of amino acids is rarely found in beta sheets? Polar…
A: Beta sheets are a common secondary structure in proteins, characterized by a sheet-like arrangement…
Q: What is the secondary structure of the peptide hormone GLP-1
A: GLP-1 (glucagon-like peptide 1) is a peptide hormone that is essential to control blood sugar…
Q: 1/Vo O 2 0.2 4 3.5 0.5 2.5 0.25 2 1.5 1 0.5 What is the closet value to the Vmax? 0 0 1/[s] 2 graph…
A: The graph that is plotted by taking reciprocal values of substrate concentration and reaction…
Q: In a sequence of amino acids, a non-polar amino acid is mutated into a polar charged amino acid.…
A: Protein or a polypeptide chain is made up of amino acids linked together by peptide bonds. Protein…
Q: Dr. Herman Branson.... was a physicist and chemist that discovered the double-helix structure in DNA…
A: Two types of secondary structures are abundant in protein: alpha helix and beta sheets. The alpha…
Q: A scaffold protein can serve as a platform to accommodate a collection of enzymes involved in…
A: Scaffold proteins can serve as a platform to accommodate multiple enzymes involved multi-step…
Q: What are enzymatic markers within the mitochondria of oxidative metabolism
A: Mitochondria is the membrane-bound organelle. Mitochondria is the powerhouse of the cell. It plays a…
Q: What are the differences in atp formation in glycolysis vs oxidative met
A: ATP (adenosine triphosphate) is a critical molecule that stores and releases energy for cellular…
Q: For each Acetyl CoA that enters the Krebs Cycle and the products goes through the ETC…
A: The Krebs Cycle, also known as the citric acid cycle, is a crucial component of cellular…
Q: Draw a mechanism using the general features of a serine protease to explain how inhibitor x might…
A: Inhibitors can be broadly classified into reversible and irreversible inhibitors. If the bond…
Q: An allosteric enzyme that follows the concerted mechanism (MWC model) has a T/R ratio of 300 in the…
A: Allosteric enzymes contain an extra binding site for effector molecules in addition to the active…
Q: Part C If, in addition to the constraints on glucose concentration listed previously, we have in the…
A: Pi + Glucose -> Glucose-6-Phosphate + H2OFor the above reaction, ΔG°’ = + 13.8 kJ/mol and…
Q: 2.(a) The two diagrams on the right compare O2 binding pro- perties of Hb Kariya, a human hemo-…
A: Here we are given the hill plot for analyzing the binding kinetics of 2 hemoglobin (Hb) variants,…
Q: How many ATP, NADH, and FADH are formed in the krebs cycle?
A: Cellular respiration can be defined simply as a series of metabolic processes that take place within…
Q: Which of the following amino acids will bind to anion exchange resin at pH 7.0?
A: Anion-exchange chromatography is a type of ion exchange chromatography. Here the stationary phase…
Q: 2. Draw the chemical mechanism for the addition of an RNA nucleotide triphosphate to a growing RNA…
A: RNA or ribose nucleic acid is one of the nucleic acids that act as the genetic material of some…
Q: What kind of catalysis is shown at position #1? Substrate rest of renzyme OHK Acid catalysis Metal…
A: General acid/base: proton transfer occurs between enzyme to substrate or from substrate to enzyme…
Q: A gel filtration column was calibrated by measuring elution volumes for two proteins of known mass:…
A: The established amounts of the elution volumes for the two proteins with determined masses can be…
Q: 3. Fates of pyruvate. Pyruvate has several metabolic fates (some of which you'll learn later) but in…
A: Pyruvate is an important product of glycolysis. It can also be defined as an important junction…
Q: Although all of these may play a part, the major driving force in protein folding is: a) hydrogen…
A: Protein folding is the physical process by which a linear polypeptide folds into its characteristic…
Q: The sigmoidal, cooperative binding curve commonly observed for hemoglobin is a result of: a)…
A: Since you have posted a question with multiple sub parts, we will provide the solution only to the…
Q: An example of omega-3 fatty acid is? Arachidonic acid Alpha-linolenic acid Linoleic acid Oleic acid
A: Long chains of hydrogen-attached carbon atoms give rise to the chemical compounds known as fatty…
Q: A diploid organism with a 45,000-kb haploid genome contains 21% G residues. Calculate the number of…
A: According to Chargaff's rules, DNA from each cell of any organism should contain a 1:1 ratio (base…
Q: Identify the shape of the hemoglobin complex. tetrahedral pentadral hexadral heptadral octahedral
A: Red blood cells (erythrocytes) have presence of a protein which is known as Hemoglobin. Hemoglobin…
Q: Draw beta sheet with backbone hydrogen bonds, is this structure on the interior or exterior of the…
A: A typical structural motif in proteins is a beta sheet, commonly referred to as a beta strand. It is…
Q: 1. (a) By binding one L-tryptophan molecule/monomer, the trp repressor binds to DNA to sup- press…
A: An atom's or molecule's electrostatic charge, which can be either positive or negative depending on…
Q: Draw the following trinucleotide: pGAU
A: A nucleotide is composed of a nitrogen base, a pentose sugar and a phosphate group. A trinucleotide…
Q: Shown below is a substrate for a Trypsin. Draw the mechanism for this serine protease using the…
A: Trypsin is an enzyme which is normally present in living organism to digest proteins but it is also…
Q: Which is the best explanation of why kinesin doesn't bind covalently to its structural protein…
A: Kinesins are motor proteins responsible for transporting cellular cargo along microtubules within…
Q: In the scenario shown above, the green spheres are Glucose molecules and the blue dots are water…
A: Note:- sorry as per the honor code we are not allowed to refer to external links, However, we will…
Q: Disulfide bridges can be formed by structures. O Methionine; tertiary and quaternary OCysteine;…
A: Cysteine is an amino acid that contains a sulfur atom in its side chain (R group). This sulfur atom…
Q: Decide whether each of the following statements is true about chitin deacetylase. It tremendously…
A: Chitin deacetylase is an enzyme found in a wide range of microorganisms, including fungi and…
Q: Name the monosaccharides in the images by placing the appropriate terms. CH₂OH OH OH ОН OH…
A: Carbohydrates are of various types. Based on the number of carbohydrate molecules, it is of 3 types,…
Q: O A) H₂N H3N² B) D) H3N H₂N -CH-COO™ CH₂ CH₂ S CH3 -CH-COO CH₂ CH₂ CIO -o -CH-COO CH₂ OH -CH-COO CH₂…
A: Organic substances known as amino acids are the foundation of proteins and are important to many…
Q: ou have been researching two additional methyltransferase enzymes that catalyze the same reaction.…
A: For a one-substrate enzyme-catalyzed reaction, the Michaelis-Menton equation shows the quantitative…
Q: Explain why the cartoon pictures of proteins often look like ribbons coiled and laying flat. Your…
A: Proteins are primarily polypeptide chains. A polypeptide chain is simply a polymer of amino acids.…
Q: Which of the following would not increase efficiency of transfer of oxygen from hemoglobin to…
A: Haemoglobin is a transport protein that helps in carrying of respiratory gases like oxygen and…
Q: QUESTION 27 If you mixed SDS with the protein below and ran it in SDS-PAGE, how many bands would you…
A: SDS-PAGE or Sodium Dodecylsulphate- Poly Acrylamide Gel Electrophoresis is a molecular technique to…
Q: ration Determine how reaction rate (velocity) varies with substrate concentration. Rate increases…
A: Q.Explanation:- Substrate is a specific term for the reactant on which a particular type of enzyme…
Q: Which statement is true Select one: O a. In earth, amino acids present in D form O b. Sugars present…
A: Biomolecules are the organic molecules present in loving organisms and very useful for the life of…
Q: Find the charge of the peptide KEALYR at pH 7.2. Below is the pKa chart. Provide your answer up to…
A: Before going into the intricate and precise calculation that gives us the charge of the given…
Q: Write out the mechanism of TIM-catalyzed reaction in the direction it goes in glycolysis. Show…
A: In order to produce energy, glucose or other carbohydrates must be broken down. This process is…
Q: Most enzymes are quite specific, catalyzing a particular reaction on a set of substrates that are…
A: Specificity is a property of an enzyme which estimates the number of different chemical species…
Q: In the peptide shown below, a covalent bond that could rotate to form secondary structure is…
A: Two types of secondary structures are abundant in protein: alpha helix and beta sheets. The alpha…
Q: Inhibitors are compounds capable of blocking the catalytic process. Outline with the use of graphs…
A: Ezymes are the biocatalysts that increase the rate of reaction without changing itself to the…
Q: Creatinine, C4H7N3O, is a by-product of muscle metabolism, and creatinine levels in the body are…
A: Let's calculate the mass of creatinine in a 10.0 mL blood sample. The normal level of creatinine in…
Step by step
Solved in 5 steps with 7 images
- a) Calculate the enzyme and specific activity of a reaction with 3 μM Hsp90 using the following information: The rate is measured in a spectrophotometer as 0.028 OD units/min in a 1 ml reaction volume. The absorbance was detected at 340nm and the extinction coefficient for NADH at this wavelength is 6200 L M-1 min-1 and the molecular mass of Hsp90 is 82.7 kDa. The rate of NADH utilisation is equivalent to the rate of ATP utilised by Hsp90. Show all your calculations and the units for your answers. b) Calculate the turnover number for the reaction described in (a) aboveDirections: Solve the following problem: The enzyme ẞ-methylaspartase catalyzes the deamination of ẞ-methylaspartate: CH,NH, CH OOC-CH-CH-COOOOC-CH-CH-COO+NH mesaconate Williams and Selbin The effects of hydroxymethylaspartate as an inhibitor for this enzyme was studied. The following data wer Substrate Concentration obtained: Reaction Rate without inhibitor (mM) 1 × 10-4 5 x 10-4 1.5 x 10-3 2.5 x 10-3 5 x 10-3 (mM/s) 0.026 0.092 0.136 0.150 0.165 Reaction Rate with inhibitor (mM/s) 0.010 0.040 0.086 0.120 0.142 Use Lineweaver-Burk plot to determine the KM and Vmax of the enzyme in the absence of inhibitor. Moreover, determine as well whether the inhibitor is competitive or noncompetitive. Show the graphs and calculations below.From your Lineweaver-Burk plot,the vlaues are: Km Vmax Uninhibited 0.09 mmol/L 3.02 min/mmol Inhibited 6.22 mmol/L 9.98 min/mmol By describing the potential changes in the kinetic parameters, identify and justify the type of inhibitor that was inhibiting the acid phosphatase activity.
- a) Calculate the enzyme and specific activity of a reaction with 3 pM Hsp90 using the following information: The rate is measured in a spectrophotometer as 0.028 OD units/min in a 1 ml reaction volume. The absorbance was detected at 340nm and the extinction coefficient for NADH at this wavelength is 6200L M- 1 min-1 and the molecular mass of Hsp90 is 82.7 kDa. The rate of NADH utilisation is equivalent to the rate of ATP utilised by Hsp90. Show all your calculations and the units for your answers. b) Calculate the turnover number for the reaction described in (a) aboveYou make reaction progress curve by plotting absorbance vs time (seconds) and find the equation of the line to be y = -0.00235x + 0.7129. Calculate the U/µL and U/mL of lactate dehydrogenase activity in this fraction. The LDH activity is done identical to what is indicated in the lab manual. Show each step of the calculation from AU/time to M/min, to mol/min, to µmol/min to µmol/min/µL (=U/µL).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
- Lineweaver-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?Calculate AG for the below balanced redox reaction as written. You may find a list of standard reduction potentials useful. 3 12 (s) + 2 Al (s) → 61 (aq) + 2 Al3+ (aq) O-4.24 x 102 kJ/mol O-6.48 x 102 kJ/mol O -2.12 x 102 kJ/mol O-1.27 x 103 kJ/mol O-6.37 x 102 kJ/molCalculcate Kcat for PNP substrate for both enzyme concentrations. enzyme volume: 20 ul Bovine Intensince Alkaline phosphatase molecular weight: 140,000 Bovine intenstine Alkaline phosphatase activity: 300 units/ml and 14 units/mg extinction coefficient PNP: 18.5 abs (mM-1 cm-1) Vmax: 0.332 moles/sec a) enzyme 1 concentration: undiluted b) enzyme 2 concentration: 1:1 dilution
- In an enzyme kinetics study, three inhibitors resulted to the following results: Inhibitor ABC Inhibitor XYZ Inhibitor PQR Without Inhibitor Vmax 40.2 mM/ sec 40.3 mM/ sec 12.32 mM/ sec 65.43 mM/ sec Km 24.3 mM 28.5 mM 24.3 mM 15.7 mM d. Draw the estimated Michaelis Menten Curve of Inhibitor ABC and the curve without the inhibitor.From your Lineweaver-Burk plot, derive the values for the following table. Indicate the appropriate units. (b) By describing the potential changes in the kinetic parameters, identify and justify the type of inhibitor that was inhibiting the acid phosphatase activity. Km Vmax Uninhibited InhibitedLineweaver-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?