Case Study: Enzyme Kinetics Data for new statin drug (inhibits HMG CoA reductase): I Substrate (UM) 0.5 1.0 1.5 2.5 3.5 11 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: Consider a peptide AKCVSEAALRIKQEANSL. Which of the following secondary structures the peptide can…
A: In the light of proteins, secondary structure refers to the regional spatial organization of the…
Q: +H₂N-CH-COO™ 1 CH₂ I CH₂ I CH₂ I +H₂N-CH₂ A. amino acid D O amino acid B amino acid C O amino acid A…
A: Amino acids are biomolecules that have a hydrogen atom, an amino group and a carboxyl group linked…
Q: Why mutation would have a greater effect on the stability of a protein. a. Threonine to Valine b.…
A: A protein's propensity to preserve its initial, useful structure under a variety of circumstances is…
Q: The graph shows three plots of velocity (Vo) versus substrate concentration ([S]). Determine which…
A: Enzymes are biological catalysts that increase rate of biochemical reactions.Most enzymes are…
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: Estimate the number of amino acid residues in each of the two helices of a segment of the…
A: The structural configuration of alpha-keratin proteins, a class of fibrous structural protein…
Q: Define these aspects of bioenergetics: couple reactions, allosteric enzymes, activation energy
A: Bioenergetics is the field of biochemistry that deals with how cells convert energy, most often…
Q: Rank these three amino acids from most polar to least polar: +H₂N-CH-C-O CH-OH CH3 *H₂N-CH-C-o CH₂…
A: Amino acids are biomolecules that have an amino group and a carboxyl group linked to the same carbon…
Q: The protein fragments ABS1 and ABS2 of tropomodulin were produced as fusion proteins with chitin…
A: It is possible to filter proteins or fragments of proteins which have been fused with a…
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: Put these three molecules in the order of most oxidized to least oxidized. нн нс-с-н нн H > > 0=…
A: In chemistry, the concept of oxidation state plays a crucial role in assessing the degree of…
Q: You will now build a 15 amino acid peptide using another paper or wire backbone as you did above.…
A: Peptides are polymers of amino acids. Proteins are primarily peptides. There are 20 general…
Q: If a liver extract capable of carrying out normal metabolic reactions (including gluconeogenesis) is…
A: The metabolic pathway that converts non-carbohydrate metabolites like pyruvate into glucose is known…
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: 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: 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: The formation of “hard” clots by factor XIIIa involves linking lysine and glutamine side chain…
A: Fibrin forms long, continuous strands of thick, insoluble protein that are linked to the platelets.…
Q: which region (ribose or base) could be modified to create an inhibitor ?
A: Inhibitors are the molecules or substances that result in inhibiting (stopping) the chemical or…
Q: What kind of catalysis is cysteine driving in this picture? H-N. Metal catalysis Covalent catalysis…
A: General Acid/Base Catalysis: Catalysis involves proton transfer from weak acid or to weak base other…
Q: Write the name of a naturally-occuring nonpolar amino acid. (You will find the structures of the…
A: The proteins are composed of twenty naturally occurring amino acids that are connected via peptide…
Q: The fungus Aspergillus giganteus degrades wood using the ribonuclease a-Sarcin. Of the molecules…
A: The ribonuclease α-Sarcin is used by the fungus Aspergillus giganteus to decompose wood. By…
Q: Analyze the pair of compounds.
A: β - L- galactose & β - L- glucose are both monosaccharides. They are the simplest form of sugar…
Q: A hypothetical protein has a molar mass of 23,300 Da. Assume that the average molar mass of an amino…
A: Amino acids are organic compounds that combine to form proteins; thus, they are known as protein…
Q: You're examining an amino acid at position 3 in an alpha helix. Without knowing the specific amino…
A: Amino acids are the building blocks of proteins and play essential roles in various biological…
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: The hexokinase can be inhibited by a non competitive inhibitor. On your enzyme show where the non…
A: Hexokinase catalyzes the reaction of glucose binding to ATP to form glucose 6 phosphate. The…
Q: Many biochemists go bananas, and justifiably, when they see a Michaelis-Menten plot like the one…
A: For a one-substrate enzyme catalyzed reaction, the Michaelis-Menton equation shows the quantitative…
Q: In the presence of oxygen, most living cells make ATP by oxidative phosphorylation, which takes…
A: a.the given chemical equation is- An…
Q: Suppose a hypothetical "molecule X" binds to hemoglobin (at a different site than the O2 binding…
A: Hemoglobin is a globular protein, ie it is roughly spherical. It is a tetramer of two types of…
Q: The Michaelis-Menten equation models the hyperbolic relationship between [S] and the initial…
A: Protein-based biological entities called enzymes serve as accelerators in living things. They are…
Q: =) D) CH₂ H₂N CH₂ CH₂ NH3 H3NCH-Coo CH₂ OH -CH-COO CH-OH CH3 H3NCH-COo CH-CH3 C10 NH₂
A: There are 20 naturally occurring amino acids in nature. Out of these 10 are essential and 10 are non…
Q: Highlight the atoms or groups that are in hydrophobic portions of this molecule in blue, and the…
A: The name of above given structure is 2-methyl pentanal
Q: 2. You are in a South American rain forest looking for naturally occuring peptides with potential as…
A: Since you have posted a question with multiple sub-parts, we will solve the first three sub-parts…
Q: 3. (a) In Bakers yeast there are two variants of cytochrome c, a heme containing protein of 108…
A: The ionizable groups in peptides/proteins (like cytochrome c) include the side chain groups (R…
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: atalyze cleavage of molecules driven by dition of water talyze transfer of functional groups within…
A: An enzyme is usually a protein that increases the rate of the reaction without itself being used up…
Q: What is the concept of FoldIt protein folding game, and how is it used to elucidate and visualize…
A: The Department of Biochemistry and the Center for Game Science at the University of Washington…
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: Determine whether each of the carbohydrates is a monosaccharide, disaccharide, or polysaccharide.
A: Carbohydrates are biomolecules that comprise carbon, hydrogen and oxygen atoms. The hydrogen-oxygen…
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: Draw dipeptide Arg-Thr at pH 6.0. Circle the six atoms that are restricted in one plane. Calculate…
A: Dipeptide is simply 2 amino acids bonded to each other via a peptide bond. The two amino acids that…
Q: Consider the reaction. 2XY+Z When the concentration of X is doubled, the reaction rate increases by…
A:
Q: Decide whether each of the following statements is true about pyruvate decarboxylase. It…
A: It is an enzyme which catalyses the reaction of decarboxylation of pyruvic acid in to acetaldehyde.…
Q: The ESI-MS spectrum in positive ionization mode for lysozyme is obtained. a. What is the molecular…
A: The y-axis of the ESI-MS spectrum reflects relative abundance and the x-axis the m/z (mass charge)…
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: Which sketches represent the action of an enzyme? Check none of them if none of them do. For that…
A: Enzyme is a catalyst present in living organism which is responsible for alteration of speed of a…
Q: Show the calculation for the preparation of 0.01%, 0.001%, 0.0001%, 0.00001% standard DNA solutions…
A: A liquid combination containing DNA molecules is called a DNA solution. It is frequently employed in…
Q: Assume a fragment of two-stranded antiparallel β-structure is 3.3 nm long. What is the approximate…
A: Deoxyribonucleic acid also known as DNA, is a molecule that houses the genetic instructions required…
Q: Part B Calculate the nonequilibrium concentration of ethanol in yeast cells, if AG = -38.3 kJ/mol…
A: The free energy of a reaction is represented by ∆G. Under standard conditions, it is represented as…
Q: For the DNA sequence shown, indicate the products of its cleavage with the following restriction…
A: In the field of molecular biology and genetic engineering, restriction enzymes, commonly referred to…
Trending now
This is a popular solution!
Step by step
Solved in 5 steps with 7 images
- Case Study: Enzyme Kinetics Data for new statin drug (inhibits HMG CoA reductase): ● ● I 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 38.91From 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.Directions: 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.
- 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) 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).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) above
- Calculcate 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 dilutionConsider the two half-reactions below and their standard reduction potentials. NAD+ + H+ + 2e → NADH Elo= -0.32 V a-Ketoglutarate + CO₂ + 2H+ + 2e → Isocitrate E' = -0.38 V (a) What is AE" for the spontaneous redox reaction that is, the reaction that actually occurs under standard biochemical conditions (pH 7)? (b) Which of the following statements are correct under standard biochemical conditions? i. The concentration of H+ is 1.0 M. ii. The reaction NAD+ + Isocitrate → NADH + H+ + a-Ketoglutarate + CO₂ is favor- able. iii. NAD+ accepts electrons from isocitrate. iv. The NAD → NADH reaction actually occurs in reverse. The a-ketoglutarate → isocitrate reaction occurs as written. (c) Calculate AG" for the reaction in (a). (pH 7, 25°C, pressure, 1 atm.) (d) Suppose that the actual conditions are T = 25°C, pH = 7, CO₂ = 1 atm, [a-Ketoglutarate] 10 mM, [NAD+] = 2.5 mM, and [NADH] = 0.5 mM. PAR = 2 mM, [Isocitrate] DE What is the value of AG under those conditions? (Hints: pH 7 is already…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?41 The following data describe an enzyme-catalyzed reaction (hydrolysis of carbobenzoxyglycyl-L-tryptophan) Plot these results using the Lineweaver-Burk method, and determine values for KM and Vmax Velocity (mM.sec-) 0 024 0 036 0 053 0 060 0 061 0 062 Substrate Concentration (mM) 25 50 10 0 15 0 200 25 0 42 If the KM of an enzyme for its substrate remains constant as the concentration of the inhibitor increases, what can be said about the mode of inhibition and why? 43 Calculate the turnover number for an enzyme, assumıng Vmax IS 05 M sec1 and the concentration of the enzyme used is 0 002 M Why is it useful to know this? 44 Dıscuss the mechanism of the Bohr effect that occurs during the interactions of Hb with oxygen under physiological conditions in the lungs and tissues Make use of relevant graphs and diagrams to explain your answerFrom 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 Inhibited