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- Triose phosphate isomerase is a diffusion-controlled enzyme. What reaction is catalyzed by this enzyme (structures of molecules not needed)? Explain why this enzyme has evolved to be a very fast enzyme
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- CH₂OH 애 H2COPO 2- ATP OH 1 애 애 어 애 The class of the enzyme catalyzing the reaction shown in this figure is a(n) Choose the one best answer. ligase 매 +ADP 매Many types of cells are able to use membrane-spanning transport proteins and a source of energy to drive the active transport of glucose across the cell membrane. Leť's consider a specific protein that is able to transport (from outside the cell into the cytoplasm) one molecule of glucose for each molecule of ATP the protein hydrolyzes. The details of this process are not important for this problem except that you can treat it like equilibrium process. The overall reaction and the associated AG at 298 K for this process are given below. Glc(out) + ATP + H20 = Glc(in) + ADP + P at T = 298 K, AG = -31.3 kJ mol-1 Additional Information: • P. is "inorganic phosphate" (i.e. PO4²- & related species). At equilibrium, [P] = 3 x 10-3 M. • The cell maintains a ratio of ATP to ADP of about 20 (i.e. [ATP]/[ADP] = 20). • The maximum ratio of [Glc(in)] to [Glc(out)] occurs when the system is at equilibrium. a) Write an expression for the equilibrium constant for this process. b) Your expression for…Enzyme - Acid Phosphatase Substrate - Para-nitrophenylphosphate Product - para-nitrophenol and phosphate. NaOH is added to stop the reaction and absorbance is measured. Explain at the molecular level what would happen if you replace NaOH with HCl.
- The protein catalase is an enzyme that catalyzes the decomposition of hydrogen peroxide:2 H2O2 (aq) → 2 H2O (l) + O2 (g)and has a Michaelis-Menten constant of 25 × 10-3 mol·dm-3 and a turnover number of 4.0×107s-1.The total enzyme concentration is 0.016×10-6 mol·dm-3 and the initial substrate concentration is4.32×10-6 mol·dm-3 Calculate the maximum reaction rate (????) for this enzyme, and the initial rateof this reaction. Note that catalase has a single active site.The hydrolysis of pyrophosphate to orthophosphate drives biosynthetic reactions such as DNA synthesis. In Escherichia coli, a pyrophosphatase catalyzes this hydrolytic reaction. The pyrophosphatase has a mass of 120 kDa and consists of six identical subunits. A unit of activity for this enzyme, U, is the amount of enzyme that hydrolyzes 10 umol of pyrophosphate in 15 minutes. The purified enzyme has a Vnax of 2800 U per milligram of enzyme. When (S] >> KM, how many micromoles of substrate can 1 mg of enzyme hydrolyze per second? Vnas umol-s. mg-! max If each enzyme subunit has one active site, how many micromoles of active sites, or (E]r, are there in 1 mg of enzyme? (Er= umol · mg-!The enzyme phosphoglucomutase catalyzes the conversion of glucose 1-phosphate to glucose 6-phosphate. After the reactants and products were mixed and allowed to reach equilibrium at 25°C, the concentration of glucose 1-phosphate was 4.5 mM and that of glucose 6-phosphate was 86 mM. Calculate Keq' and AG for this reaction. The reaction coordinate diagram for an enzyme-catalyzed reaction is shown below. How many transition states and intermediates are in the reaction? Is the reaction thermodynamically favorable? Which step is the rate-determining step of the reaction? G Reaction coordinate
- The enzyme which catalyzes the reaction below belongs to which enzyme classification? Н.С— ОН HC=0 C=0 Н-С—ОН H,C-0-P-o- || H,C –0-P-0- O Transfera Hydrolase Isomerase Oxidoreductasethe enzyme dUTPase from the African swine fever virus (ASFV), which is a virus that spreads rapidly in swine (pigs) and is often deadly. The normal function of the dUTPase enzyme is to convert dUTP to dUMP. Which of the following statements about the dUTP substrate for a dUTPase is true? Explain your choice in 25 words or less. The dUTP substrate binds with lower affinity to the enzyme than the dUMP product The dUMP product is more easily formed when catalyzed by the dUTPase because the equilibrium is shifted away from the dUTP substrate The formation of the dUTP-dUTPase complex is driven by entropy More than one of the above statements is true None of the above statements is trueSubstrates and reactive groups in an enzyme’s active site must be precisely aligned in order for a productive reaction to occur. Why, then, is some conformational flexibility also a requirement for catalysis?
- Consider the reaction: Galactose 1-phosphate + UDP-glucose → UDP-galactose + glucose 1-phosphate Which pairing correctly matches the enzyme class and Enzyme Commission number for the enzyme that catalyzes this reaction? translocase; 2 translocase; 7 transferase; 2 transferase; 7 isomerase; 5Given the reaction below, what major class of enzyme will catalyze such reaction? OH HO OH OH 'OH Select the correct response: Isomerase Ligase Oxido-reductase Transferase Lyase + ATP Hydrolase || HO‘ OH OH "OH + ADPIn covalent catalysis, either nucleophilic catalysis or electrophilic catalysis occurs. Do you agree or disagree with this statement? Explain.