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- Instructions. Given each set of information which may include common name(s) and the reaction catalyzed, you are required to identify the main class of the specific enzyme described. Name: citryl-CoA synthetase Reaction: ATP + citrate + CoA = ADP + phosphate + (3S)-citryl-CoA Name: D-xylulose reductase Reaction: xylitol + NAD+ = D-xylulose + NADH + H+ Name: cellobiose phosphorylase Reaction: cellobiose phosphate = α-D-glucose 1-phosphate + D-glucose Name: carbonic anhydrase Reaction: H2CO3 = CO2 + H2O Other info: The enzyme catalyzes the reversible hydration of gaseous CO2 to carbonic acid, which dissociates to give hydrogencarbonate above neutral pH. Name: pantoate activating enzyme Reaction: ATP + (R)-pantoate = AMP + diphosphate + (R)-pantothenate.Od. Vitamin B2 s page Hexokinase catalyzes phosphorylation of glucose to clucose-6-phosphate, where ATP is used as a donor of phosphate group, this an example of: Select one: NAVIGATION a. Oxidoreductase b. Ligase c. Lyase d. Transferase Next pageWhat is the catalytic efficiency of Catalase ? Table. The values of KM and kcat for some Enzymes and Substrates Enzyme Carbonic anhydrase Substrate CO2 HCO3 KM (M) 1.2 x 10-2 2.6 x 10-2 Kcat (s-1) 1.0 x 106 4.0 x 105 Catalase H2O2 2.5 x 10-2 1.0 x 107 Urease Urea 2.5 x 10-2 4.0 x 105 O A. 4 x 108 M-s-1 O B. 4 x 108 M-1.s-1 OC25x 10-9 M-s1 D. 2.5 x 102 M-1.s-1 OE 1.0 x 107 s1
- Enzymes catalyze chemical reactions. What constitutes the active site of an enzyme? What are the turnover number (kcat), the Michaelis constant (Km), and the maximal velocity (Vmax) of an enzyme? The kcat (catalytic rate constant) for carbonic anhydrase is 5 × 105 molecules per second. This is a “rate constant,” but not a “rate.” What is the difference? By what oncentration would you multiply this rate constant in order to determine an actual rate of prod- uct formation (V)? Under what circumstances would this rate become equal to the maximal velocity (Vmax) of the enzyme?Hi, help please. Discuss each method of regulating phosphofructokinase below as indicated by the circle. Discuss 1.) The type of regulation occurring, 2.) What compound or condition performs the regulation, 3.) How/why it influences the enzyme activity.Please ASA. Thanku. In the reaction Na + Cl à Na+ + Cl-, which component is said to become ‘oxidized’ and which is considered reduced? Na, Cl Cl, Cl Na, Na Cl, Na
- Worksheet on Computation of ATP yield from Fatty acid metabolism. Consider docosanoic acid, C21H43CO2H a. Label alpha (a) and beta ( B) carbons b. Draw the acyl COA derived from this fatty acid c. How many acetyl CoA molecules are formed by complete B-oxidation? d. How many cycles of B- oxidation are needed for complete oxidation? e. How many molecules of ATP are formed from the complex catabolism of this fatty acid.. Recall your study of equilibria and kinetics from general chemistry. You used equations with upper case Kand lower case k during the study of equilibria and kinetics respectively. What do the upper and lower case letters refer to?Draw TCA Cycle. Please make sure to state all the enzymes and co-factors for each step of the pathway.
- Fill in the blanks.: Write Cif only statement A is correct, Hif only statement B is correct, E if both statements are correct, M if both statements are incorrect. A. An enzyme catalyzes a reaction by providing an alternative reaction pathway that has a lower energy of activation. B. The enthalpy of the enzyme-catalyzed reaction decreases significantly as compared to the uncatalyzed reaction.G. ENZYME CLASSIFICATION. Identify the main class of enzymes used to catalyzed the following reactions: 1. Lactate dehydrogenase: NADH+H NAD HC-OH CH3 CH Pynnte Lactate 2. Methylmalonyl-CoA mutase: CH CH SCOA CH,CH, SCOA coenzyme B12 COO COO methylmalonyl-CoA succinyl-CoA 3. Enolase: 0. H–Ċ–0–P–0- C-0–P-0- + H,0 HO–CH, CH 6 Phosphoenolpyruvate 2-Phosphoglycerate 4. Chymotrypsin: -0–CH,CH3 + H2O - RCOOH + HOCH,CH3 5. Pyruvate carboxylase: coo • co, • ATP + H,0 H-C-H . ADP + P, + 2H čoo CH, Pyruvate Oxaleacetatein human 2. Human xanthine oxidase catalyzes the oxidation of hypoxanthine to xanthine and can further catalyze the oxidation of xanthine to uric acid. For the treatment of hyperuricemia and gout. several medications are used to inhibit the activity of xanthine oxidase and reduce the production of uric acid. You are a biochemist and just discovered a chemical that can inhibit the activity of the human xanthine oxidase. When analyzing its mode of inhibition, you found that the enzyme inhibitor complex requires 450 kJ.mol to dissociate and that it displays kinetics somehow similar to noncompetitive inhibition. You sent your inhibitor to the ministry of health for approval as a medication for gout. Based on the data provided, are they going to authorize it as a medication or not? Explain?