1. Label I, II, III, IV II Energy level IV I III Progress of reaction 2. If A is original enzyme reaction state, and B and C chemicals were added. What is the role of B and C chemicals? Potential Energy A Reaction Coordinate
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- 1. An enzyme-catalyzed reaction has a KM of 1 mM and a Vmax of 5 nM s-1. What is the reaction velocity when the substrate concentration is 0.25 mM? 2. If an enzyme-catalyzed reaction has a velocity of 2 mm/min and a Vmax of 10 mm/min when the substrate concentration is 0.5 mM, what is the KM?Calculate the specificity constant for an enzyme-catalyzed reaction if the total enzyme concentration is 15 nM, Vmax is 9 M/s, and Km is 150 M. A. Has the enzyme achieved catalytic perfection? (Y or N)Which of the listed effects would be brought about by any enzyme catalyzing the following reaction? k1 S P where K'eg = [P]/[S] and AG°' = -RT In K'ea k2 (a) Decreased K'egi (b) increased k1; (c) increased K'ea; (d) increased AG*; (e) decreased AG*; (f) more negative AG°; (g) increased k2. Justify your answer using a reaction energy diagram. Problem 2. (a) The following data were obtained for an enzymatic reaction, in which the total enzyme concentration was 0.005 mM. Without plotting the data, can you estimate the approximate Km for this enzymatic reaction? How did you determine it?
- ac cic with equal ease? 4 Compare the activation energy in uncatalyzed reac- tions and in enzyme-catalyzed reactions. q 190 WIL nood in many different. Relation between Reaction Velocity and Substrate Concentration: MichaelisMenten Equation: At what substrate concentration would an enzyme with a kcat of 30.0s−1 and a Km of 0.0050 M operate at one-quarter of its maximum rate?Please answer the calculation
- answer quickly:The following data were obtained in a study of an enzyme known to follow Michaelis-Menten kinetics Vo (mmol/min) S (mmol/L) 0.8 3 4 217 325 433 488 1,000 :The Km for this enzyme is approximately 647 mM 4 O mM 1 O mM 1,000 Ⓒ mM 3 O mm 6 OWhich of the following contributes most substantially to rate acceleration produced by an enzyme? O A. Ability to bind the substrate OB. Ability to bind the transition state O c. Ability to bind the product O D. All of the above contribute equally. 56
- Devise a biosynthesis for the natural product (II) from an appropriate starter co-enzyme A and malonyl coenzyme A. appropriate starter molecule (I) + OiiS.COM malonyl coenzyme A → 'N (II)5. An enzyme catalyzes the reaction M concentration of 1 nM, and the Vmax is 2 µM s-1. The Km for substrate M is 4 µM. N. The enzyme is present at a (a) Calculate kcat. (b) What values of Vmax and Km would be observed in the presence of sufficient amounts of an uncompetitive inhibitor to generate an a' of 2.0? Increased or decreased?3. (а) 0.0050 M operate at one-quarter of its maximum rate? At what substrate concentration would an enzyme with a kcat of 30.0 s-1 and a KM of (b) trations [So]: ½ Km, 2 KM, and 10 KM. Determine the fraction of Vmax that would be obtained at the following substrate concen- (c) 1 (HIV-1) has been the object of innumerable studies to develop effective chemotherapeutic agents. It has been shown that p6* known as the late assembly protein is an inhibitor of HIV protease. An assay was developed using an artificial polypeptide substrate containing a p-nitrophenylalanine residue at the cleavage point that undergoes a small change in absorption at 295 nm upon bond hydrolysis that could be followed spectrophotometrically. The cleavage of the peptide bond is shown schematically on the right. Results of the assay are given in the table below. The protease of the human immunodeficiency virus- Lys NH2 Ala Nle Arg Ala Val-Nle-NH-CH-Ċ–NH-Glu CH2 Lys NH2 Ala NO2 Nle H2ON HIV-1 protease Ala Vo…