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- Express the initial velocity of α-amylase in terms of substrate disappearance and product (as glucose) formation.The conversion of glucose (C6H1206) into lactic acid (2CH3CH(OH)COOH) drives the phosphorylation of 2 moles of ADP to ATP and has a AG° = %3D -135 kJ/mol. CH1206laq) +2HPO (aq) +2ADP3- (aq) +2H* (aq) 2CH,CH(OH)COOH(aq) +2ATP4- (aq) +2H,0(1) The conversion of ATP to ADP has a AG° = -30.5 kJ/mol. ATP4- (aq) +H,0(1) ADP (aq) +HPO (aq) +H*(aq)(Thanks for the help if you can break down the steps and provide drawings(needed) during the answer since i am trying to see if i have solved this in the right way not copy :)) Draw the heme environment in oxymyoglobin and explain how the geometric data for the attached oxygen molecule may be understood. Fe O (bond length) = 1.809 Å; O-O (bond length ) = 1.246 Å; Fe - O - O (bond angle) = 123 \deg
- + OH HO + !!!10 HO HOLI > OsO4 (catalytic) NMOPlease don't provide handwriting solution(75) (75) Consider the following reaction. From the given choices of intermediates and/or final products, choose the 5 related to this reaction and put them in order to describe the complete mechanism (all the steps involved) for this reaction.
- Find the AHrn for the following reaction: 2N29) + 502(9) → 2N,O5(9) given the following reactions and subsequent AH° values 2H2(9) + O2(9) → 2H,Ou) N½O5(9) + H2Ou → 2HNO3(1) AH° = -541.6 kJ AH° = -54.6 kJ %D N2(9) + 302(9) + H2(9) → 2HNO3(1) AH° -331.1 kJChemistry Use the References to access important values if needed for this question. Suppose a sequence of enzymatically catalyzed reactions converts substrate A to final product D through a sequem reactions involving the production of intermediate products B and C as shown. Product D inhibits enzyme E₁. If the enzymes E₁-E3 are all present in a test tube and substrate A is added to the reaction mixture, how will the concentration of product D change? E₁ E₂ E3 A B C D increase to a fixed value first increase, then decrease remain at zero oscillate between zero and the concentration of A added increase to the concentration of A added Submit Answer Try Another Version 1 item attempt remainingS Suppose that, in the absence of enzyme, the forward rate constant, kf, for the conversion of S to P is 10-4 s-¹ and the reverse rate constant, kp, for the conversion of P to S is 10-6 s-¹. What is the equilibrium constant, K, and what is the AG°, or standard free-energy change at pH 7, for the uncatalyzed reaction? K = KF 10-45-1 S=P 10-6-1 = Suppose an enzyme enhances the rate of the reaction 100 fold. What are the KF and KR values for the enzyme-catalyzed reaction? K= AGO! $`1 KR || = What are the K and AG' values for the enzyme-catalyzed reaction? = AGO = kJ.mol-¹ 8`1 kJ.mol-1
- predict the products of the following reactions for numbers 44 and 45.As you know, the enolase enzyme of glycolysis utilizes an E1CB mechanism to expel hydroxide as a leaving group, converting 2-PG to PEP. Like other transformations we have studied in this course, enolase has strict stereoelectronic requirements for its substrate. Two possible conformations of the intermediate within the enolase active site are shown below. (Some bond lengths are exaggerated for clarity.) HO H H =0 H OH HO Conformation 1 HO Conformation 2 a) State which of these two conformations is correct, and briefly explain. For full credit, your explanation must cite a specific donor-acceptor orbital interaction and alignment. You do not need to draw any "cartoon" orbitals. b) As shown above, the phosphate group of 2-PG is maintained in an unusual state within the enzyme active site. Briefly explain what is unusual about this phosphate group under physiologic conditions, and what strategic advantage this provides for the reaction. c) PEP, the product of the enolase reaction, is…235L-6. For the following, a) predict the product and b) using curved arrows to show electron movement, provide a reasonable mechanism for the reaction. CI H2N, (-HС) 2 `NH2 ???
