QUESTION 63The reaction catalyzed by UDP-glucose pyrophosphorylase,UTP + glucose-1-phosphate <-> UDP-glucose + PPproceeds with approximately AGO = 0. Meanwhile, the reaction PP; + H20 --> 2 Pj, catalyzed by pyrophosphatase, proceeds with AG0 = -19.3 kJ mol1. If these two reactions are coupled in the cell, what isAGO' for the net reaction:UTP + glucose-1-phosphate + H20 <--> UDP-glucose + 2 PiO -19.3 k) mol-1O Approximately 0 kj mol-1O +19.3 k) mol1O Cannot tell from the information given.

QUESTION 63 The reaction catalyzed by UDP-glucose pyrophosphorylase, UTP + glucose-1-phosphate <-> UDP-glucose + PP; proceeds with approximately AGO = 0. Meanwhile, the reaction PP; + H20 --> 2 Pj, catalyzed by pyrophosphatase, proceeds with AGO = -19.3 kJ mol1. If these two reactions are coupled in the cell, wh- AGO' for the net reaction: UTP + glucose-1-phosphate + H20 <--> UDP-glucose + 2 P; O 19.3 k) mol-1 O Approximately 0 kj mol1 O +19.3 k) mol1 O Cannot tell from the information given.

QUESTION 63 The reaction catalyzed by UDP-glucose pyrophosphorylase, UTP + glucose-1-phosphate <-> UDP-glucose + PP; proceeds with approximately AGO = 0. Meanwhile, the reaction PP; + H20 --> 2 Pj, catalyzed by pyrophosphatase, proceeds with AGO = -19.3 kJ mol1. If these two reactions are coupled in the cell, wh- AGO' for the net reaction: UTP + glucose-1-phosphate + H20 <--> UDP-glucose + 2 P; O 19.3 k) mol-1 O Approximately 0 kj mol1 O +19.3 k) mol1 O Cannot tell from the information given.

Human Anatomy & Physiology (11th Edition)

11th Edition

ISBN:9780134580999

Author:Elaine N. Marieb, Katja N. Hoehn

Publisher:Elaine N. Marieb, Katja N. Hoehn

Chapter1: The Human Body: An Orientation

Section: Chapter Questions

Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...

See similar textbooks

Similar questions

Help me please
Question 2 of 13 Fill in the blanks: Write Cif only statement A is correct, Hif only statement B is correct, E if both statements are correct, Mif both statements are incorrect. A. The dissociation of the ES complex to the product is more energetically favored than its dissociation into the separate enzyme and substrate. B. The rate determining step in enzymatic catalysis is the binding of the substrate to the active site of the enzyme.
Question 1: Part a: Assume that the standard free energy of ATP hydrolysis is -31 kJ/mol. Assume the following values for the standard free energy changes of the four reactions: HK -16.7 kJ/mol; PFK -14.2 kJ/mol; PGK -18.9 kJ/mol; PK -31.7 kJ/mol. (from bio.libretexts.org). Use these values to compute the standard free energy of hydrolysis (releasing Pi) of i. glucose 6-P ii. fructose 1,6-bis-P iii. 1,3-bisphosphoglycerate iv. phosphoenolpyruvate Part b: Which of these four compounds is the strongest phosphoryl donor?______________ Which is the weakest?__________________ Part c: The phosphoglycerate kinase reaction is favorable by -18.9 kJ/mol in the glycolytic direction, as stated above. In gluconeogenesis, this step is simply reversed; i.e. it is not one of the three steps in gluconeogenesis that is driven by using different chemistry than that of glycolysis. How can this be? (Be specific: what specific factors could enable reversal of this step?)
Question 29 Which enzymes produce 2 ATP's for every glucose? hexokinase O phosphoglyceromutase O Triose phosphate dehydrogenase O phosphofructokinase O pyruvate kinase
Do question 31
Question 28 Which enzyme breaks glucose into 2 molecules of 3 carbons each? O pyruvate deydrogenase O phosphoglycerokinase Aldolase O phosphoglucoisomerase O Hexokinase
Question 1: In some microorganisms, carbon fixation occurs by reversal of the citric acid cycle. This reversal is accomplished in part by the use of a strong reductant (ferredoxin) to drive the alpha-ketoglutarate dehydrogenase reaction in the reductive direction. Part a: ΔG°‘ for reaction as it occurs in the ‘normal’ (oxidative) citric acid cycle is -30.1 kJ/mol. The standard reduction potential for NADH is -0.32 V. In order to drive the reaction in the reverse direction, the reductant (a ferredoxin) must have a lower reduction potential than NADH/NAD+. Remembering that this is a two-electron reduction, and using the numbers given just above, compute the value of the ferredoxin reduction potential that would be needed to make the standard free energy zero (so that the reductive reaction is enegetically just as favorable as the oxidative reaction). Assume that all of the other reactants are the same in the reductive as in the oxidative reaction. Write out the steps in your calculation;…
When rotenone is added to actively respiring bovine mitochondria, the ratio of NADH to NAD+ increases but the FADH2 to FAD ratio remains unchanged. a. What step in the system is being inhibited by rotenone? b. What would be the effect of rotenone on pyruvate oxidation to CO2? ____________________ Why?
QUESTION 2 What TYPE of inhibition is observed in the following plot: 1/v₂ Intersect at Y axis 1/Km Competitive Non-competitive Uncompetitive Allosteric 1/V, max 1/[S]
Question 40 A series of chemical reactions convert a polypeptide into 8 acetyl CoAs. This acetyl CoA goes into the citric acid cycle and then all of the NADH and FADH2 produced are covnerted to ATP by oxidative phosphorylation. How many total ATP is produced from this acetyl CoA including the citric acid cycle and oxidative phosphorylation? Your Answer: Answer units
Remaining V Ha Question 17 Triose phosphate isomerase catalyzes the conversion of Glyceraldehyde-3- phosphate to Dihydroxyacetone phosphate. Glyceraldehyde-3-P Dihydroxyacetone phosphate The Km of this enzyme for its substrate Glyceraldehyde-3-phosphate is 1.8 x 10 M. When [Glyceraldehyde-3-phosphate] = 30 uM the rate of the reaction (v) was 82.5 umol/mL/sec and the Vmax was 132 umol/mL/sec. Assuming 3 nanomoles/mL of enzyme was used ([Eotal = 3 nanomol/mL) the kcat for this enzyme is: Select an answer and submit. For keyboard navigation, use the up/down arrow keys to select an answer. a 44000/sec b 1100/sec 88/min d. 120/hour e 11/min Im f 450000/sec g 52800/sec 175/sec
284