Consider the graphic representation shown below for the free energy change for the overall reaction of Fructose-6-phosphate and ATP to form the products Fructose-1,6-biphosphate and ADP in the presence (blue line)or absence (red line) of enzyme. Match each of the arrows (labeled A, B, C, or D) indicated in the graph with an apropriate description by dragging the letters into their corresponding box.CDreactantsFructose-6-phosphate+ ATPAproductsFructose-1,6-biphosphate+ ADPProgress of the ReactionResetHelpD BAcВCEnergy of activation for theforward reaction in theabsence of enzymeEnergy of activation for theforward reactionEnergy of activation for thereverse reaction in absenceAG for the reactionthepresence of enzymeof enzymeEnergy

ΔG for the reaction: ΔG represents the total free energy change of the system, i.e., the free energy…

Answered: Reset Help DBAC AG for the reaction…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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Match the enzymatic activity with the proper description within the ubiquitin-proteasome pathway. Drag and drop options on the right-hand side and submit. For keyboard navigation... SHOW MORE ✓ E1 E2 E3 Proteasome = ||| = ||| = ||| Degradation Ubiquitin-activating enzymes Ubiquitin-conjugating enzymes. Ubiquitin ligases
The clinical symptoms of two forms of galactosemia—deficiency of galactokinase or of UDPglucose: galactose 1-phosphate uridylyltransferase—show radically different severity. Although both types produce gastric discomfort after milk ingestion, deficiency of the transferase also leads to liver, kidney, spleen, and brain dysfunction and eventual death. What products accumulate in the blood and tissues with each type of enzyme deficiency? Estimate the relative toxicities of these products from the above information.
A solution of [U 14C] glucose-1-phosphate (specific activity = 16,000 cpm/mmole) was incubated with glycogen and glycogen phosphorylase, an enzyme which adds glucose units on to glycogen. Radioactivity was incorporated into the glycogen primer at a rate = 2550 cpm/min. The rate of the enzymatic reaction in units of mmole glucose incorporated per minute is: (a) 0.016 mmol/min (b) 0.57 mmol/min (c) 0.16 mmol/min (d) 5.7 mmol/min
Describe the mechanism of action of 1 cycle of the ubiquitin (Ub) ligase system. Describe how the E1, E2 and E3 ligases work to covalently link Ub to the target protein, including which uses an energy source (and how), and the operative amino acids on the enzymes, Ub and target protein
In biochemistry laboratories, phenylmethylsulfonyl fluoride (PMSF) is a serine protease inhibitor commonly added to cell homogenates to protect proteins from digestion form serine proteases that are released when cell membranes and cell organelles are broken. =S-F PMSF: phenylmethylsulfonyl fluoride 1. Based on our discussion of covalent inhibition of acetylcoline, esterase by diisopropylfluorophosphate, predict the effect of PMSF on chymotrypsin and predict how PMSF will modify the chymotrypsin active site. Justify your answer based on the propertied of the active sites of the enzymes.
The enzyme glucose oxidase isolated from the mold Penicillium notatum catalyzes the oxidation of B-D-glucose to D-glucono-6-lactone. The enzyme is highly specific for the B anomer of glucose and does not affect the a anomer. In spite of this specificity, the reaction catalyzed by glucose oxidase is commonly used in a clinical assay for total blood glucose -that is, for solutions consisting of a mixture of B- and a-D-glucose, as well as other sugars present in blood. The oxidation proceeds in the presence of oxygen and forms hydrogen peroxide, in addition to the lactone. A second enzyme, called peroxidase, catalyzes the reaction of hydrogen peroxide with colorless compounds to create a colored product, which is quantified with a simple spectrophotometer. What are the circumstances required to make this possible? Aside from allowing the detection of smaller quantities of glucose, what advantage does glucose oxidase offer over the Fehling's reagent for measuring blood glucose?
The enzyme lysozyme kills certain bacteria by attacking a sugar called N-acetylglucosamine (NAG) in their cell walls. At an enzyme concentration of 2 × 10-6 M, the maximum rate for substrate (NAG) reaction, found at high substrate concentration, is 1 × 10-6 mol L¯'s1. The rate is reduced by a factor of 2 when the substrate concentration is reduced to 6 x 10-6 M. Determine the Michaelis-Menten constants Km and k, for lysozyme.
Consider the complete oxidation of one mole of simple TAG containing behenic acid residues (22:0). I. For one mole of the fatty acid residue, determine the following: d. What is the number of net ATP yield of ATP in the complete oxidation of the fatty acid residue
A. Lineweaver-Burk plot of the enzyme with increasing amounts of substrate in the absence or the presence of the inhibitor is shown below. Graph A : x-intercept Graph B : x-intercept = - 0.012, y-intercept = 0.8 Graph C : x-intercept = - 0.027, y-intercept = 0.8 Graph D : x-intercept = - 0.039, y-intercept = 0.8 - 0.007, y-intercept = 0.8 Graph A 4 Graph B Graph C Graph D 1 -0,04 -0,02 0,00 0,02 0,04 1/[Substrate] (uM) (i) Which graph indicates an enzymatic reaction without inhibitor? (ii) Which type of inhibitor is it? Briefly explain. (iii) Which graph indicates the highest concentration of inhibitor? (iv) Calculate the Vmax and Km of the graph showing an enzymatic reaction with the lowest concentration of inhibitor. Show the steps of calculation and unit in your answers. Keep 2 decimal places in your answers. 1/Rate (umol/min)
Intramitochondrial ATP concentrations are about 5 mM, and phos- phate concentration is about 10 mM. If ADP is five times more abundant than AMP, calculate the molar concentrations of ADP and AMP at an energy charge of 0.85. Calculate AG for ATP hydrolysis at 37 °C under these conditions. The energy charge is the concentra- tion of ATP plus half the concentration of ADP divided by the total adenine nucleotide concentration: [ATP] + 1/2[ADP] [ATP] + [ADP] + [AMP]
Using the appropriate graph and table above, explain what the N426S mutation appears to be doing to the enzyme’s function. Discuss the kinetic parameter changes and their meaning in this context, not the structure of the enzyme, which was not given to you.
Beginning with molecule Y shown above, determine the net ATP equivalents that would be required to add 3 glucose residues to a glycogen primer. Please show your calculations (clearly) also indicate how many molecules of Y would be required to extend the glycogen primer by three glucose residues, so that full credit may be given.

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Reset Help DBAC AG for the reaction Energy of activation for the forward reaction in the Energy of activation for the forward reaction in the presence of enzyme Energy of activation for the reverse reaction in absence of enzyme absence of enzyme