In humans, the biosynthesis of L-glutamine is catalyzed by the L-glutaminesynthetase. The global reaction can be written as follows:ATP + glutamate + NH3ADP + phosphate + glutamineThe A,Gº' value for this reaction is -16.3 kJ.mol-1 (from left to right).1- Explain the significance this information.2- This reaction can be considered as the sum of two component reactions whichare exergonic and endergonic, respectively, under standard conditions. Writethese two component reactions and evaluate A,Gº of the endergonic reaction.Data: A,Gº of ATP hydrolysis = -30.4 kJ mol-¹

A negative ∆G value for a reaction implies that the reactants, or initial state, have more free…

Answered: In humans, the biosynthesis of…

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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The rate constants of an enzyme-catalyzed reaction, obeying the Michaelis-Menten kinetics, have been determined : E + S K₁ = 2 x 108 M-¹ S-¹ -1 -1 -1 K-₁= 1 x 10³ S K₂ = 5 x 10³ S-1 K₁ 1 K-1 ES K₂ E +P 1- Determine the Michaelis constant Km of the enzyme. 2- Determine the catalytic constant (kcat) of the enzyme. 3- Determine the catalytic efficiency of the enzyme.
Consider an enzyme that follows standard Michaelis-Menten kinetics and has the following kinetic constants: %3| k2 = 1.5 x 10? s1 Еo 3D 1 х 104 М = 1 x 104 M a. What is the value of the maximum rate VM? b. Prepare a hand-drawn quantitative plot on graph paper (not a simple sketch nor an EXCEL-generated graph) of the enzymatic reaction rate versus substrate concentration (like Fig 3-3) using the kinetic parameters given above. Be sure to label the axes and include numeric values on the axes. C. Based upon your hand drawn saturation plot, at what substrate concentration is the enzymatic reaction rate 75% of Vm?
24. Hexokinase catalyzes the phosphorylation of glucose from ATP, yielding glucose-6-P and ADP. The standard-state free energy change for hydrolysis of glucose-6-P is -13.9 kJ/mol. Calculate the standard-state free energy change and equilibrium constant for the hexokinase reaction. AG" for ATP hydrolysis -31.5 kJ/mol
The O2-consumption curve of a dilute, well-buff ered suspension of mito chondria containing an excess of ADP and Pi takes the following form: Sketch the curves obtained when (a) amytal is added at time t = 1 and (b) amytal is added at t = 1 and succinate is added at t = 2.
make a schematic diagram of BChE/AChE inhibitory determination Butyrylthiocholine iodide (BChI), as well as acetylthiocholine iodide(AChI) molecules were utilized as substrate compounds of the reaction. Inthis regard, 5,5′‐dithio‐bis(2‐nitro‐benzoic acid) compound (DTNB) wasused to estimate BChE/AChE activity. In summary, 100 μL Tris buffersolution (HCl, 1.0M, pH 8.0, Tris) and variety of concentrations of thesample solution (50‐200 mL) were added in deionized water and also20 μL of BChE/AChE enzymes solutions added. The mixture was thenincubated for 10 minutes at 20°C. Finally, 50 μL of DTNB (0.5 mM and25 mL) BChI/AChI were added to the incubator mixture. The reactionwas also started by adding 50 μL BChI/AChI. The activity of theseenzymes was evaluated using spectrophotometric spectra with awavelength of 412 nm.
You are working on an enzyme that obeys standard Michaelis-Menten kinetics. Based on the following reaction expression, what is the Km value for this enzyme? E+SESE + P . . . k₁ = 880.8 M-¹5-1 k.₁ = 42.18 S-1 k₂ = 56.29 S-1
what is the Vmax and Km of the enzyme in the reaction asap please.
Provide a reasonable step-wise mechanism for the reaction below, involving TPP as acoenzyme (can abbreviate the pyrophosphate as R), and invoking any general acids or base fromacetolactate synthase that you might need .
Prostaglandins are a group of lipid compounds having diverse hormone-like activities in animals. They are biosynthesized from the fatty acid arachidonic acid, catalyzed by the enzyme cyclooxygenase. The biosynthesis involves via a multistep radical mechanism. Can u show me in a stepwise mechanism how it is converted from radical intermediate A to prostaglandin PGG2.
38. The shown reaction is one of the four repeating steps during fatty acid biosynthesis. Which of the following statements is correct? 유 CH3-C-CH₂-C-S-ACP A B OH 유 CH3-C-CH₂-C-5-ACP → A. The small molecule in box A is NADPH + H* B. It is the second reduction reaction during fatty acid biosynthesis C. Both A and B D. Neither A nor B
Table 1 shows the kinetic data that have been obtained for glucoamylase from Aspergillus niger at different temperatures in the production of glucose from maltodextrin. The rates of reaction measured are using an enzymes concentration of 0.003 μmolml-¹. Table 1: Glucoamylase Activity at different temperatures Maltodextrin Concentration (μmol/L) 0.5 1 1.5 2.2 5.5 11 Initial Reaction Velocity (μmol/L.s) T = 40°C 2.1 3.5 4.9 5.6 589 8.3 9.3 T = 60°C 5.2 9.7 13 16 23 31

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