(a)
Interpretation:
The standard energy change for the phosphoglycerate reaction should be calculated
Concept Introduction:
The energy which allows predicting the reaction spontaneously at a particular temperature is called free energy. The reaction which proceed both forward and backward reaction is called as equilibrium constant K.
Answer to Problem 15P
Explanation of Solution
In phosphoglycerate reaction ATP combine with hydrolysis to obtain following equation.
In the first reaction hydrolysis of 1,3-BPG mixes to give
In the second reaction, it is reverse process of hydrolysis of ATP. In this reaction we use opposite value of free energy.
In the coupled reaction free energy stated as
In phosphoglycereate kinase reaction the standard free energy obtained is
(b)
Interpretation:
The equilibrium constant of the reaction should be calculated.
Concept Introduction:
The energy which allows predicting the reaction spontaneously at a particular temperature is called free energy. The reaction which proceed both forward and backward reaction is called as equilibrium constant K
Answer to Problem 15P
Explanation of Solution
Hence
The temperature of the body is
Convert Celsius to Kelvin
Substitute the equation in following formula.
The equilibrium constant for the reaction is
(c)
Interpretation:
The ratio of
Concept Introduction:
The energy which allows predicting the reaction spontaneously at a temperature is called free energy. The reaction which proceed both forward and backward reaction is called as equilibrium constant K
Answer to Problem 15P
Explanation of Solution
The steady state concentration for the reaction is
Concentration ratio for
Substitute the value
Rearrange the equation to get ratio of ATP AND ADP
The ratio of
Want to see more full solutions like this?
Chapter 18 Solutions
Biochemistry
- Need help, please.arrow_forwardNot too sure if my answer is correct.arrow_forwardKINETIC CONSTANT No Na2HPO4 25mM Na2HPO4 50mM Na2HPO4 Vmax nmol p-NP. Min- 20.3252 14.30615 17.30104 Km mM -0.819106 -0.46495 -0.352941 1. What does this suggest about the structure of the active side of the enzyme?arrow_forward
- ENZYME KINETICS ANALYSIS of 6 Xanthine oxidase (XO) is the enzyme that catalyzes the synthesis of uric acid, which in excess causes gouty arthritis. The inhibition of this enzyme is therefore critical in its treatment. A student researcher is investigating the inhibitory effects of kaempferol (Kmp) and chlorogenic acid (Cha) on XO which uses xanthine (Xan) as substrate. Table 1 below shows the enzyme kinetic data. Construct the Lineweaver-Burk plot complete with the linear regression analvsis. Fill in the needed information on Table 2 and paste a copy of your Lineweaver-Burk plot. submit the picture of your output in PNG or JPG format. Table 1. Enzyme Kinetic Data Velocity, mM/s [S], mM Хan Kmp Cha 0.492 0.0678 0.0351 0.0615 0.211 0.0531 0.0261 0.0451 0.087 0.0298 0.0157 0.0211 0.048 0.0195 0.0091 0.0142 0.029 0.0127 0.0067 0.0081 Table 2. Enzyme Kinetic Parameters Xanthine Kaempferol Chlorogenic acid Parameters Vmax Км Type of Inhibition Mode of Binding NA NA Lineweaver-Burk Plotarrow_forwardKinetic Parameters of Enzyme-Catalyzed Reactions TABLE 12-1 The Values of KM, Keat, and Keat/KM for Some Enzymes and Substrates Enzyme Substrate KM (M) 9.5 x 10-5 1.2 x 10-² 2.6 x 10-2 2.5 x 10-2 4.4 x 10-1 8.8 x 10-2 6.6 x 10-4 Acetylcholinesterase Carbonic anhydrase Catalase Chymotrypsin Fumarase Urease Acetylcholine CO₂ HCO₁ H₂O₂ N-Acetylglycine ethyl ester N-Acetylvaline ethyl ester N-Acetyltyrosine ethyl ester Fumarate Malate Urea 5.0 x 10-6 2.5 x 10-5 2.5 x 10-2 Keat (S-¹) 1.4 x 104 1.0 × 106 4.0 × 105 1.0 X 107 5.1 x 10-2 1.7 × 10-1 1.9 X 10² 8.0 x 10² 9.0 × 10² 1.0 X 104 Keat/KM (M¹s¹) 1.5 × 108 8.3 x 107 1.5 x 107 4.0 X 108 1.2 x 10-1 1.9 2.9 × 105 1.6 × 108 3.6 X 107 4.0 X 105 Which enzyme is the most catalytically efficient? Which substrate does chymotrypsin bind to most tightly (assume k_₁ >> K₂)? Is fumarate or malate a better substrate of fumarase? Is it possible to have a kcat/KM of greater than 1 x 10⁹ M-¹ s-¹? Why or why not?arrow_forwardPRESSURE OF A WHAT IS THE asmoTIC SOLUTION OF BOVINE insuLIN (MOLAR MASS, 5700g mol - 1 ) aT 18 °C IF 100.0 ML OF THE SOLUTION conTains 0.103 a OF THE INSULIN?arrow_forward
- Calculation about delta standard G, delta H, detla S. Question attached as photo below. And my answer attempted. Need my answer verified and corrected if neccesary. Please let me know where I got wrong and what key ideas I had miss. Thanks.arrow_forwardO BIOCHEMISTRY Understanding major biochemical energy storage and release. A certain anabolic biochemical reaction A has AG- 17.8 kJ mol , and is always coupled to another reaction B, which has two reactants and two products, I this: R + R2 P + P2 The molecule in the drawing area below is either R, or P. • If it's R, change it into P. But if it's P, change it into R. • In either case, draw the molecule as it would exist at physiological pH. • Also please answer the questions about Reaction B in the table below. OR, Was the molecule in the drawing area R, or P, before you changed it? What is R? Enter its common name, usual symbol, or chemical formula: What is P2? Enter its common name, usual symbol, or chemical formula: O BIOCHEMISTRY Understanding major biochemical energy storage and release.. ODO its common name, usual symbol, or chemical formula: NH, -CH N. H OH OH ...... to IIIarrow_forwardNonearrow_forward
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningBiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage Learning