4. (a) here were collected from a blood analysis for a l-month-old. Which citrate cycle enzyme is defective in this patient? Explain your reasoning. Defects in the citrate cycle are rare but have been described. The data in the table shown Patient (mM/L) 25.5 + 1.2 Control (mM/L) Compound Lactate 1.5 ± 0.3 Fumarate 7.1 ±0.5 < 0.1 Succinate 10.0 ± 1.0 <0.1 0.5 ± 0.2 Malate 4.2 ±0.4 Citrate 5.5 + 1.5 150 ± 25

4. (a) here were collected from a blood analysis for a l-month-old. Which citrate cycle enzyme is defective in this patient? Explain your reasoning. Defects in the citrate cycle are rare but have been described. The data in the table shown Patient (mM/L) 25.5 + 1.2 Control (mM/L) Compound Lactate 1.5 ± 0.3 Fumarate 7.1 ±0.5 < 0.1 Succinate 10.0 ± 1.0 <0.1 0.5 ± 0.2 Malate 4.2 ±0.4 Citrate 5.5 + 1.5 150 ± 25

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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1. Enzyme X has a molecular weight of 35,000 Da. When this enzyme is assayed for enzyme activity, the corresponding line of the double reciprocal plot has the equation y = 75,253X + 102,392. The substrate concentration was in mM and the velocity was measured in mM min". From these data calculate the following: a. KM and Vmax b. kcat if the enzyme concentration was 2 mg/mL. 2. When you run enzyme X from question one on an SDS-PAGE you find that, after Coomassie staining, there is only one band on the gel that runs just below the 20,000 Dalton molecular weight marker. What does this result tell you about the nature of the quaternary structure of your 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?
A bacterial culture is grown using either octadecane (C18H38) or pentachlorophenol (C6HOCl5)) as the sole source of carbon and energy. The cell yield value is determined by dry weight analysis to be 1.49 for octadecane and 0.05 for pentachlorophenol. Using either octadecane or pentachlorophenol, please describe the steps taken (and the final result) showing what percentage of the substrate carbon will be found as cell mass and as CO2? Please show all calculations and give correct answers.
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Calculate the concentration of p-aminophenol control to match the 0.075 % w/w limit in 200 mg/10 ml Your Answer: 0.0015% show work
3. Below is a Michaelis-Menten plot for a wild-type (WT) and mutant (V105A) enzyme isolated from the bacterium Staphylococcus aureus. The enzyme is involved in carbohydrate metabolism and is a potential biocatalyst for the large-scale production of rare sugars. -1 v, μmol s¹ mg-¹ 1.50- 1.25- 1.00- 0.75- 0.50- 0.25- 0.00+ 0 100 → WT 200 300 [s], mM 400 500 → V105A (a) Estimate the Km and Vmax for the wild-type and mutant enzyme from the graph. (b) Calculate the Keat and Keat/Km for the wild-type and mutant enzyme based on your estimated values in (a) if the total enzyme concentration is 0.5 µmol/mg. (c) Is the mutant enzyme a more or less efficient catalyst than the wild-type enzyme? Briefly explain.
3. b. If chymotrypsin is treated with disopropylfluorophosphate, catalysis cannot occur even in the presence of excess substrate concentration. Is this Inhibltion reversible or Irreversible?. Dilsopropylfluorophosphate Hyd
The enzyme, fumarate, has the following kinetic constants: k 1 k 2 k -1 where k 1 = 10 9 M -1 s -1 k -1 =4.4 x 10 4 s -1 k 2 = 10 3 s -1 a. What is the value of the Michaelis constant for this enzyme? b. At an enzyme concentration of 10 -6 M, what will be the initial rate of product"
Please don't provide handwritten solution .....
what is the Vmax and Km of the enzyme in the reaction asap please.
4. a. Use the data in the graph above to estimate a KM value for the enzyme in the presence of these metabolites, and enter them into the table below. b. Classify these metabolites as either activators or inhibitors, and explain your rationale below.
There are parts A-C for this picture included. A) What type of enzyme is Malate Dehydrogenase? choices: Hydrolase, Isomerase, Ligase, Oxideoreductase, Transferase, or Translocase B) Which of the following statements are true in biochemical standard conditions? There can be more than 1. Choices: The reaction is spontaneous since ∆G°' is positive The reaction is spontaneous since ∆G°' is negative The reaction is not spontaneous since ∆G°' is positive The reaction is not spontaneous since ∆G°' is positive The equilibrium favors products since K is greater than 1 The equilibrium favors reactants since K is greater than 1 The equilibrium favors products since K is less than 1 The equilibrium favors reactants since K is less than 1 The reaction is always at equilibrium C) If the concentration of Oxaloacetate is 10^7 times lower than the concentration of Malate D.,Is the reaction Spontanuous? Choices: No, because RTInQ is very positive Yes, because RTlnQ is very…