![Biochemistry](https://www.bartleby.com/isbn_cover_images/9781464126109/9781464126109_largeCoverImage.gif)
Concept explainers
(a)
Interpretation:
The effect of enzyme mutation on enzyme activity with varying concentrations of carnitine must be determined.
The KM and Vmax values of wild-type and mutant enzymes must be determined.
Concept introduction:
Carnitine palmitoyl transferase I is a mitochondrial enzyme, which forms acyl carnitine by catalyzing the reaction between acyl CoA, and l-carnitine. This allows the transfer of fatty acid chain from cytosol to the mitochondria of the cell. there are three isoforms of CPT I enzyme, CPT1A, CPT1B, and CPT1C.
(b)
Interpretation:
The effect of enzyme mutation on enzyme activity with varying concentrations of palmitoyl CoA must be determined.
The KM and Vmax values of wild-type and mutant enzymes must be determined.
Concept introduction:
Carnitine palmitoyl transferase I is a mitochondrial enzyme, which forms acyl carnitine by catalyzing the reaction between acyl CoA, and l-carnitine. This allows the transfer of fatty acid chain from cytosol to the mitochondria of the cell. there are three isoforms of CPT I enzyme, CPT1A, CPT1B, and CPT1C.
(c)
Interpretation:
The enzyme that is more sensitive to malonyl CoA inhibition must be determined.
Concept introductionCarnitine palmitoyl transferase I is a mitochondrial enzyme, which forms acyl carnitine by catalyzing the reaction between acyl CoA, and l-carnitine. This allows the transfer of fatty acid chain from cytosol to the mitochondria of the cell. there are three isoforms of CPT I enzyme, CPT1A, CPT1B, and CPT1C.
(d)
Interpretation:
Effect of 100 µM palmitoyl CoA, 100 µM carnitine, and malonyl CoA 10µM on mutant enzyme and wild type enzyme must be determined.
Concept introduction:
Carnitine palmitoyl transferase I is a mitochondrial enzyme, which forms acyl carnitine by catalyzing the reaction between acyl CoA, and l-carnitine. This allows the transfer of fatty acid chain from cytosol to the mitochondria of the cell. there are three isoforms of CPT I enzyme, CPT1A, CPT1B, and CPT1C.
(e)
Interpretation:
Role of glutamate 3 in CPTI function should be determined.
Concept introduction:
Carnitine palmitoyl transferase I is a mitochondrial enzyme, which forms acyl carnitine by catalyzing the reaction between acyl CoA, and l-carnitine. This allows the transfer of fatty acid chain from cytosol to the mitochondria of the cell. there are three isoforms of CPT I enzyme, CPT1A, CPT1B, and CPT1C.
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Chapter 22 Solutions
Biochemistry
- In the 1950s, Christian Anfinsen demonstrated the renaturation of the protein ribonuclease (RNase) in vitro. After reduction and the addition of urea, the protein was in an unfolded state. After removing the urea and then the reducing agent, the protein oxidized and refolded, with greater than 90% activity. If reducing agent removal occurs before removing the urea, the protein showed less than 5% activity. Why does RNase refold incorrectly if the reducing agent is removed before urea removal? Contaminants in the RNase preparation would form covalent bonds with the protein, preventing reactivation. Urea would participate in weak bonding interactions with RNase, preventing oxidation of cysteine. Disulfide bonds are not positioned correctly unless weak bonding interactions are present. The protein would not fully denature.arrow_forwardA hospital blood processing unit uses apheresis to concentrate red blood cells (RBCs) fromwhole blood donations. Whole blood is drawn from a donor at a rate of 100 g/min and passedthrough a centrifuge-based apheresis system. The whole blood contains 45% RBC and 1%WBCs and platelets by mass, with the remainder consisting of plasma. The separated plasma andnon-RBC components are returned to the donor at a rate of 90 g/min.The goal of the system is to collect a concentrated RBC fraction containing 80% red blood cells.Assume that red blood cells do not break down during processing and that no fluid loss occurs inthe system.(a) How long will it take to collect 100g of the concentrated RBC fraction?arrow_forwardPlease give an intuitive explanation of the blood-brain barrier. Specifically, what is it, what is its structure and function, what types of cells compose it, etc.,..?arrow_forward
- Obtain the sequence for the 5-HT receptor HTR1A and generate a hydropathy plot usingthe ExPASY tool ProtScale, the appropriate window, and the Kyte-Doolittle weightingalgorithm. How many transmembrane domains are present in this receptor?arrow_forwardFrom the reaction data below, determine whether the reaction is first order or second order and calculate the rate constant. Time (s) 0 Reactant (mM) 5.4 1 4.6 2 3.9 3 3.2 4 2.7 5 2.3 Only a plot of In[reactant] versus t gives a straight line, so the reaction is first order . The negative of the slope, k, is 0.171arrow_forwardHair grows at a rate of about 20 cm/yr. All this growth is concentrated at the base of the hair fiber, where a-keratin filaments are synthesized inside living epidermal cells and assembled into ropelike structures. Two-chan 14 Protofilament 20-30 A Two-chain Intermediate flament -Protob Protofilament Cross section of a hair The fundamental structural element of a keratin is the a helix, which has 3.6 amino acid residues per turn and a rise of 5.4 A perlum. 54A (36) Amino terminus Carbon Hydrogen Oxygen Nitrogen group Carboxyl terminus Assuming that the biosynthesis of a helical keratin chains is the rate-limiting factor in the growth of hair, calculate the rate at which peptide bonds of a-keratin chains must be synthesized (peptide bonds per second) to account for the observed yearly growth of hair. 0422 rate of peptide bond formation: Income bonds/sarrow_forward
- Specific rotation is a measure of a solution's capacity to rotate circularly polarized light. The unfolding of the a helix of a polypeptide to a random conformation is accompanied by a large decrease in specific rotation. Polyglutamate, a polypeptide made up of only 1-Glu residues, has the a helix conformation at pH 3. When researchers raise the pH to 7, there is a large decrease in the specific rotation of the solution. Similarly, polylysine (1.-Lys residues) is an a helix at pH 10, but when researchers lower the pH to 7 the specific rotation also decreases, as shown in the graph. a Helix Specific rotation Poly(Glu) a Helix Random conformation Poly(Lys) Random conformation T + ° 2 4 6 В 10 12 14 PH Complete the statements about the molecular mechanism for these changes in specific rotation. Increasing the pH of a polyglutamate solution from 6 to 7 causes the carboxyl group of each glutamate residue Comed Artwer lose a proton. The negatively charged groups in each glutamate residue…arrow_forwardFrom the reaction data below, determine whether the reaction is first order or second order and calculate the rate constant. Time (s) 0 Reactant (mM) 6.2 1 3.1 2 2.1 3 1.6 4 1.3 5 1.1 Only a plot of 1/[reactant] versus t gives a straight line, so the reaction is 0.150 mM-1 s-1 . S second order . The slope, k, isarrow_forwardFrom the reaction data below, determine whether the reaction is first order or second order and calculate the rate constant. Time (s) 0 Reactant (mM) 5.4 1 4.6 2 3.9 3 3.2 4 2.7 5 2.3 Only a plot of In[reactant] versus t gives a straight line, so the reaction is s-1. . The negative of the slope, k, isarrow_forward
- A protein has a molecular mass of 400 kDa when measured by size-exclusion chromatography. When subjected to gel electrophoresis in the presence of sodium dodecyl sulfate (SDS), the protein gives three bands with molecular masses of 180, 160, and 60 kDa. When electrophoresis is carried out in the presence of SDS and dithiothreitol (DTT), three bands again form, this time with molecular masses of 160, 90, and 60 kDa. How many subunits does the protein have, and what is the molecular mass of each? four subunits: 180, 160, 90, and 60 kDa three subunits: 180, 160, and 60 kDa three subunits: 160, 90, and 60 kDa four subunits: 160, 90, 90, and 60 kDa Correct Answerarrow_forwardCalculate KM and Vmax from the following data: KM= i Vmax [S] (μM) vo (mM.s-¹) 0.1 0.34 0.2 0.53 0.4 0.74 0.8 0.91 1.6 1.04 μM mM s-1arrow_forwardPropose a detailed chemical mechanism for the enzyme catalyzed reaction below and briefly note similarities, if any, to enzymes that we've studied. CO2 + CO2 2 CO2 HO CH3arrow_forward
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