To explain: The reason that it is not possible to predict whether 14C and 13C are present in the white circular representations of atoms as given in the figure.
Introduction: One of the techniques of detecting the position of atoms and the structure and function of a molecule is based on isotope labeling. It involves both radioactive isotope labeling in which the presence of labels is checked by measuring the amount of radiation emitted from the radioactive isotope upon
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Chapter 9 Solutions
Becker's World of the Cell (9th Edition)
- Draw the structures of two compounds that result from the hydrolysis of phosphatidyl choline in a reaction catalyzed by phospholipase A2. The starting phosphatidyl choline molecule contains a18:0 fatty acid and a 18:2(9,12) fatty acid. You must show the ionization of the products at neutral pH.arrow_forwardPhosphoglycerate mutase transfers a phosphoryl group from C3 of 3-phosphoglycerate to C2 position to give 2-phosphoglycerate. Why is it important to have the phosphoryl group at position 2 rather than at C3? It was observed that the activity of some preparations of the enzyme could be increased if catalytic (very small) amount of 2, 3-bisphosphoglycerate was added to the enzyme. Give a possible explanation for this observation.arrow_forwardA reaction involved in the metabolism of sugars is the splitting of fructose-1,6-diphosphate to give glyceraldehyde-3- phosphate and dihydroxyacetone phosphate. In the living system, this retro-aldol is catalyzed by an enzyme called aldolase; however, it can also be catalyzed by a mild base. Propose a mechanism for the base-catalyzed reaction. CH,-0-P-0- CH,-0-P-0- C=0 C=0 CH,OH dihydroxyacetone phosphate HO-C-H aldolase or "OH H-C-OH H-C-OH H-C-OH CH,-0-P-0- CH2-0-P-0- fructose-1,6-diphosphate glyceraldehyde-3-phosphatearrow_forward
- Consider the following list of phosphorylated compounds with their free energy changes of phosphate hydrolysis: Glucose-1-phosphate (-5.0 kcal/mol), PEP (-14.8 kcal/mole), 1,3-bisphosphoglycerate (-11.8 kcal/mole) and Glucose-6-Phosphate (-3.3 kcal/mol). Given that the free energy change of ATP hydrolysis is -7.3 kcal/mole, which of these molecules be directly synthesized by the transfer of a phospho- group from ATP? 1,3-bisphosphoglycerate Glucose-6-phosphate All of those phosphorylated compounds. PEP Glucose-1-phosphatearrow_forwardExplain the basis for the following statement. For efficient conver- sion of galactose to glucose-1-phosphate, UDP-glucose need be present in catalytic amounts only.arrow_forwardThe isomerization of dihydroxyacetone phosphate (DHAP) to glyceraldehyde 3-phosphate (GAP) is catalyzed by triose phosphate isomerase. In the cell, the concentration ratio of DHAP/GAP = 5.5. Calculate [DHAP] (in M) when [GAP] = 0.00002arrow_forward
- In proteins involved in blood clotting to heal a wound, the amino acid GLU is often chemically modified to carboxy-glutamic acid (abbreviated GLA, shown in diagram at pH 7) by a carboxylase enzyme in the blood. The pKa values for the two ionizable protons in the R-group of GLA are shown. A sample of the octopeptide ILE-GLA-ARG-GLY-MET-ARG-PHE-SER was digested with trypsin, adjusted to pH 13, and applied to an anion exchange column. The peptides were then eluted from the column using a pH gradient from 13 to 0.5. Write the order of the products (no structures required) at the pH they would elute from the column and indicate the pH value. Assume pKa values for any newly generated a-amino and a-carboxyl groups are 9.6 and 2.2 respectively. (Relevant pKa values are 2.2, 3.2, 4.8, 9.6, and 12.5).arrow_forwardThe enzyme Glucose-6-phosphate dehydrogenase catalyzes the nicotinamide adenine dinucleotide oxidation of cyclic glucose-6-phosphate to form the lactone product shown below. Propose a mechanism for this reaction showing all electron flow (using the arrow convention). You must draw the substrate glucose-6-phosphate (the configuration of the anomeric carbon does not matter) and the “business end” of the cofactor.arrow_forwardRefer to the reaction scheme of the GAPDH catalyzed formation of 1,3-BPG. In the reaction, the nucleophile in step (4) is an inorganic phosphate molecule. The enzyme active site is elaborately constructed so that inorganic phosphate, not water, acts as the nucleophile. What advantage is gained by using inorganic phosphate, instead of water, as the nucleophile? Discuss in terms of the energy yield of glycolysis. No need to calculate the total net energy yield of glycolysis.arrow_forward
- Acid phosphatases are an important group of enzymes that can be detected in human blood serum. Under slightly acidic conditions (pH 5.0), this group of enzymes can hydrolyze biological phosphate esters as follows; R-O-P-O3-2+ H 20 OR-OH + HO-P-O3-2. Acid phosphatases are produced and can be detected in erythrocytes, kidney, spleen, the liver, and prostate gland. The enzyme from the prostate gland is clinically important because an increased activity in the blood is frequently an indication of cancer of the prostate gland. Tartrate ion can strongly inhibit the phosphatase from the prostate gland, but not acid phosphatases from other tissues. How can you use the information above to develop a specific procedure for measuring the activity of the acid phosphatase of the prostate gland in human blood serum?arrow_forwardIn the first step of the aldolase reaction, an active site Lys229 residue, with its side chain amino group in the deprotonated state, acts as a nucleophile and attacks the carbonyl C2 carbon of fructose 1,6-bisphosphate to form a Schiff base (boxed in the scheme). Since the pKa of the Lys side chain amino group in free solution is ~10.5, the pKa of Lys229 side chain must have been perturbed to a (higher lower) value for the enzyme to be active at neutral pH. the answer should include sufficient details, including the definition of pKa.arrow_forwardDraw the (B1-->A1) linked dissacharide formed between the C3 epimer of B-D-glucose and the C2 epimer of a-D-galactose. Explain in 1-2 sentences why (or why not) a precipiate would be observed when mixing this dissacharide in an alkaline solution of copper.arrow_forward
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