Interpretation:
A series of steps or a cycle of reactions that could achieve the enrichment of phosphatidylinositol with 1-stearoyl-2-archidonoyl phosphatidylinositol needs to be proposed.
Concept Introduction:
The phosphatidylinositol cycle involves in cell signaling. Its major purpose is to synthesize phosphatidylinositol and its phosphorylated forms. The lipid intermediate of PI cycle are highly enriched with 1-stearoyl-2-arachidnoyl molecular species. This enrichment is retained as long as the intermediates are segregated from other lipids. What happens in the enrichment of a particular phospholipid molecule is selective addition of one specific type of alkyl or the acyl chain. There are several enzymes that involve in the conversion of phospholipids to exhibit specific acyl or alkyl chains.
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Chapter 24 Solutions
Biochemistry
- The compound below, doxorubicin, is a substrate for p-glycoprotein. Cancer cells with a higher expression of P-gp (more P-gp protein per cell) than normal cells were treated with doxorubicin. What would be the expected observation? o= 0= OH O OH HCI OH -OH NH₂ & OH more doxorubicin inside the cell doxorubicin would be oxidized doxorubicin would have more cytotoxic effect on these cancer cells less doxorubicin inside the cellarrow_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_forwardIntramitochondrial ATP concentrations are about 5 mM, and phos- phate concentration is about 10 mM. If ADP is five times more abundant than AMP, calculate the molar concentrations of ADP and AMP at an energy charge of 0.85. Calculate AG for ATP hydrolysis at 37 °C under these conditions. The energy charge is the concentra- tion of ATP plus half the concentration of ADP divided by the total adenine nucleotide concentration: [ATP] + 1/2[ADP] [ATP] + [ADP] + [AMP]arrow_forward
- The reaction catalyzed by phosphorylase is readily reversible in vitro. At pH 6.8, the equilibrium ratio of orthophosphate to glucose 1-phosphate is 3.6. The value of ΔG°’ for this reaction is small because a glycosidic bond is replaced by a phosphoryl ester bond that has a nearly equal transfer potential. However, phosphorolysis proceeds far in the direction of glycogen breakdown in vivo. Suggest one means by which the reaction can be made irreversible in vivo.arrow_forwardWhen hyaluronan synthase from Pasteurella multocida was expressed in E. coli, the bacteria spun out a capsule of hyaluronan. This reaction was analyzed using purified membrane fragments containing the hyaluronan synthase, a radio-labeled tetrasaccharide acceptor (Part A), along with the activated forms of the sugar subunits: UDP-N-acetylglucosamine and UDP-glucuronic acid. In short incubations with the complete mixture, the tetrasaccharide primer elongated by several units, although only odd-numbered chains were visible (Part B lane 2). If one or both activated sugars were left out, the results shown in lanes 3-5 (Part B) were obtained. Why do you suppose that only odd-number chains are visible in your assay? (A) ACCEPTOR nonreducing end HO- HO OH COO glucuronic acid (GICUA) HO- CH3 T C=O I NH CH₂ OH N-acetylglucosamine (GlcNAc) COO но- HO OH OH I CH₂ reducing end NH C=O CH3 Choose one: O A. Synthase adds GlcNAc much more slowly than it adds GICUA. O B. One of the monosaccharide…arrow_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_forward
- Consider a protein with two surface-exposed histidine residues: HisA is a “typical” histidine residue with a pKa = 6.2 HisB is involved in a stabilizing interaction (His-NH+ ..... -O2C-Glu) with a neighboring glutamic acid residue. For HisB, the Gibbs free energy of deprotonation at pH = 7.0 and T = 293K is ΔG'o = +15 kj mol-1. If you had a solution, at pH = 7.0 and T = 293K, containing this protein: a) What fraction of HisA residues are protonated? b) What fraction of HisB residues are protonated? c) What is the pKa of HisB?arrow_forwardDe novo purine biosynthesis is a 10-step pathway that builds the purine rings one atom, or one group of atoms, at a time. The pathway converts 5-phosphoribosyl-1-pyrophosphate (PRPP) to inosine monophosphate (IMP). Identify the nine intermediates on the pathway diagram. 5-phosphoribosyl-1-amine PRPP glycinamide ribonucleotide formylglycinamide rimuclocticke N-succinyl-5-aminoimidazole-4- carboxamide ribonucleotide 5-aminoimidazole-4- carboxamide ribonucleotide Incorrect -CH, H H OH Gn Glu -CH. H 0. CH H glycine + ATP HN HC HC ADP+P OH OH OH 0 -PFI HN (P-Ribose Formy-THF HN THE H HN -Ribose -ATP 6-Ⓡ CH₂ HN HC CH, P-Ribose -ATP ADP+P NH, ADP+P HN NH -Ribose NH, N-formylaminoimidazole-4- carboxamide ribonucleotide formylglycinamidine ribonuclcotide S-aminoimidazole ribonuclotidie ATP ADP+Pi HCO, carboxyanincimidazole ribonucleotide -Ribose H -Ribose H₂O Formyl-THF- ASP Fumarate HC THE 0 N. "NH₂ Ⓒ-Abse NH, NH, -ATP NH -N-CH COO ADP+PI Coo IMP COO NH, 000 Answer Bankarrow_forwardThe reaction in which glucose 6-phosphate (G6P) is converted to fructose 6-phosphate (F6P) is an example of an isomerization reaction. Notice that both molecules have the molecular formula C6H13O9P. The isomerization is catalyzed by glucose 6-phosphate isomerase. This is a reversible reaction in cells, with a moderately negative ΔG, but a very high activation energy. If you have a flask that contains a solution containing cellular concentrations of G6P and F6P, but no enzyme, how will the concentration of each molecule change over time?arrow_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_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_forwardAcetylating agents such as acetic anhydride react preferentially with primaryamines, iodoacetate reacts preferentially with sulfhydryl groups (see Tools of Biochemistry 5B), and ATP-dependent kinases preferentially add a phosphoryl group to side-chain hydroxyl or phenolic —OH groups. Which amino acid side chains, or main-chain groups, in a polypeptide are most likely to be modified by treatment with:(a) acetic anhydride(b) iodoacetate(c) a kinase + ATParrow_forward
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage Learning