As stated in the text, adenosine deaminase deficiency can be treated by injection of the stabilized enzyme. Why might this treatment be effective, while injection of the missing enzyme is ineffective in other conditions, such as HGPRT deficiency or a deficiency of one of the mitochondrial deoxyribo- nucleoside kinases?
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- After being stabilized with supplemental oxygen, a blood transfusion, and medication to help with the pain, JJ was prescribed the drug hydroxyurea to help increase the level of fetal hemoglobin (ay2) in the red blood cell. Though the exact pharmacological effect of hydroxyurea is unclear in the treatment of Sickle Cell Disease, it is known that the drug is an inhibitor of ribonucleotide reductase and acts to transiently inhibit deoxyribonucleotide synthesis in dividing cells. Q5: In which phase of the cell cycle does hydroxyurea produce its main effect?Orotic aciduria results when one of the enzyme activities of UMP synthetase is absent. This syndrome is characterized by large amounts of orotic acid in the blood and urine, megaloblastic anemia (characterized by large, immature , and dysfunctional red blood cells) and retarded growth. Suggest a possible treatment for this condition.A genetic defect in coagulation factor IX causes hemophilia b, a disease characterized by a tendency to bleed profusely after very minor trauma. However, a genetic defect in coagulation factor XI has only mild clinical symptoms. Explain this discrepancy in terms of the mechanism for activation of coagulation proteases shown in Box.
- Thiopurine S-methyltransferase (TPMT) is an enzyme that is responsible for the metabolism of the drugs azathioprine and 6-mercaptopurine, which are used to treat acute lymphoblastic leukemia and inflammatory bowel disease. Metabolism by TPMT reduces the bioavailability of the drugs. In addition to the thiopurine substrates, TPMT also binds S-adenosyl methionine as a cofactor. TPMT is a highly polymorphic enzyme; almost 30 variants are known to be expressed in humans, with most of the variants possessing lower enzymatic activity than the wild-type protein (TPMTwt). Despite having substitutions remote from the active site, TPMT*2 (an A80P variant) and TPMT*5 (an L49S variant) have enzyme activities of 47% and 14% relative to TPMTwt at 18°C, respectively. Two techniques were used to understand the relationships between enzymatic activity and protein stability. Circular dichroism (CD) spectroscopy measures the differential absorption of left and right-circularly polarized light and is used…Orotic aciduria is a rare hereditary disorder due to deficient orotate phosphoribosyltransferase and orotidine-5'-decarboxylase activities that are encoded by Uridylate (UMP) synthetase gene in de novo pyrimidine biosynthesis. The characteristic of this disorder is excessive excretion of orotic acid in urine. A mutation of UMP synthetase gene has been identified as R96G (at amino acid position 96, Arginine is changed to Glycine). In orotic aciduria, predict the consequences of deficient UMP synthetase by identifying which downstream enzyme missing its action. One of important molecules to be derived from pyrimidine biosynthesis is deoxycytidine triphosphate (dCTP) for DNA replication and repair. How is dCTP synthesized, include what enzymes and important intermediates in the pathway? 3. As thymidine triphosphate (dTTP) is needed for DNA replication and repair, what enzymes and intermediates are required to get dTTPA Leu →Ala mutation at a site buried in the core of the enzyme lysozymeis found to be destabilizing. Explain the observed effect of this mutationon lysozyme stability by predicting how enthalpy (ΔH°), conformationalentropy (ΔS°peptide), and the hydrophobic effect (ΔS°solvent) are expected to change for the mutant compared to wild-type lysozyme. Explain how ΔG°for unfolding is affected by your predicted changes in enthalpy or entropy.
- Leigh syndrome is characterized by psychomotor regression: that is, the progressive loss of mental andmovement abilities. Patients also suffer from lacticacidosis, a condition in which mitochondrial respiration is deficient, so their tissues metabolize glucoseanaerobically, leading to the buildup of lactate. Somepatients with Leigh syndrome have a mutation in themitochondrial gene MT-CO3, which encodes a subunit of the electron transport complex cytochromec oxidase. Other patients diagnosed with Leigh syndrome have a loss-of-function mutation in the nucleargene SURF1, which encodes a factor needed for theassembly of this same enzyme complex.a. How can the same symptoms result from mutationsin a mitochondrial gene and from mutations in anuclear gene?A 65-year-old man with severe atherosclerotic coronary artery disease comes to the emergency department because of a 12-hour history of chest pain. Plasma activity of the MB isozyme of creatine kinase (MB-CK) is markedly increased. Which of the following processes is the most likely explanation for the increased plasma MB-CK? (A) Cell membrane damage (B) Endoplasmic reticulum dilation (C) Mitochondrial swelling (D) Polysome dissociation (E) Sodium pump dysfunctionWhich disease occurs when homogentisic acid oxidase is defective?
- Kinases are enzymes that transfer a phosphoryl group from a nucleosidetriphosphate. Which of the following are valid kinase-catalyzed reactions? (a) ADP + CMP → AMP + CDP. (b) AMP + ATP → 2 ADP.In early studies of cultured cells, a respi- ration-deficient mutant of Chinese hamster fibroblasts was found. The respiration rate of the mutant cell line was only 8% of the wild type cell line. It was determined that that all enzymes of the Krebs cycle or Tri- carboxylic Acid Cycle were present in the mutant. Also, absorption spectra of the cy- tochrome content of mitochondria showed no deficit in cytochrome content. Various assays were carried out and results are il- lustrated below. moles 02 consumed / hr/mg protein 2.0) 15 0.5 A Succinate a-glycerol- phosphate 0.4 0.3 0.2 01 4. B Malate Glutamate d-Keto- Isocitrate glutarate (a) Rates of reduction of O2 catalyzed by wild type and mutant mitochondria and supported by oxidation of substrates are compared by the histogram graph on the previous page. Open bars rep- resent Wild Type mitochondria; cross-hatched bars represent the mutant mitochondria. Oxidation of each of the substrates in the two graphs requires a coenzyme. On what…In the case of normal RNase A, Anfisen found that oxidizing the Cys residues before slowly removing the urea gave a very different result than oxidizing the Cys after slowly removing the urea. When the urea was removed first, Anfisen recovered 100% of the catalytic activity. When the urea was removed after oxidation, only about 1% of the activity (1/105) was recovered. The conclusion was that 104 of every 105 molecules was misfolded, and therefore catalytically inactive. Let's say someone raises an objection to this interpretation, and says that perhaps, instead, something chemically happens to the active site of RNase A when it is oxidized before refolding, and that the ~1% activity measured represents the residual and greatly reduced enzyme activity of all of the molecules, and the number is just coincidently similar to 1/105. (In other words, instead of 104 completely inactive molecules for every 1 completely active molecule, all molecules are equally damaged, and only function at…