questions Flashcards
Dietary recommendations for patients with early stage kidney disease include following a low protein, high carbohydrate diet. What is the metabolic reasoning for such a diet?
In early-stage kidney disease, a low-protein, high-carbohydrate diet is recommended to minimize nitrogen waste production, reduce the kidney’s workload, prevent the breakdown of muscle protein, manage acidosis, and possibly lower the risk of cardiovascular complications. This type of diet helps slow the progression of kidney damage and preserve kidney function for a longer period.
Give FOUR experimental parameters which are varied in the search to grow protein crystals suitable for structural studies
Protein Concentration: Optimized to avoid precipitation and ensure sufficient material for crystal growth (typically 5–20 mg/mL).
Salt Concentration and Type: Adjusted to stabilize the protein and promote crystal formation, typically ranging from 0.1 M to 1.5 M.
pH: Varied to stabilize the protein’s structure, usually in the range of 4.5 to 8.5, depending on the protein.
Temperature: Controlled to balance crystal growth rate, with lower temperatures (4°C–20°C) often improving crystal quality by slowing growth.
Patients with thiamine deficiency have higher levels of pyruvate in the blood. Briefly explain the role of thiamine in cell metabolism, and why blood pyruvate would be elevated in thiamine deficiency.
Thiamine (vitamin B1) is a cofactor for several enzymes involved in cellular metabolism, particularly in the conversion of pyruvate to acetyl-CoA via the pyruvate dehydrogenase complex. Thiamine is also involved in the pentose phosphate pathway and the transketolase enzyme.
In thiamine deficiency, the pyruvate dehydrogenase complex becomes impaired, preventing the conversion of pyruvate to acetyl-CoA. As a result, pyruvate accumulates in the blood because it cannot be efficiently metabolized through the citric acid cycle. This leads to elevated pyruvate levels in the blood, a hallmark of thiamine deficiency.
Briefly explain the role of malonyl-CoA in the regulation of fatty acid synthesis and degradation.
Malonyl-CoA plays a key regulatory role in both fatty acid synthesis and degradation:
Fatty Acid Synthesis: Malonyl-CoA is the primary substrate for fatty acid synthase in the biosynthesis of fatty acids, providing the building blocks for elongation of the fatty acid chain.
Fatty Acid Degradation: Malonyl-CoA inhibits carnitine acyltransferase I (CAT-I), which is involved in transporting fatty acids into the mitochondria for β-oxidation. This prevents fatty acid degradation when synthesis is active.
Thus, malonyl-CoA regulates the balance between synthesis and degradation by promoting one while inhibiting the other.
identify if t or f
All of the intermediates in the TCA cycle carry a phosphate group
FALSE. Not all intermediates in the TCA cycle carry a phosphate group. For example, citrate and isocitrate do not carry a phosphate group
T or F
None of the reactions in the TCA cycle involve molecular oxygen.
TRUE. The TCA cycle itself does not directly involve molecular oxygen. However, oxygen is required in oxidative phosphorylation to regenerate NAD+ and FAD, which are needed for the cycle to continue.
T or F
The coenzyme FADH/FADH2 is required in several of the enzyme-catalyzed steps in the glycolytic pathway.
FALSE. FADH/FADH2 is not used in glycolysis. Glycolysis mainly involves NAD+ as a coenzyme (e.g., in the oxidation of glyceraldehyde 3-phosphate to 1,3-bisphosphoglycerate).
T or F
Two reactions in the TCA cycle lead to the loss of a molecule of carbon dioxide.
TRUE. Two decarboxylation reactions in the TCA cycle release carbon dioxide:
The conversion of isocitrate to α-ketoglutarate (catalyzed by isocitrate dehydrogenase).
The conversion of α-ketoglutarate to succinyl-CoA (catalyzed by α-ketoglutarate dehydrogenase).
T or F
The net gain of ATP from gluconeogenesis is 2 ATP.
FALSE. The net gain of ATP from gluconeogenesis is -4 ATP (it consumes 6 ATP and produces 2 ATP and 2 GTP).
T or F
Only one reaction in the TCA cycle involves substrate-level phosphorylation.
TRUE. The only substrate-level phosphorylation in the TCA cycle occurs during the conversion of succinyl-CoA to succinate, which generates GTP (or ATP, depending on the tissue type).
T or F
Acetyl coenzyme A (AcetylCoA) conveys two carbon atoms from the “link reaction” into the TCA cycle.
TRUE. Acetyl-CoA, produced in the link reaction from pyruvate, donates its two-carbon acetyl group to oxaloacetate, forming citrate to begin the TCA cycle.
T or F
Each of the reactions in the TCA cycle produces a reduced hydrogen carrier.
TRUE. Each turn of the TCA cycle produces reduced coenzymes: 3 NADH, 1 FADH2, and 1 GTP (or ATP). These reduced carriers are essential for the electron transport chain.
Summarise, in your own words, the main steps by which ubiquitin is attached to a target protein.4 mark
Ubiquitination is the process by which a small protein called ubiquitin is attached to a target protein, marking it for degradation by the proteasome. The main steps involved are:
Activation of Ubiquitin: Ubiquitin is first activated by an enzyme called E1 (ubiquitin-activating enzyme), which attaches ubiquitin to itself in an ATP-dependent manner, forming a high-energy thioester bond.
Conjugation: The activated ubiquitin is then transferred to a ubiquitin-conjugating enzyme (E2). This step involves the transfer of ubiquitin from the E1 enzyme to the E2 enzyme.
Ligation: The E3 ubiquitin ligase enzyme facilitates the transfer of the ubiquitin from the E2 enzyme to the target protein. E3 ensures specificity, selecting the appropriate target protein for ubiquitination.
Polyubiquitination: A chain of ubiquitin molecules is often added to the first ubiquitin via isopeptide bonds (specifically between lysine 48 of one ubiquitin and the C-terminal glycine of another). This polyubiquitin chain signals that the target protein should be degraded by the proteasome.
Briefly describe the role of glycogen synthase and Amylo-(1,4 →1,6)-transglycosylase in glycogen synthesis.4marks
Glycogen synthase and Amylo-(1,4 → 1,6)-transglycosylase are both key enzymes in glycogen synthesis:
Glycogen Synthase: This enzyme is responsible for the elongation of the glycogen chain by adding glucose units from UDP-glucose to the non-reducing ends of the growing glycogen molecule. It forms α-1,4-glycosidic bonds, extending the glycogen chain during synthesis.
Amylo-(1,4 → 1,6)-transglycosylase (also known as branching enzyme): This enzyme introduces branch points into the glycogen molecule by transferring a segment of the linear chain (typically 6-7 glucose units) from the α-1,4-glycosidic bond to a hydroxyl group of a glucose residue, forming α-1,6-glycosidic bonds. This creates the characteristic branching structure of glycogen.
Together, these enzymes ensure the synthesis of a highly branched glycogen molecule, which is important for efficient storage and rapid mobilization of glucose.
T or F
Glycogen is a storage polysaccharide that contains two different types of glycosidic linkage.
TRUE. Glycogen is a highly branched polysaccharide made up of glucose units. It contains α-1,4-glycosidic bonds in the linear chain and α-1,6-glycosidic bonds at the branch points.
T or F
The first reaction in glycolysis is phosphorylation by hexokinase or glucokinase.
TRUE. The first step in glycolysis is the phosphorylation of glucose to form glucose-6-phosphate, catalyzed by hexokinase (in most tissues) or glucokinase (in the liver).
T or F
The glycolytic pathway is tightly regulated at the step cataly by the enzyme aldolase.
FALSE. The glycolytic pathway is regulated at three key steps, but aldolase is not one of the regulatory enzymes. The main regulatory steps are catalyzed by hexokinase, phosphofructokinase-1 (PFK-1), and pyruvate kinase.
T or F
All of the enzymes involved in the glycolytic pathway are kinases.
FALSE. While many enzymes in glycolysis are kinases (e.g., hexokinase, phosphofructokinase, pyruvate kinase), not all enzymes are kinases. For example, aldolase is an aldolase enzyme, and enolase is an isomerase.