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Questions and Answers

What is the result of thiamine (vitamin B1) deficiency?

  • Increased activity of pyruvate dehydrogenase
  • Inhibition of enzymes requiring TPP as a coenzyme (correct)
  • Enhanced glucose oxidation
  • Decrease in blood pyruvate levels

What is a common symptom of the disease caused by TPP deficiency?

  • Digestive problems
  • Respiratory issues
  • Neurological and cardiovascular disorder (correct)
  • Skin rashes

What clever chemistry allows living organisms to oxidize acetate in the TCA cycle?

  • Condensation with oxalacetate followed by b-cleavage (correct)
  • Formation of acetyl-CoA without condensing reactions
  • Direct oxidation of acetate without any cleavage
  • Condensation with pyruvate followed by a-cleavage

How can thiamine deficiency be detected in the blood?

<p>Low enzyme activity, especially transketolase (A)</p> Signup and view all the answers

Which food could help treat thiamine deficiency?

<p>Unpolished rice (B)</p> Signup and view all the answers

What is the role of aconitase in the citric acid cycle?

<p>It catalyzes the conversion of citrate to isocitrate. (B)</p> Signup and view all the answers

Why cannot tertiary alcohols be oxidized easily in the citric acid cycle?

<p>They cannot form a carbon-oxygen bond without breaking a carbon-carbon bond. (D)</p> Signup and view all the answers

What type of alcohol is isocitrate classified as?

<p>Secondary alcohol (C)</p> Signup and view all the answers

What is the intermediate formed during the conversion of citrate to isocitrate?

<p>Cis-aconitase (C)</p> Signup and view all the answers

How does citrate interact with citrate synthase in the citric acid cycle?

<p>It acts as a substrate. (D)</p> Signup and view all the answers

What characterizes ATP despite being labeled as a high-energy compound?

<p>It is kinetically stable. (D)</p> Signup and view all the answers

Which of the following best describes the nature of ATP breakdown?

<p>It typically involves synthesis of glucose-6-phosphate. (A)</p> Signup and view all the answers

What does the hexokinase reaction specifically involve?

<p>Nucleophilic attack of glucose on the γ-phosphate of ATP. (C)</p> Signup and view all the answers

What happens to carbon atoms during oxidation in organic compounds?

<p>They lose shared electrons associated with C-H bonds. (A)</p> Signup and view all the answers

What illustrates the term 'high phosphoryl group transfer potential' in ATP?

<p>Strength of phosphate bonds during reactions. (C)</p> Signup and view all the answers

How do carbon atoms become oxidized during the respiratory chain process?

<p>By losing both protons and electrons. (C)</p> Signup and view all the answers

What effect does the nucleophilic attack in hexokinase have?

<p>It facilitates glucose phosphorylation. (B)</p> Signup and view all the answers

Which of the following statements is incorrect about high-energy compounds like ATP?

<p>They are always chemically unstable. (A)</p> Signup and view all the answers

What inhibits the activity of the pyruvate dehydrogenase complex (PDC)?

<p>Acetyl-CoA and NADH (D)</p> Signup and view all the answers

Which enzyme is responsible for the formation of oxaloacetate in the TCA cycle?

<p>Pyruvate carboxylase (B)</p> Signup and view all the answers

Which of the following pathways contributes to replenishing TCA cycle intermediates?

<p>Transamination (A)</p> Signup and view all the answers

Which amino acids are NOT typically associated with the TCA cycle through anaplerotic reactions?

<p>Methionine and Arginine (D)</p> Signup and view all the answers

What is the primary role of the TCA cycle in relation to other metabolic pathways?

<p>Providing precursors for biosynthetic processes (A)</p> Signup and view all the answers

Which compound enters the TCA cycle at the level of succinyl-CoA?

<p>Isoleucine (C)</p> Signup and view all the answers

What is the $ riangle G^o$ value for the hydrolysis of the thioester bond of Acetyl-CoA?

<p>-31.5 KJ/mol (B)</p> Signup and view all the answers

Which functional group is found in the thiazolium ring of thiamine (TPP)?

<p>Thiazole ring (C)</p> Signup and view all the answers

What is succinyl-CoA classified as in the TCA cycle?

<p>A high-energy intermediate (D)</p> Signup and view all the answers

Which phosphorylation occurs with succinyl-CoA in mammals during the TCA cycle?

<p>GDP to GTP (B)</p> Signup and view all the answers

Which molecule is coupled with the formation of GTP in mammals when utilizing succinyl-CoA?

<p>GDP (A)</p> Signup and view all the answers

What is the role of the enzyme succinyl-CoA synthetase in the TCA cycle?

<p>Catalyze the transfer of a phosphoryl group (D)</p> Signup and view all the answers

Which of the following correctly describes the first step in the reaction catalyzed by succinyl-CoA synthetase?

<p>Formation of succinyl phosphate (C)</p> Signup and view all the answers

In which type of organisms does succinyl-CoA lead to ADP being converted to ATP?

<p>Only in plants (C)</p> Signup and view all the answers

What is produced when GTP exchanges its terminal phosphoryl group with ADP?

<p>ATP (C)</p> Signup and view all the answers

Which cofactor is covalently bound to succinate dehydrogenase?

<p>FAD (C)</p> Signup and view all the answers

Which of the following steps takes place after the formation of phosphoryl-His in the reaction catalyzed by succinyl-CoA synthetase?

<p>Transfer of the phosphoryl group to GDP (D)</p> Signup and view all the answers

What is the final product of the reaction involving succinyl-CoA in mammals?

<p>GTP (C)</p> Signup and view all the answers

What is produced during the conversion of succinyl CoA in the TCA cycle?

<p>GTP or ATP (D)</p> Signup and view all the answers

Which molecule is directly generated from isocitrate in the TCA cycle?

<p>a-Ketoglutarate (B)</p> Signup and view all the answers

Which of the following components is oxidized during the conversion of succinate to fumarate?

<p>FAD (D)</p> Signup and view all the answers

What molecule enters the TCA cycle combining with oxaloacetate?

<p>Acetyl CoA (D)</p> Signup and view all the answers

What is the role of NAD+ in the TCA cycle?

<p>It serves as an electron transport molecule. (A)</p> Signup and view all the answers

Which compound is produced from the hydration of fumarate?

<p>Malate (D)</p> Signup and view all the answers

What happens to carbon atoms during the TCA cycle?

<p>They are released in the form of CO2. (B)</p> Signup and view all the answers

Which process is primarily associated with GTP production in the TCA cycle?

<p>Conversion of succinyl CoA (B)</p> Signup and view all the answers

What is the immediate precursor of ATP or GTP in the TCA cycle?

<p>Succinyl CoA (B)</p> Signup and view all the answers

Which coenzyme participates in oxidation during the conversion of succinate?

<p>FAD (D)</p> Signup and view all the answers

What is the role of magnesium ions in the reaction involving ATP investment?

<p>They stabilize the negative charges of the ATP molecule. (A)</p> Signup and view all the answers

Which aspect of ATP is crucial for its function as an energy molecule?

<p>The high phosphoryl group transfer potential. (A)</p> Signup and view all the answers

Why is the nucleophilic attack of glucose on ATP considered irreversible?

<p>It releases a significant amount of energy. (A)</p> Signup and view all the answers

What is the first step in the reaction involving glucose and ATP?

<p>Nucleophilic attack of glucose on the γ-phosphate of ATP. (C)</p> Signup and view all the answers

What aspect of ATP's structure increases its electrophilicity during nucleophilic attack?

<p>The chelation with magnesium ions. (A)</p> Signup and view all the answers

What type of reaction occurs during the conversion of glucose 6-phosphate to fructose 6-phosphate?

<p>Isomerization (B)</p> Signup and view all the answers

What must occur to glucose 6-phosphate before isomerization can take place?

<p>Its cyclic form must be opened. (A)</p> Signup and view all the answers

What characterizes the new carbonyl position after the isomerization of glucose 6-phosphate?

<p>It becomes a ketone at C-2. (D)</p> Signup and view all the answers

What facilitates the subsequent C-C bond cleavage in glycolysis after isomerization?

<p>Activation of C-3. (A)</p> Signup and view all the answers

What distinguishes an aldose from a ketose in the context of carbohydrates?

<p>The position of the carbonyl group. (C)</p> Signup and view all the answers

Which enzyme catalyzes the isomerization of glucose 6-phosphate to fructose 6-phosphate?

<p>Phosphoglucose isomerase (A)</p> Signup and view all the answers

What type of carbon structure is formed from fructose 6-phosphate after the isomerization process?

<p>Five-membered ring (B)</p> Signup and view all the answers

Which functional group is highlighted as becoming a new feature at C-1 after the isomerization of glucose 6-phosphate?

<p>Primary alcohol group (B)</p> Signup and view all the answers

What role does hexokinase play in glucose metabolism?

<p>It phosphorylates glucose, initiating glycolysis. (B)</p> Signup and view all the answers

Which of the following statements is true regarding hexokinases?

<p>Hexokinases consist of tissue-specific isoenzymes. (D)</p> Signup and view all the answers

What is the product of the enzymatic reaction catalyzed by aldolase?

<p>Glyceraldehyde 3-phosphate. (D)</p> Signup and view all the answers

Which enzyme is responsible for the conversion of fructose 6-phosphate to fructose 1,6-bisphosphate?

<p>Phosphofructokinase. (C)</p> Signup and view all the answers

What distinguishes different hexokinases from each other?

<p>Their tissue localization and kinetic properties. (A)</p> Signup and view all the answers

What intermediate is formed during the phosphorylation of glucose?

<p>Glucose 6-phosphate. (C)</p> Signup and view all the answers

What is the main function of phosphoglucoisomerase in glycolysis?

<p>To convert glucose 6-phosphate into fructose 6-phosphate. (B)</p> Signup and view all the answers

Which of the following best describes the glycolytic pathway's initial phase?

<p>It requires the input of ATP. (A)</p> Signup and view all the answers

What is the net yield of ATP per mole of glucose during glycolysis?

<p>2 mol (B)</p> Signup and view all the answers

How many moles of NADH are produced per mole of glucose during glycolysis?

<p>2 mol (A)</p> Signup and view all the answers

What indicates that a reaction is thermodynamically favored during glycolysis?

<p>Negative ΔG (A)</p> Signup and view all the answers

During the ATP-generating phase of glycolysis, how many moles of triose phosphate are formed?

<p>2 mol (A)</p> Signup and view all the answers

What is the change in free energy represented by ΔG in the context of glycolysis?

<p>ΔG = ΔH - TΔS (B)</p> Signup and view all the answers

Which substances are produced alongside 2 moles of pyruvate from the glycolysis of one mole of glucose?

<p>2 NADH and 4 ATP (B)</p> Signup and view all the answers

What characterizes the three large negative standard free-energy changes in glycolysis?

<p>They are all irreversible processes. (D)</p> Signup and view all the answers

Which of the following statements about glycolysis is incorrect?

<p>Glycolysis occurs in the mitochondrial matrix. (B)</p> Signup and view all the answers

What two phosphorylated three-carbon compounds are generated from the aldol cleavage of fructose 1,6-bisphosphate?

<p>Glyceraldehyde 3-phosphate and Dihydroxyacetone phosphate (B)</p> Signup and view all the answers

Which enzyme catalyzes the cleavage of fructose 1,6-bisphosphate into triose phosphates?

<p>Aldolase (A)</p> Signup and view all the answers

What type of reaction mechanism does aldolase utilize in the forward direction?

<p>Aldol cleavage (C)</p> Signup and view all the answers

What role does the lysine ε-amino group play in the aldolase reaction?

<p>Provides nucleophilic attack on the keto carbon (B)</p> Signup and view all the answers

Which of the following correctly describes the activity of aldolase in the metabolic pathway?

<p>Converts DHAP into Glyceraldehyde 3-phosphate (A)</p> Signup and view all the answers

During which phase of glycolysis does aldol cleavage occur?

<p>Energy Investment Phase (C)</p> Signup and view all the answers

Which sugar is isomerized to form Glyceraldehyde 3-phosphate?

<p>Dihydroxyacetone phosphate (C)</p> Signup and view all the answers

What is the main function of aldolase in glycolysis?

<p>To split fructose 1,6-bisphosphate into triose phosphates (D)</p> Signup and view all the answers

What is the primary product of glycolysis after the oxidation of glucose 6-phosphate?

<p>Two pyruvate molecules (D)</p> Signup and view all the answers

Which shuttle is involved in transferring reducing equivalents from cytosolic NADH to the electron-transport chain?

<p>Glycerol 3-phosphate shuttle (B)</p> Signup and view all the answers

What is the net gain of ATP from one molecule of glucose during glycolysis?

<p>Two molecules of ATP (A)</p> Signup and view all the answers

In which cellular location does glycolysis occur?

<p>Cytosol (D)</p> Signup and view all the answers

What is produced as a result of pyruvate oxidation by pyruvate dehydrogenase?

<p>Acetyl-CoA (A)</p> Signup and view all the answers

Approximately how many molecules of ATP can be generated from the complete aerobic oxidation of one molecule of glucose?

<p>30 to 32 mol of ATP (A)</p> Signup and view all the answers

What is the first step in glycolysis that involves the phosphorylation of glucose?

<p>Conversion of glucose to glucose 6-phosphate (D)</p> Signup and view all the answers

How is the reducing equivalent from NADH generated during glycolysis transport across the inner mitochondrial membrane?

<p>Malate-aspartate shuttle or glycerol 3-phosphate shuttle (A)</p> Signup and view all the answers

What type of polysaccharide is cellulose?

<p>Structural polysaccharide (C)</p> Signup and view all the answers

Which form of starch is more branched and preferred for storage in plants?

<p>Amylopectin (D)</p> Signup and view all the answers

What structural linkages characterize glycogen?

<p>1-4 linkages and 1-6 linkages (C)</p> Signup and view all the answers

Why is cellulose indigestible for most animals?

<p>Animals do not have the enzyme to break it down (D)</p> Signup and view all the answers

What is the primary function of starch in plants?

<p>Energy storage (B)</p> Signup and view all the answers

Which form of glucose is primarily found in cellulose?

<p>β-glucose (D)</p> Signup and view all the answers

What distinguishes amylose from amylopectin?

<p>Amylose is linear, while amylopectin is branched (A)</p> Signup and view all the answers

What type of molecules does glycogen primarily serve as in animals?

<p>Energy storage molecules (A)</p> Signup and view all the answers

What does the Km of an enzyme indicate?

<p>The concentration of substrate required to reach half of Vmax (B)</p> Signup and view all the answers

Which type of allosteric interaction occurs when effectors are different from substrate molecules?

<p>Heterotropic interaction (A)</p> Signup and view all the answers

What shape does the plot of an allosteric interaction typically exhibit?

<p>Sigmoid plot (B)</p> Signup and view all the answers

What is the main function of the urea cycle?

<p>Prevent NH4+ toxicity by converting NH4+ to urea (D)</p> Signup and view all the answers

When is Vmax of an enzyme typically achieved?

<p>At an infinite concentration of substrate (C)</p> Signup and view all the answers

Which regulatory mechanism allows for changes in enzyme activity through specific chemical modifications?

<p>Covalent modification (B)</p> Signup and view all the answers

What does a rectangular hyperbola graph represent in enzyme kinetics?

<p>The enzyme's saturation behavior at varying substrate levels (D)</p> Signup and view all the answers

Which of the following best describes the role of isoenzymes?

<p>They catalyze the same reaction but differ in properties and regulation (B)</p> Signup and view all the answers

What happens to the Φ and Ψ angles as the carbonyl or amide nitrogens rotate clockwise?

<p>They increase. (B)</p> Signup and view all the answers

What factors can influence the rotational hindrance of bonds in the backbone?

<p>Size and charge of R groups. (C)</p> Signup and view all the answers

What do aromatic amino acids potentially generate when arranged in a specific way?

<p>Forces leading to stabilization of protein architecture. (B)</p> Signup and view all the answers

In what state can R groups be depending on their environment?

<p>Either protonated or deprotonated based on pH. (A)</p> Signup and view all the answers

What angle is observed when the Φ and Ψ angles are at their maximum in the given conformation?

<p>180°. (B)</p> Signup and view all the answers

What defines the primary roles of metabolism in biological systems?

<p>Generation of energy and synthesis of biological molecules (C)</p> Signup and view all the answers

How do catabolic pathways differ from anabolic pathways?

<p>Catabolic pathways release energy while anabolic pathways consume energy. (B)</p> Signup and view all the answers

What role do the sizes and charges of R groups play in conjunction with single bonds in the backbone?

<p>They influence rotational hindrance. (A)</p> Signup and view all the answers

Which organ primarily provides quick fuel needs for the body?

<p>Liver (D)</p> Signup and view all the answers

Which statement correctly describes the function of aromatic amino acids?

<p>They can be arranged to generate stacking forces. (B)</p> Signup and view all the answers

What role do hormones play in metabolism?

<p>They are used to coordinate and regulate biochemical pathways. (A)</p> Signup and view all the answers

What effect do the properties of R groups have on peptide/protein stability?

<p>They influence the rotational freedom of single bonds. (A)</p> Signup and view all the answers

In which manner do insulin and glucagon interact with metabolic pathways?

<p>They differentially stimulate and inhibit specific pathways. (A)</p> Signup and view all the answers

What is the effect of hormonal signals on metabolic needs across various organs?

<p>They ensure a steady supply of energy while allowing for energy storage. (B)</p> Signup and view all the answers

Which of these hormones is NOT typically involved in regulating metabolism?

<p>Epinephrine (D)</p> Signup and view all the answers

What are the main signals used in the integration of metabolism among organs?

<p>Catecholamines, gluco-corticoids, and growth hormone (D)</p> Signup and view all the answers

What is one advantage of multienzyme complexes in metabolic pathways?

<p>They prevent the loss or dilution of intermediates. (A)</p> Signup and view all the answers

How are enzymes for glycolysis and the citric acid cycle segregated in the cell?

<p>Glycolysis takes place in the cytosol, while the citric acid cycle occurs in the mitochondria. (B)</p> Signup and view all the answers

What is a feature of membrane-bound enzyme systems?

<p>Enzymes must diffuse only in two dimensions. (A)</p> Signup and view all the answers

Which compounds are classified as being in a more reduced state relative to others?

<p>Carbohydrates (B)</p> Signup and view all the answers

What primarily drives biosynthetic reactions in living systems?

<p>Oxidation of organic substrates. (C)</p> Signup and view all the answers

Why is the compartmentalization of metabolic pathways beneficial?

<p>It facilitates the efficiency of biochemical reactions. (B)</p> Signup and view all the answers

Which statement best describes soluble multienzyme systems?

<p>They function independently with diffusing intermediates. (A)</p> Signup and view all the answers

Where are most glycolytic enzymes located in the cell?

<p>Cytosol (B)</p> Signup and view all the answers

Which of the following substances are classified as common nucleophiles in biochemical reactions?

<p>Oxyanions (C)</p> Signup and view all the answers

What is the primary consequence of atoms sharing or transferring valence electrons?

<p>Chemical bonds are formed (D)</p> Signup and view all the answers

What is a key advantage of compartmentalizing metabolic pathways within specific organelles?

<p>It prevents uncontrolled behavior of metabolic processes (A)</p> Signup and view all the answers

Which type of chemical bond is characterized by one atom stripping electrons from another?

<p>Ionic bond (A)</p> Signup and view all the answers

Which statement accurately describes nucleophiles?

<p>They are electron-rich and can form bonds with electrophiles. (C)</p> Signup and view all the answers

What is the role of chemical bonds in the formation of molecules?

<p>They enable atoms to share or transfer electrons. (C)</p> Signup and view all the answers

Which of the following correctly describes a condition following the transfer of an electron between bonding partners?

<p>Ions are formed with complete valence shells. (D)</p> Signup and view all the answers

What is one consequence of selective permeability of membranes in metabolic pathways?

<p>Movement of metabolites can be efficiently controlled. (D)</p> Signup and view all the answers

Flashcards

High-energy compound

A compound that has a high phosphoryl group transfer potential, but is kinetically stable and not unusually reactive.

ATP hydrolysis

The breakdown of ATP, which is usually coupled with other reactions to make them favorable.

Energy coupling

ATP hydrolysis providing energy to drive an unfavorable reaction.

Phosphoryl group transfer potential

The tendency of a phosphoryl group to be transferred to another molecule.

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Hexokinase reaction

The enzyme-catalyzed reaction in which glucose is phosphorylated.

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Nucleophilic attack

An attack on an electrophilic group by a nucleophile.

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Oxidative fates of Pyruvate

Methods of oxidizing Pyruvate either through loss of hydride ion (H-) or reaction with oxygen.

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Loss of hydride ion

A method of oxidation in which a hydride ion (H-) is removed from an organic compound.

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Pyruvate Dehydrogenase Complex Inhibition

Inhibition of the enzyme Pyruvate Dehydrogenase (E1) due to a Thiamine Pyrophosphate (TPP) deficiency, blocking glucose oxidation, and impacting brain function.

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Beriberi Cause

Vitamin B1 (thiamine) deficiency results in TPP deficiency, impacting the function of enzymes needing TPP as a coenzyme. This can lead to Beriberi.

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TPP Deficiency Symptom

A problem in critical processes leading to neurological and heart abnormalities. Also, blood tests reveal increased pyruvate and low enzyme activity.

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TCA Cycle Purpose

The TCA cycle oxidizes acetyl units to CO2. It uses a clever approach to efficiently cleave C-C bonds in acetate, unlike simpler strategies that lack steps to manage the process.

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TCA Cycle's Process Detail

Combining acetate with oxalacetate and performing a targeted C-C cleavage for releasing energy, leading to CO2, regenerating oxalacetate, and creating NADH and ATP.

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Citrate isomerization

Conversion of citrate to isocitrate, a more easily oxidized molecule.

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Aconitase

Enzyme that catalyzes the conversion of citrate to isocitrate.

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Tertiary alcohol

Alcohol where the carbon atom with the hydroxyl group is bonded to three other carbon atoms.

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Isocitrate

A chiral secondary alcohol formed from citrate during the citric acid cycle.

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Citric Acid Cycle

Metabolic pathway that involves the oxidation of citrate to isocitrate.

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Succinyl-CoA

A high-energy intermediate in the TCA cycle used to drive the phosphorylation of GDP to GTP (mammals) or ADP to ATP (plants and bacteria).

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Substrate-level phosphorylation

The direct transfer of a phosphate group from a substrate molecule to ADP or GDP, creating ATP or GTP.

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Succinyl-CoA synthetase

The enzyme responsible for catalyzing the conversion of succinyl-CoA to succinate, generating GTP or ATP in the process.

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High-energy intermediate

A molecule that carries a high amount of potential energy, allowing it to drive other reactions.

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Mixed anhydride

A compound with two different acyl groups linked to a phosphate group.

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Phosphoryl–His

A high-energy intermediate formed during the catalysis of succinyl-CoA synthetase, where a phosphate group is attached to the enzyme's histidine residue.

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Nucleoside diphosphate kinase

The enzyme that catalyzes the reversible transfer of a phosphate group between GTP and ADP, producing ATP and GDP.

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Succinate dehydrogenase

An enzyme that catalyzes the oxidation of succinate to fumarate in the TCA cycle, using FAD as a coenzyme.

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FAD (Flavin Adenine Dinucleotide)

A coenzyme involved in electron transport, which can accept two electrons and two protons.

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How is Succinyl-CoA used to drive the phosphorylation of GDP or ADP?

Succinyl-CoA, a high-energy intermediate, drives the phosphorylation of GDP or ADP by releasing energy during its conversion to succinate. This energy is then used to attach a phosphate group to GDP or ADP, forming GTP or ATP respectively.

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What is the TCA cycle?

The tricarboxylic acid cycle (TCA cycle), also known as the Krebs cycle, is a series of chemical reactions used by aerobic organisms to generate energy through the oxidation of acetate derived from carbohydrates, fats, and proteins into carbon dioxide. It is a central metabolic pathway in all aerobic organisms.

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What is the starting molecule of the TCA cycle?

Acetyl CoA, a two-carbon molecule, is the starting molecule of the TCA cycle. It is formed from the breakdown of pyruvate, which is a product of glycolysis.

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What is the role of oxalacetate?

Oxalacetate is a four-carbon molecule that combines with acetyl CoA to start the TCA cycle. It is regenerated at the end of the cycle, allowing for the continuous operation of the cycle.

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What are the products of the TCA cycle?

The TCA cycle produces high-energy electron carriers like NADH and FADH2, which are used in oxidative phosphorylation to generate ATP, the primary energy currency of cells. The cycle also produces carbon dioxide as a waste product and GTP, a high-energy molecule.

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How many ATP are produced per glucose molecule in the TCA cycle?

The TCA cycle directly produces 1 ATP (or GTP, which is interchangeable with ATP) per glucose molecule. However, it produces 3 NADH and 1 FADH2 which further generate a significant amount of ATP in the electron transport chain.

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What is the significance of NADH and FADH2?

NADH and FADH2 are electron carriers that are produced during the TCA cycle and other metabolic processes. They are essential for oxidative phosphorylation, where they donate their electrons to the electron transport chain, leading to the generation of a proton gradient and ultimately ATP.

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Where does the TCA cycle take place?

The TCA cycle takes place in the mitochondrial matrix of eukaryotic cells. Mitochondria are often referred to as the "powerhouses" of the cell because they are responsible for the production of ATP.

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What is oxidative phosphorylation?

Oxidative phosphorylation is the process of converting the energy stored in the electron carriers NADH and FADH2 into ATP through a series of protein complexes embedded in the mitochondrial membrane.

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How is the TCA cycle regulated?

The TCA cycle is regulated by a variety of factors, including the availability of substrates (acetyl CoA and oxalacetate), the level of ATP, and the ratio of NADH to NAD+. This ensures that the cycle is only active when energy is needed and when substrates are available.

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PDC Inhibition

The Pyruvate Dehydrogenase Complex (PDC) can be inhibited by its products, NADH and Acetyl-CoA, which compete with NAD+ and CoA in the reaction steps. This feedback mechanism prevents the overproduction of Acetyl-CoA and slows down the pathway when sufficient energy is already produced.

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Anaplerotic Pathways

These pathways replenish intermediates of the TCA cycle, ensuring its continuous operation even when intermediates are withdrawn for biosynthesis. These pathways are essential for maintaining the flow of the cycle and providing necessary building blocks for other metabolic processes.

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Pyruvate Carboxylase

This enzyme converts pyruvate to oxaloacetate, a key intermediate in the TCA cycle. It plays a major anaplerotic role, replenishing oxalacetate when it is used for biosynthesis or other pathways.

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TCA Cycle Provides Intermediates

Besides energy production, the TCA cycle provides essential intermediates for various biosynthetic pathways. For example, oxaloacetate is used in gluconeogenesis, α-ketoglutarate in amino acid synthesis, and succinyl-CoA in heme synthesis.

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Acetyl-CoA Thioester Bond Hydrolysis

The breakdown of the thioester bond in Acetyl-CoA releases a significant amount of energy (-31.5 KJ/mol). This energy is harnessed to drive other metabolic reactions, making it a high-energy compound.

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TPP in Thiazolium Ring

Thiamine pyrophosphate (TPP) is a coenzyme used by pyruvate dehydrogenase. It contains a thiazolium ring with a functional group called a carbanion, which is crucial for the enzyme's catalytic activity.

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TCA Cycle - Energy Production

The TCA cycle efficiently oxidizes acetyl units (from carbohydrates, fats, and proteins) to carbon dioxide, releasing energy in the process. This energy takes the form of high-energy electron carriers (NADH and FADH2), which are then used to generate ATP in oxidative phosphorylation.

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TCA Cycle's Clever Approach

Unlike simpler strategies that directly oxidize acetate to carbon dioxide, the TCA cycle uses a sophisticated series of reactions to cleave C-C bonds. This allows for efficient energy extraction from acetate, avoiding the need for simpler, but less efficient, methods.

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Glycolysis

The breakdown of glucose into pyruvate, generating a small amount of ATP and NADH. This process occurs in the cytosol of cells.

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TCA Cycle

A series of reactions that oxidizes acetyl-CoA to CO2, generating ATP, NADH, and FADH2. This cycle takes place in the mitochondrial matrix.

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Pyruvate Dehydrogenase

An enzyme complex that converts pyruvate to acetyl-CoA, linking glycolysis to the TCA cycle. Its activity is regulated by product levels.

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NADH and FADH2

Electron carriers produced during glycolysis and the TCA cycle. They transfer electrons to the electron transport chain for ATP synthesis.

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Electron transport chain

A series of protein complexes in the mitochondrial membrane that uses energy from electrons to pump protons, driving ATP synthesis.

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Anaplerotic reactions

Reactions that replenish intermediates of the TCA cycle, ensuring its continuous operation. They prevent depletion of key compounds.

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Oxidation

A chemical process that involves the loss of electrons. In metabolism, oxidation often results in energy release.

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Why is Mg2+ needed in the first ATP investment?

Magnesium ion (Mg2+) is essential for the first ATP investment in glycolysis because it chelates to ATP, neutralizing the negative charges on the oxygen atoms. This makes the γ-phosphorus atom a better electrophile, more susceptible to nucleophilic attack by the C6-OH group of glucose.

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What's the role of the γ-phosphorus atom in the first ATP investment?

The γ-phosphorus atom of ATP is the electrophilic center that is attacked by the C6-OH group of glucose. This nucleophilic attack initiates the phosphorylation of glucose, a key step in glycolysis.

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What does the first ATP investment in glycolysis achieve?

The first ATP investment in glycolysis generates glucose-6-phosphate from glucose. This phosphorylation step is irreversible and sets the stage for the further breakdown of glucose in the glycolytic pathway.

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Why is the first ATP investment considered 'exergonic'?

The first ATP investment in glycolysis is exergonic because the hydrolysis of the γ-phosphate bond in ATP releases energy, driving the phosphorylation of glucose. This energy release means the reaction is spontaneous.

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How does ATP become more reactive in the first ATP investment?

ATP becomes more reactive when it forms a complex with Mg2+. The Mg2+ ion neutralizes the negative charges on ATP's phosphate groups, making the γ-phosphorus atom more susceptible to nucleophilic attack.

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Hexokinase Family

A group of enzymes that phosphorylate glucose, differing in their kinetic properties and tissue specificity.

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Energy Investment Phase

The initial steps of glycolysis, where ATP is consumed to prepare glucose for later energy extraction.

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Glucose 6-Phosphate

The first phosphorylated form of glucose, generated by hexokinase, trapping it inside the cell.

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Fructose 1,6-Bisphosphate

A crucial intermediate in glycolysis, formed by aldolase, committing glucose to energy production.

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Isomerase

An enzyme that converts one isomer to another, rearranging the molecule's structure.

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Aldolase

An enzyme that splits fructose 1,6-bisphosphate into glyceraldehyde 3-phosphate and dihydroxyacetone phosphate.

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Glyceraldehyde 3-Phosphate (G3P)

A three-carbon sugar phosphate, one of the products of aldolase, central to the energy-producing stage.

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Dihydroxyacetone Phosphate (DHAP)

A three-carbon sugar phosphate, another product of aldolase, converted to G3P for further metabolism.

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Glucose 6-Phosphate Isomerization

The conversion of glucose 6-phosphate (an aldose) to fructose 6-phosphate (a ketose) by the enzyme phosphoglucose isomerase.

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Why Isomerize Glucose 6-Phosphate?

Isomerization is essential because it creates a new primary alcohol at carbon 1, making it easily phosphorylated. It also activates carbon 3, facilitating the later cleavage of the C-C bond in glycolysis.

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Cyclic Forms of Sugars

Glucose 6-phosphate and fructose 6-phosphate primarily exist in cyclic forms. The enzyme must first open the ring, catalyze the isomerization, and then close the ring again.

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Aldose to Ketose

Isomerization of glucose 6-phosphate to fructose 6-phosphate converts an aldose (aldehyde group) to a ketose (ketone group).

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Phosphoglucose Isomerase

The enzyme that catalyzes the isomerization of glucose 6-phosphate to fructose 6-phosphate. It's essential for glycolysis.

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Primary Alcohol at Carbon 1

The isomerization creates a new primary alcohol group at carbon 1 of fructose 6-phosphate, making it easily phosphorylated in the next step of glycolysis by phosphofructokinase-1.

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Activation of Carbon 3

Isomerization activates carbon 3 of fructose 6-phosphate, making it easier to break the C-C bond between carbons 3 and 4 in the fourth step of glycolysis.

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Glycolysis's First Step

The isomerization reaction is an important early step in glycolysis, a metabolic pathway that breaks down glucose to produce energy.

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Aldolase Cleavage

The enzyme aldolase breaks down fructose 1,6-bisphosphate into two 3-carbon molecules: dihydroxyacetone phosphate (DHAP) and glyceraldehyde 3-phosphate (G3P).

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Aldol Cleavage Mechanism

Aldolase uses a lysine ε-amino group to activate the keto carbon at position 2 of fructose 1,6-bisphosphate, making it susceptible to nucleophilic attack, leading to the cleavage reaction.

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Aldolase's Dual Roles

The aldolase enzyme catalyzes both aldol cleavage in the forward reaction and aldol condensation in the reverse reaction.

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Keto Carbon

A carbon atom in a molecule that is double-bonded to an oxygen atom and single-bonded to two other groups, creating a ketone functional group.

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Lysine ε-Amino Group

A specific side chain of the amino acid lysine that contains an amino group capable of acting as a nucleophile and participating in enzyme reactions.

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Glycolysis: Energy Yield

The breakdown of one glucose molecule produces a net yield of 2 ATP, 2 NADH, and 2 pyruvate.

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Irreversible Steps in Glycolysis

The 10 steps of glycolysis include 3 irreversible steps, which are crucial for regulating the pathway.

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Thermodynamically Favored Reactions

Reactions with a negative free energy change (∆G) are thermodynamically favored and release energy.

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NADH: Electron Carrier

NADH is a reduced form of nicotinamide adenine dinucleotide (NAD+), carrying electrons that will be used in the electron transport chain.

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Pyruvate: End Product of Glycolysis

Pyruvate is a three-carbon molecule, the final product of glycolysis. It can then be used in aerobic or anaerobic respiration.

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Importance of Substrate-Level Phosphorylation

This process directly transfers a phosphate group from a substrate to ADP, producing ATP without the need for electron transport.

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Regulation of Glycolysis

The irreversible steps in glycolysis are regulated by various factors, ensuring the pathway only operates when needed.

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Cellulose Structure

A linear polysaccharide made of β-glucose subunits linked by 1-4 glycosidic bonds, found in the cell walls of plants.

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Starch

An energy storage polysaccharide found in plants, composed of α-glucose subunits linked by 1-4 glycosidic bonds. It exists in two forms: amylose (linear) and amylopectin (branched).

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Amylose vs Amylopectin

Amylose is a linear, helical form of starch, while Amylopectin is a branched form with additional 1-6 glycosidic bonds. Amylopectin is the preferred storage form.

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Glycogen

An energy storage polysaccharide found in animals, composed of α-glucose subunits linked by 1-4 and 1-6 glycosidic bonds (branched).

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Why is Cellulose Indigestible?

Most animals lack the enzyme necessary to break down the β-1,4 glycosidic bonds in cellulose.

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What is the Difference Between Starch and Glycogen?

Both starch and glycogen are α-glucose polymers, but glycogen has more branching which allows for faster energy release in animals.

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Polysaccharide Function

Polysaccharides serve as structural components (cellulose) or energy storage molecules (starch and glycogen) in organisms.

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α vs β Glucose

α-glucose and β-glucose differ in the orientation of the hydroxyl group on carbon 1, leading to different polysaccharide structures and functions.

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Rotationally Hindered Bonds

Single bonds in the protein backbone can be restricted from free rotation due to the size and charge of the side chains (R groups) attached to them.

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Φ and Ψ Angles

These angles describe the rotation around the two single bonds of the peptide backbone, defining a protein's 3D structure.

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Aromatic Amino Acids Stacking

Aromatic amino acids, like phenylalanine and tyrosine, can stack on top of each other, creating hydrophobic interactions that stabilize protein structure.

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Protonation/Deprotonation of Amino Acids

The side chains of amino acids can gain or lose protons, changing their charge and influencing protein structure and function.

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pH Dependence of Amino Acid Charge

The protonation state of amino acid side chains depends on the pH of the environment, affecting their interactions and function.

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Conformational Flexibility of the Backbone

The peptide backbone can adopt different conformations, driven by the size and charge of the side chains and interactions with the surrounding environment.

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Force Generation from Amino Acid Interactions

Interactions between amino acids can generate forces that shape the protein structure, contributing to its overall function.

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Architecture and Stability of Peptides/Proteins

The specific arrangement of amino acids determines the protein's architecture and stability, influencing its biological activity.

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Michaelis-Menten Equation

This equation describes how an enzyme's activity changes with varying substrate concentrations. It relates the initial velocity (vi) to the substrate concentration [S] and two important parameters: Km and Vmax.

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Km (Michaelis Constant)

The substrate concentration required for an enzyme to reach half its maximum velocity (Vmax). It reflects the enzyme's affinity for the substrate.

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Vmax (Maximum Velocity)

The highest velocity an enzyme can achieve when fully saturated with substrate. It represents the theoretical limit of the enzyme's catalytic activity.

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Allosteric Regulation

A type of enzyme regulation where a molecule binds to a site other than the active site, influencing the enzyme's activity.

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Heterotropic Allostery

A type of allosteric regulation where the effector molecule is different from the substrate molecule.

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Homotropic Allostery

A type of allosteric regulation where the binding of one substrate molecule to an active site influences the binding of other substrate molecules to the same enzyme.

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Sigmoid Curve

The characteristic curve that describes the relationship between substrate concentration and enzyme activity in allosteric enzymes.

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Feedback Control

A type of regulation where the product of a metabolic pathway inhibits an earlier enzyme in the pathway, preventing overproduction.

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Catabolic Pathway

A metabolic pathway that breaks down complex molecules into simpler ones, releasing energy.

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Anabolic Pathway

A metabolic pathway that builds complex molecules from simpler ones, requiring energy.

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Metabolic Map

A diagram that illustrates the interconnected pathways of metabolism, showing how different molecules are broken down and synthesized.

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Liver's Role in Metabolism

The liver acts as a central metabolic hub, providing quick fuel (glucose) and regulating blood glucose levels.

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Adipose Tissue's Role in Metabolism

Adipose tissue stores energy in the form of fat for long-term use.

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Insulin and Glucagon

Hormones that regulate blood glucose levels by influencing metabolic pathways.

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Energy-Rich Compounds

Molecules that store a high amount of potential energy, such as ATP, which can be released to drive other reactions.

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Catabolism and Anabolism

Two opposing metabolic processes that work together: catabolism breaks down molecules to release energy, while anabolism builds molecules using energy.

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Nucleophiles

Electron-rich compounds that readily form covalent bonds with electron-deficient centers.

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Common Nucleophiles in Biochemistry

Oxyanions, carbanions, deprotonated amines, and the imidazole side chain of histidine are common nucleophiles in biochemical reactions.

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Chemical Bonds

Attractions that hold atoms together in molecules, resulting from the sharing or transfer of valence electrons.

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Covalent Bonds

Bonds formed by the sharing of valence electrons between atoms.

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Ionic Bonds

Bonds formed by the transfer of electrons from one atom to another, resulting in charged ions.

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Nucleophilic Substitution

A chemical reaction where a nucleophile replaces another atom or group in a molecule.

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Compartmentalization in Metabolism

Organizing metabolic pathways within specific organelles to regulate reactions, restrict diffusion, and control metabolite movements.

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Metabolic Functions of Eukaryotic Organelles

Different organelles in eukaryotic cells are responsible for specific metabolic processes, like energy production, protein synthesis, and detoxification.

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Multienzyme Systems

A group of enzymes working together to catalyze a metabolic pathway. They can be organized as separate, diffusing enzymes or as a complex with the substrate passing from one enzyme to another.

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TCA Cycle Location

The TCA cycle occurs in the mitochondrial matrix, the inner space of mitochondria.

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Oxidation of Organic Substrates

Living systems obtain energy by oxidizing organic molecules, like fats and carbohydrates.

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State of Reduction

Reduced molecules have more electrons and hydrogen atoms (e.g., fats), while oxidized molecules have fewer electrons and more oxygen atoms (e.g., CO2).

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Glycolysis End Product

Pyruvate is the 3-carbon molecule produced at the end of glycolysis.

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Study Notes

Tricarboxylic Acid (TCA) Cycle

  • The TCA cycle, also known as the Krebs cycle or citric acid cycle, is a crucial part of cellular respiration.
  • It's a cyclical series of biochemical reactions that oxidizes the acetyl group from acetyl-CoA to carbon dioxide (CO2).
  • The cycle regenerates oxaloacetate, starting the cycle again.
  • It generates high-energy electron carriers (NADH and FADH2) and a small amount of ATP (GTP).
  • The TCA cycle is an amphibolic pathway, meaning it plays a role in both catabolic (breakdown) and anabolic (synthesis) processes.
  • Key enzymes in the cycle are: citrate synthase, aconitase, isocitrate dehydrogenase, α-ketoglutarate dehydrogenase, succinyl-CoA synthetase, succinate dehydrogenase, fumarase, and malate dehydrogenase.
  • The cycle takes place in the mitochondrial matrix.
  • Pyruvate dehydrogenase complex connects glycolysis and the TCA cycle by converting pyruvate to acetyl-CoA.
  • Anaplerotic reactions replenish TCA cycle intermediates like oxaloacetate.

Energy Transformations in Fuel Metabolism

  • Phase 1 of respiration involves the oxidation of fuels (glucose, fatty acids, amino acids), transferring electrons.
  • Coenzymes NAD+ and FAD accept the transferred electrons, forming NADH and FAD(2H) respectively.
  • Phase 2 of respiration generates ATP through oxidative phosphorylation using the energy from the high-energy electron carriers (NADH and FAD(2H)).

Overview of Glycolysis and Important Reactions

  • Glycolysis is an anaerobic process that converts glucose into pyruvate.
  • Important reactions like hexokinase, phosphofructokinase, and pyruvate kinase are involved in these conversions.
  • ATP is required in glycolysis, but a net gain of 2 ATP is yielded.
  • These reactions take place in the cytosol.

Oxidative Fates of Pyruvate and Nicotinamide Adenine Dinucleotide

  • Aerobic glycolysis utilizes pyruvate to make Acetyl CoA to enter the TCA cycle.
  • Anaerobic glycolysis converts pyruvate into lactate.
  • Oxidation of organic compounds either involves loss of hydride ions (H−) or combining with oxygen.
  • Enzymes called dehydrogenases are responsible for these oxidation reactions.

Anaerobic Conversion of Pyruvate to Ethanol

  • Yeast cells convert pyruvate to ethanol and CO2 in the absence of oxygen.
  • Two reactions are necessary. One being decarboxylation to pyruvate then to acetaldehyde, and the other being alcohol dehydrogenase reducing acetaldehyde to ethanol.
  • This process regenerates NAD+ from NADH allowing glycolysis to continue.

The Citric Acid Cycle and What We Will Learn Today

  • The citric acid cycle (TCA cycle) is a cyclical process.
  • The cycle interconnects glycolysis and pyruvate dehydrogenase complex.
  • The cycle's reactions and the enzymes involved in the reactions.
  • Regulation of TCA cycle activity.
  • Anaplerotic reaction that replenishes TCA cycle intermediates.

The Loci of Substrate-Level Phosphorylation

  • Substrate-level phosphorylation occurs in the cytosol during glycolysis and in the mitochondrion during the TCA cycle.
  • Electrons are transferred via NADH and FAD(2H) in these processes.

Conversion of Pyruvate to Acetyl-CoA by Oxidative Decarboxylation

  • The conversion is carried out by the pyruvate dehydrogenase complex (PDC), a multi-enzyme complex.
  • The PDC requires five cofactors: TPP, lipoic acid, CoA, FAD, and NAD+.
  • The reaction takes place in the mitochondrial matrix.

Acetyl-Coenzyme A (Acetyl-CoA)

  • Acetyl-CoA carries acetyl groups for metabolic processes.
  • It's a high-energy molecule that releases free energy for cellular reactions.
  • The common product of breakdown of carbohydrate, fatty acids, and amino acids.

Comparison of Free Energies of Hydrolysis of Thioesters and Oxygen Esters

  • Thioesters are more favorable for hydrolysis than oxygen esters.
  • Lack of resonance stabilization in thioesters is why their hydrolysis is more favorable compared to oxygen esters.

Conversion of Pyruvate to Acetyl-CoA by Oxidative Decarboxylation (Alternative)

  • Pyruvate Dehydrogenase Multienzyme Complex (PDC) catalyzes the conversion.
  • The PDC has three enzymes: E1 (pyruvate dehydrogenase), E2 (dihydrolipoyl transacetylase), and E3 (dihydrolipoyl dehydrogenase).
  • Five cofactors are needed: TPP, lipoic acid, CoASH, FAD, NAD+.
  • Occurs in the mitochondrial matrix.

Structural Organization of the E. coli PDC

  • PDC is a multi-enzyme complex with a structure (E1, E2, E3) core. The structure is important to understand the mechanism in which they work together.

The Coenzymes and Prosthetic Groups of PDC

  • Different coenzymes within the PDC facilitate different reaction steps, with TPP, lipoic acid, CoA (respectively E1, E2), and FAD & NAD+ (in E3) involved in specific parts and steps.
  • The roles of TPP and lipoic acid.
  • The role of CoA and FAD
  • The role of NAD+ within the complex.

Interconversion of Lipoamide and Dihydrolipoamide

  • Lipoamide is a cofactor involved in the conversion of lipoic acid in the PDC complex, and crucial to the process.

Thiamine Pyrophosphate (TPP)

  • TPP is a cofactor of pyruvate dehydrogenase complex.
  • It's involved in decarboxylation of pyruvate and transfer of a two-carbon unit.

TPP in the Pyruvate Dehydrogenase Reaction

  • TPP plays a key role in the pyruvate dehydrogenase reaction, accepting the activated two-carbon unit of pyruvate, then transferring to an intermediate then to the next cofactor, CoA, which then becomes acetyl CoA.
  • The pyruvate dehydrogenase reaction, and each step is essential in order for the entire process to happen.

Malfunction of Pyruvate Dehydrogenase Complex: TPP Deficiency

  • TPP deficiency inhibits pyruvate dehydrogenase complex activity.
  • Symptoms of TPP deficiency include neurological and cardiovascular disorders.
  • Deficiency can be diagnosed by testing the levels of pyruvate in the blood.

TCA Cycle Provides a Way of Cleaving a Two-Carbon Compound

  • The TCA cycle provides a means to oxidize the acetyl group of acetate and convert to CO2, which requires C-C cleavage.
  • There is a chemical basis for the complexity of apparent oxidation of acetate units to carbon dioxide (CO2).

The Concept of the TCA (Krebs) Cycle

  • The TCA cycle involves eight steps, each catalyzed by a specific enzyme.
  • The acetyl group from acetyl-CoA joins the cycle by combining with oxaloacetate to make citrate.
  • The cycle then regenerates oxaloacetate through the subsequent steps.
  • The NADH and FADH2 produced the cycle carry electron energy for electron transport chain.

Formation of Succinyl-CoA (Alternative)

  • The process involves a series of redox reactions and decarboxylations ultimately creating Succinyl-CoA.

Mechanism of the NAD+-Dependent Isocitrate Dehydrogenase

  • The reaction involves a series of redox steps leading to release of CO2 and the oxidation of an alcohol to form a keto-group.
  • The isocitrate dehydrogenase reaction uses Mn2+ (or Mg2+) to coordinate and facilitate the catalytic process.

Mechanism of the NAD+-Dependent α-Ketoglutarate Dehydrogenase

  • This reaction catalyzes the oxidative decarboxylation of α-ketoglutarate to form succinyl-CoA using 5 cofactors: TPP, lipoic acid, CoASH, FAD&NAD+.

Mechanism of the Succinyl-CoA Synthetase

  • The enzyme catalyzes substrate-level phosphorylation.
  • Succinyl-CoA is phosphorylated converting GTP to GDP, or ADP to ATP.
  • This is an essential process producing high-energy compounds.

Reactions Catalyzed by Succinyl-CoA Synthetase

  • This enzyme catalyzes the formation and conversion of succinyl-phosphate, then a phosphoryl-His intermediate and finally product GTP through a series of intermediate steps, using GDP.

Standard Free Energy Changes (ΔG') and Physiological Free Energy Changes (ΔG) of Citric Acid Cycle Reactions

  • The enzyme and reactions involved in each cycle step and their corresponding standard free energy changes values.
  • Standard and physiological free-energy changes for individual TCA cycle reactions.

Major Regulatory Interactions in the TCA Cycle

  • The rate of ATP hydrolysis regulates the rate of NADH oxidation.
  • ADP and NADH provide feedback to control the TCA cycle.
  • Isocitrate dehydrogenase, α-ketoglutarate DH, and malate DH are affected by changes in NADH concentration.
  • Citrate inhibits citrate synthase.
  • ADP and Ca2+ concentration activates isocitrate and α-ketoglutarate DH.

Factors Controlling the Activity of the PDC

  • Feedback of NADH and acetyl-CoA.
  • Production inhibition of a key reactant, pyruvate.

Anaplerotic Pathways to Replenish TCA Cycle Intermediates

  • Anaplerotic reactions replenish TCA cycle intermediates.
  • Key reactions like pyruvate carboxylase and transamination.
  • The importance of these pathways.

The TCA Cycle Provides Intermediates for Biosynthetic Processes

  • The TCA cycle provides building blocks for other metabolic processes and produces intermediates for biosynthesis.

Quiz Questions (Information, not study notes)

  • Question 1: What is the ΔG°' value for hydrolysis of the thioester bond of Acetyl-CoA?
  • Question 2: What is the functional group in the thiazolium ring of TPP?
  • Question 3: How can the reduction of NAD+ spectroscopically be observed?
  • Question 4: Why is the Krebs cycle called Tricarboxyl Acid cycle (TCA)?
  • Question 5: Which enzyme/cofactor in the TCA cycle has a membrane connection? What cofactor does it use in catalysis?
  • Question 6: Which enzymes from the TCA cycle are likely to function far from equilibrium under physiological conditions?

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Related Documents

Metabolism Lecture 1 PDF
Lecture 3- TCA Cycle PDF

Description

Test your knowledge on the Tricarboxylic Acid (TCA) cycle, also known as the Krebs cycle. This quiz covers key components, processes, and enzymes involved in cellular respiration, including the regeneration of oxaloacetate and the role of electron carriers. Challenge your understanding of this essential metabolic pathway in biochemistry!

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