Metabolism and Enzyme Reactions

<p>The inhibitor competes with the substrate for the active site. (B)</p> Signup and view all the answers

<p>The inhibitor becomes ineffective. (D)</p> Signup and view all the answers

<p>Non-competitive inhibitors bind to a site other than the active site. (D)</p> Signup and view all the answers

<p>They involve multiple linear steps. (C)</p> Signup and view all the answers

<p>Through the management of intermediates (C)</p> Signup and view all the answers

<p>To alter the enzyme's structure and prevent substrate binding (C)</p> Signup and view all the answers

<p>It can be overcome by increasing substrate concentration. (B)</p> Signup and view all the answers

<p>By inhibiting an earlier enzyme to prevent excess production. (A)</p> Signup and view all the answers

<p>The inhibition is removed, and production increases. (A)</p> Signup and view all the answers

<p>It inhibits threonine deaminase activity. (D)</p> Signup and view all the answers

<p>Non-competitive inhibitors do not depend on substrate concentration. (A)</p> Signup and view all the answers

<p>Tight regulation of product synthesis to match cellular needs. (D)</p> Signup and view all the answers

<p>It is a non-competitive inhibitor that halts ATP production. (C)</p> Signup and view all the answers

<p>The enzyme is permanently inactivated. (D)</p> Signup and view all the answers

<p>It irreversibly inhibits transpeptidases, disrupting bacterial cell wall synthesis. (B)</p> Signup and view all the answers

<p>Bacteria can modify transpeptidases to reduce penicillin's effectiveness. (B)</p> Signup and view all the answers

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

<p>New enzymes must be synthesized. (D)</p> Signup and view all the answers

<p>Creation of covalent bonds that inhibit enzyme activity (B)</p> Signup and view all the answers

<p>By irreversibly inhibiting transpeptidases involved in cell wall synthesis (D)</p> Signup and view all the answers

<p>Modification of transpeptidase enzymes to reduce binding affinity (C)</p> Signup and view all the answers

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

<p>Disruption of the bacterial cell wall prevents pressure regulation (C)</p> Signup and view all the answers

<p>Alters the enzyme's structure, preventing substrate binding. (B)</p> Signup and view all the answers

<p>By using the final product to inhibit an enzyme in the pathway. (D)</p> Signup and view all the answers

<p>It does not affect the overall rate of reaction at high substrate concentrations. (B)</p> Signup and view all the answers

<p>It increases overall metabolic pathway efficiency. (C)</p> Signup and view all the answers

<p>It serves as a non-competitive inhibitor of threonine deaminase. (C)</p> Signup and view all the answers

<p>It inhibits further synthesis of isoleucine. (D)</p> Signup and view all the answers

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

<p>The metabolic pathway resumes production of the product. (D)</p> Signup and view all the answers

<p>The end product regenerates the starting molecule. (A)</p> Signup and view all the answers

<p>It competes with the substrate for the active site, reducing activity. (C)</p> Signup and view all the answers

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

<p>By increasing the concentration of the substrate. (B)</p> Signup and view all the answers

<p>They allow more control over the chemical changes within the cell. (D)</p> Signup and view all the answers

<p>Outside the cell, such as in the digestive tract. (A)</p> Signup and view all the answers

<p>It binds to an allosteric site and alters the enzyme's structure. (C)</p> Signup and view all the answers

<p>Statins blocking HMG-CoA reductase in cholesterol production. (C)</p> Signup and view all the answers

<p>It is permanently inactivated and requires new enzyme synthesis for activity restoration. (C)</p> Signup and view all the answers

<p>It inhibits transpeptidases involved in cell wall synthesis, leading to cell lysis. (D)</p> Signup and view all the answers

<p>They modify the target enzyme, decreasing its affinity for penicillin. (D)</p> Signup and view all the answers

<p>They create covalent bonds during the catalytic reaction, permanently modifying the enzyme. (A)</p> Signup and view all the answers

<p>Resistance genes can be transferred between bacteria, aiding survival. (C)</p> Signup and view all the answers

<p>It inhibits an earlier enzyme in the metabolic pathway. (D)</p> Signup and view all the answers

<p>It serves as a non-competitive inhibitor to regulate its own production. (A)</p> Signup and view all the answers

<p>Inhibition of the enzyme threonine deaminase. (B)</p> Signup and view all the answers

<p>The inhibitor binds to a site other than the active site, altering enzyme activity. (C)</p> Signup and view all the answers

<p>Cyanide alters the structure of cytochrome oxidase, inhibiting its function. (D)</p> Signup and view all the answers

<p>To regulate the concentration of metabolites and prevent waste. (B)</p> Signup and view all the answers

<p>It inhibits further synthesis of the product by affecting earlier enzymes. (C)</p> Signup and view all the answers

<p>It prevents substrates from binding to the enzyme. (D)</p> Signup and view all the answers

<p>Extracellular reactions typically involve digestion. (C)</p> Signup and view all the answers

<p>Cyclic pathways regenerate the starting molecule. (B)</p> Signup and view all the answers

<p>The inhibitor causes a conformational change in the enzyme. (C)</p> Signup and view all the answers

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

<p>It increases the likelihood of substrate binding over the inhibitor. (A)</p> Signup and view all the answers

<p>They help to regulate the metabolic pathways efficiently. (A)</p> Signup and view all the answers

<p>They can be outcompeted by increasing substrate concentration. (A)</p> Signup and view all the answers

<p>Cyclic pathways regenerate the starting molecule while linear pathways do not. (B)</p> Signup and view all the answers

Sum of all enzyme-catalyzed reactions in an organism, vital for life.

Chemical changes in cells controlled by enzymes in steps.

Reactions happening inside the cell, like glycolysis.

Reactions happening outside the cell, like digestion.

Series of reactions where product of one step is next step's reactant, like a chain.

Reactions form a cycle, starting and ending molecules are the same.

Inhibitor binds to active site, blocking substrate, reversible

Inhibitor binds to allosteric site, altering enzyme's shape.

A type of enzyme inhibition where an inhibitor irreversibly binds to the enzyme, often through a covalent bond, making the enzyme unable to function.

A type of inhibitor that covalently binds to and permanently inactivates an enzyme.

Penicillin inhibits bacterial transpeptidases, enzymes crucial for bacterial cell wall synthesis, leading to cell lysis (destruction).

Some bacteria develop modified transpeptidases with reduced affinity for penicillin, making them survive penicillin treatment.

A process where bacteria transfer genetic material, including resistance genes, to other bacteria.

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

A site on an enzyme other than the active site, where a molecule can bind and affect the enzyme's activity.

A specific type of feedback inhibition; final product of a pathway inhibits earlier steps to control production.

Pathway creating isoleucine from threonine (5 steps).

Enzyme catalyzing the first step in isoleucine synthesis.

The control of biochemical reactions within a cell to ensure efficiency and accuracy.

Penicillin acts as a suicide inhibitor that targets bacterial transpeptidases, enzymes essential for building the bacterial cell wall. By inhibiting these enzymes, penicillin weakens the cell wall, leading to cell lysis (rupture) and bacterial death.

Chemical reactions occurring within the cell, like glycolysis and the Krebs cycle, which are essential for energy production.

Chemical reactions happening outside the cell, like digestion in the gut, where nutrients are broken down.

A series of reactions where the product of one step becomes the reactant for the next, like a chain reaction.

Reactions form a cycle, where the end product regenerates the starting molecule, like a continuous loop.

A type of metabolic regulation where the product of a pathway inhibits an enzyme earlier in the pathway to control production.

A site on an enzyme other than the active site, where a molecule can bind and affect the enzyme's activity.

Cyanide is a non-competitive inhibitor that binds to cytochrome oxidase, a crucial enzyme in the electron transport chain, preventing it from transferring electrons to oxygen, leading to ATP production stoppage and eventual death.

Isoleucine, an amino acid synthesized in bacteria and plants, acts as a non-competitive inhibitor of threonine deaminase, the first enzyme in its synthesis pathway. This ensures that isoleucine production is regulated.

Feedback inhibition ensures that metabolic pathways are efficient and avoid overproduction of unnecessary products.

The regulation of isoleucine synthesis through feedback inhibition ensures that enough isoleucine is produced without depleting threonine, a vital precursor.

A series of enzyme-catalyzed reactions that occur in a specific order within a cell. They are essential for maintaining life and include both linear and cyclic pathways.

A series of reactions where the product of one step becomes the reactant of the next, creating a chain reaction.

Reactions that form a cycle, where the end product regenerates the starting molecule.

Cyanide acts as a non-competitive inhibitor of cytochrome oxidase, blocking electron transport and ATP production, leading to cell death.

Feedback inhibition ensures efficient metabolic pathways by preventing overproduction and waste.

Isoleucine acts as a non-competitive inhibitor of threonine deaminase, the first enzyme in its synthesis pathway. This ensures that isoleucine production is regulated.

Increasing substrate concentration does not overcome non-competitive inhibition. The inhibitor alters the enzyme's shape, so the substrate cannot bind effectively.

Competitive inhibition can be overcome by increasing substrate concentration, as the inhibitor and substrate compete for the active site. Non-competitive inhibition cannot be overcome by increasing substrate concentration, as the inhibitor changes the enzyme's shape, preventing substrate binding.

Penicillin targets bacterial transpeptidases, enzymes involved in building the bacterial cell wall.

The emergence of penicillin-resistant bacteria poses a significant threat to human health, making it difficult to treat bacterial infections.