WK 1: Enzymes as Drug Targets

<p>To hold the substrate sufficiently long for the reaction to occur (B)</p> Signup and view all the answers

<p>It reverses the inhibition of the enzyme (B)</p> Signup and view all the answers

<p>Inhibition of the enzyme (C)</p> Signup and view all the answers

<p>To act as the body's catalysts (A)</p> Signup and view all the answers

<p>It decreases the activation energy (A)</p> Signup and view all the answers

<p>It acts as a catalyst (A)</p> Signup and view all the answers

<p>They play a crucial role in both metabolic pathways and can be used as biomarkers of organ injury (C)</p> Signup and view all the answers

<p>It has no effect on ΔG (B)</p> Signup and view all the answers

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

<p>To catalyse biochemical reactions (B)</p> Signup and view all the answers

<p>To lower the activation energy of the reaction (C)</p> Signup and view all the answers

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

<p>To hold the substrate sufficiently long for the reaction to occur (A)</p> Signup and view all the answers

<p>To play a crucial role in metabolism and can be used as biomarkers of injury to specific organs (B)</p> Signup and view all the answers

<p>Formation of product (B)</p> Signup and view all the answers

<p>To bind reactants and position them correctly (A)</p> Signup and view all the answers

<p>The shape of the enzyme changes to fit the substrate (C)</p> Signup and view all the answers

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

<p>To catalyse the reaction (C)</p> Signup and view all the answers

<p>The reaction rate is increased (A)</p> Signup and view all the answers

<p>To position reactants correctly for reaction (C)</p> Signup and view all the answers

<p>Acting as an acid/base catalyst (D)</p> Signup and view all the answers

<p>Orientating histidine for catalysis (D)</p> Signup and view all the answers

<p>Acting as a nucleophile (D)</p> Signup and view all the answers

<p>Hydrolysis of a peptide bond (A)</p> Signup and view all the answers

<p>Improving catalytic efficiency (B)</p> Signup and view all the answers

<p>Digestion of proteins in the small intestine (C)</p> Signup and view all the answers

Enzymes are biological catalysts that speed up biochemical reactions without being consumed in the process.

Phosphorylation by a protein kinase activates the enzyme by changing its shape and allowing it to bind to its substrate.

Reversible inhibitors bind to the enzyme in a way that can be reversed, typically by increasing the substrate concentration.

Binding interactions between an enzyme and its substrate hold the substrate in the active site long enough for the reaction to occur.

Increasing substrate concentration can overcome the inhibition by pushing the equilibrium towards the formation of the enzyme-substrate complex.

Designing molecules with stronger binding interactions with an enzyme can inhibit its activity by preventing the substrate from binding.

Enzymes act as catalysts within the body, accelerating biochemical reactions necessary for life.

Enzymes lower the activation energy of a reaction, making it easier for the reaction to proceed.

Lactate dehydrogenase (LDH) is an enzyme that catalyzes the interconversion of lactate and pyruvate, a key step in energy metabolism.

Enzymes are crucial for metabolic pathways, allowing for the synthesis and breakdown of molecules needed for cellular processes. Levels of certain enzymes can also be indicative of organ damage, making them useful biomarkers.

Enzymes do not alter the overall free energy change (ΔG) of a reaction. They only accelerate the rate at which the reaction proceeds.

Cofactors are non-protein molecules that bind to enzymes and are essential for their activity. They can be metal ions or organic molecules.

Enzymes are biological catalysts that speed up biochemical reactions without being consumed in the process.

The oxyanion hole in chymotrypsin helps to stabilize the negatively charged transition state during peptide bond hydrolysis, thereby lowering the activation energy.

Designing molecules with stronger binding interactions with an enzyme can block the active site, preventing the substrate from binding and inhibiting the enzyme's activity.

Binding interactions between the enzyme and substrate hold the substrate in the active site long enough for the reaction to occur.

Enzymes are crucial for metabolism, allowing for the synthesis and breakdown of molecules needed for cellular processes. Levels of certain enzymes can also be indicative of organ damage, making them useful biomarkers.

Enzyme catalysis results in the formation of a product from the substrate through a specific chemical reaction.

The active site of an enzyme serves as the binding site for reactants, positioning them correctly for a chemical reaction to occur.

The induced fit process of substrate binding involves a conformational change in the enzyme's active site to better accommodate the substrate, leading to optimal binding.

Intermolecular bonds, such as hydrogen bonds, ionic interactions, and van der Waals forces, are formed between the functional groups in the substrate and the active site during substrate binding.

Enzymes act as catalysts, accelerating the rate of a biochemical reaction by lowering the activation energy barrier.

The catalytic mechanism of an enzyme increases the rate of the reaction by lowering the activation energy and facilitating the formation of the transition state.

The active site of an enzyme binds reactants in a specific orientation that favors the correct chemical interactions for the reaction to occur.

Histidine in chymotrypsin acts as a general acid/base catalyst, alternating between protonated and deprotonated states to facilitate the transfer of protons during the catalytic cycle.

Aspartate in chymotrypsin helps to orientate histidine for optimal catalytic activity by forming a hydrogen bond with it, ensuring proper positioning.

Serine in chymotrypsin acts as a nucleophile, attacking the carbonyl carbon of the peptide bond during the initial step of the catalytic mechanism.

The catalytic mechanism of chymotrypsin involves a series of steps, including nucleophilic attack by serine, formation of a tetrahedral intermediate, and hydrolysis of the peptide bond, resulting in the cleavage of the peptide chain.

The catalytic triad, consisting of serine, histidine, and aspartate, works together to increase the catalytic efficiency of chymotrypsin by optimizing the positioning and reactivity of the catalytic residues.

Chymotrypsin is a digestive enzyme that breaks down proteins into smaller peptides in the small intestine, facilitating their absorption into the bloodstream.