Enzymology Chapter Quiz

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

<p>Metal ions can act as cofactors. (B)</p> Signup and view all the answers

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

<p>Removal of carboxyl groups (D)</p> Signup and view all the answers

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

<p>Conversion of an aldose to a ketose (A)</p> Signup and view all the answers

<p>Joining two molecules into one (C)</p> Signup and view all the answers

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

<p>The class of the enzyme (B)</p> Signup and view all the answers

<p>They cannot function without their cofactors. (D)</p> Signup and view all the answers

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

<p>Loss of enzyme structure and function (C)</p> Signup and view all the answers

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

<p>An enzyme with both protein and cofactor components. (A)</p> Signup and view all the answers

<p>They may undergo denaturation. (D)</p> Signup and view all the answers

<p>Enzyme activity can decrease due to denaturation (C)</p> Signup and view all the answers

<p>pH 2.0 (B)</p> Signup and view all the answers

<p>As enzyme concentration increases, reaction rate increases (D)</p> Signup and view all the answers

<p>Reaction rate eventually reaches a saturation point (C)</p> Signup and view all the answers

<p>Increasing temperature typically increases reaction rates (D)</p> Signup and view all the answers

<p>The reaction rate stabilizes at its maximum level (A)</p> Signup and view all the answers

<p>Enzymes are not consumed and can be reused many times (C)</p> Signup and view all the answers

<p>pH 7.0 - 7.5 (B)</p> Signup and view all the answers

<p>Enzyme-Substrate Complex (A)</p> Signup and view all the answers

<p>Lock &amp; Key Model (C)</p> Signup and view all the answers

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

<p>It undergoes denaturation (C)</p> Signup and view all the answers

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

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

<p>R-groups (side chains) of amino acids (C)</p> Signup and view all the answers

<p>Induced Fit Model (B)</p> Signup and view all the answers

<p>It increases the reaction rate until saturation occurs. (B)</p> Signup and view all the answers

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

<p>It permanently deactivates the enzyme. (D)</p> Signup and view all the answers

<p>It binds to the active site and prevents substrate access. (B)</p> Signup and view all the answers

<p>Enzymes denature and become non-functional. (D)</p> Signup and view all the answers

<p>They bind to a site other than the active site. (B)</p> Signup and view all the answers

<p>They stabilize an active conformation of the enzyme. (B)</p> Signup and view all the answers

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

<p>They exhibit a quaternary structure. (A)</p> Signup and view all the answers

<p>They do not resemble substrates. (B)</p> Signup and view all the answers

<p>Permanent catalytic inhibition (D)</p> Signup and view all the answers

<p>Any site other than the active site. (C)</p> Signup and view all the answers

A non-protein part of an enzyme that helps it function.

The protein part of an enzyme, without any cofactors attached.

A complete active enzyme, formed by the apoenzyme combined with its cofactor.

A type of cofactor, usually a small organic molecule, that helps enzymes.

An enzyme that consists only of a protein, without any non-protein parts.

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

Most enzymes are made up of proteins, but some are made of RNA.

Enzymes have a specific three-dimensional structure that allows them to bind to specific molecules called substrates.

Enzymes are named based on the reaction they catalyze, often ending with the suffix '-ase'. For example, an enzyme that breaks down lactose is called lactase.

The specificity of an enzyme refers to its ability to bind to a specific substrate, like a lock and key.

Conjugated enzymes are composed of two parts: a protein part called the apoenzyme, and a non-protein part called a cofactor.

The apoenzyme is the protein part of a conjugated enzyme, it cannot catalyze its specific reaction without its cofactor.

Cofactors are non-protein molecules that help enzymes function. They can be metal ions or organic molecules called coenzymes.

Enzymes that break down molecules by adding water.

Enzymes that catalyze the addition or removal of atoms to or from double bonds.

Enzymes that rearrange atoms within a molecule, changing its structure.

Enzymes that join two molecules together using energy from ATP.

A reaction that breaks down bonds by adding water molecules.

The pH at which an enzyme exhibits maximum activity.

A change in pH can cause an enzyme to lose its shape and function, becoming inactive.

Enzymes accelerate chemical reactions by lowering activation energy.

The point at which increasing substrate concentration no longer increases reaction rate.

The rate of an enzyme-catalyzed reaction is directly proportional to the amount of enzyme present.

Enzymes are not consumed during a reaction, they are reusable, acting as catalysts.

The site on an enzyme where the substrate binds and the reaction takes place.

The substance that an enzyme acts on.

The specific region on an enzyme where substrate molecules bind and undergo chemical reactions.

The 3D structure formed by the folding of an enzyme's protein chain. This structure creates a 'crevice-like' cavity where the substrate binds.

The enzyme-substrate complex is a temporary association formed when the substrate binds to the active site of an enzyme. This binding facilitates the chemical reaction.

The 'lock and key' model proposes that the active site of an enzyme has a rigid shape that perfectly complements the shape of the substrate.

The 'induced fit' model suggests that the active site of an enzyme is flexible and adapts its shape to accommodate the substrate.

Absolute specificity means an enzyme can only catalyze a specific reaction for one single substrate.

Group specificity means an enzyme can act on substrates that share a particular functional group.

Linkage specificity refers to the enzyme's ability to target specific chemical bonds within a molecule, regardless of the rest of the molecule's structure.

Stereochemical specificity means an enzyme can differentiate between stereoisomers, or molecules with the same chemical formula but different spatial arrangements.

An increase in body temperature from 37°C to 42°C can cause enzymes to lose their optimal shape and function, leading to a decrease in their activity.

If an enzyme is non-functional, the chemical reaction it normally catalyzes will slow down or stop completely, as the enzyme is no longer able to facilitate the reaction.

A substance that binds to an enzyme and reduces its catalytic activity, slowing down or stopping the enzyme's normal function.

A type of enzyme inhibition where the inhibitor competes with the substrate for binding to the enzyme's active site. This can be reversed by increasing the substrate concentration.

A type of enzyme inhibition where the inhibitor binds to a site on the enzyme other than the active site, altering the enzyme's shape and reducing its activity. This can be reversed by reducing the inhibitor concentration.

A type of enzyme inhibition where the inhibitor binds to the enzyme's active site irreversibly, permanently deactivating the enzyme. This cannot be reversed by adding more substrate.

Enzymes with a quaternary structure (composed of multiple protein chains) that have two or more binding sites: one active site for the substrate and another regulatory site for a regulator molecule. The binding of a regulator molecule to the regulatory site can alter the enzyme's shape and activity.

A molecule that binds to an allosteric enzyme's regulatory site and increases the enzyme's activity, promoting the active conformation.

A molecule that binds to an allosteric enzyme's regulatory site and decreases the enzyme's activity, compromising the active site and making it less efficient.

The binding of a positive regulator to an allosteric enzyme enhances enzyme activity by promoting a more active conformation of the active site, allowing the enzyme to bind to the substrate more efficiently.