Enzymes: Biological Catalysts

What structural aspect of an enzyme is most critical to its function?

Enzymes increase the rate of reaction by lowering what?

Which of the following is true regarding uncatalyzed reactions?

What environmental conditions are most suitable for enzyme function?

What is the induced fit model?

What might be needed in addition to amino acids for some enzymes to function?

What is the primary consequence if human enzymes malfunction?

Enzymes are known to catalyze almost every reaction within which system?

Why are enzymes highly specific and efficient compared to industrial catalysts?

What happens to an enzyme if it is denatured or dissociated?

What is the role of digestive enzymes in the body?

In what industries might enzymes be commonly found and used?

Which of the following represents the correct sequence of events in enzyme catalysis according to the induced fit model?

How do enzymes provide an alternative reaction pathway?

Given that enzymes function optimally under specific conditions, what would likely happen if an enzyme were moved from its optimal temperature to a much higher temperature?

If a reaction that is normally catalyzed by an enzyme in the human body began to occur at a significantly reduced rate, what factor might be responsible?

A scientist discovers a new enzyme. Preliminary studies show it functions best at a pH of 2.0. In what part of the human body might this enzyme be most active?

In the context of industrial applications, why might an enzyme be preferred over a traditional chemical catalyst?

If a genetic mutation caused a change in the amino acid sequence of an enzyme but did not significantly alter its 3D structure, what would be the most likely outcome?

Why do enzymes not get consumed during a reaction?

According to the 'RNA world hypothesis', what dual role did RNA play in early evolutionary life?

What is the role of metal ions like $Fe^{2+}$ or $Zn^{2+}$ in enzyme activity?

How do coenzymes primarily function in enzymatic reactions?

Many coenzymes are derived from what class of biomolecules?

In redox reactions, what role does $NAD^+$ play, and in what forms does it exist?

What distinguishes ribozymes from other enzymes?

What is the purpose of cofactors in enzymatic reactions?

How does $Zn^{2+}$ facilitate the reaction catalyzed by alcohol dehydrogenase?

What kind of role can cofactors play in the structure of enzymes?

Hammerhead ribozymes are known for what specific function?

What is the role of inorganic ions such as $Cu^{2+}$ or $Fe^{3+}$?

What chemical groups are biotin and coenzyme A responsible for transferring?

What enzyme is zinc commonly a cofactor for?

What do flavin adenine dinucleotide and lipoate have in common?

What precursor is thiamine pyrophosphate derived from?

What chemical groups are transferred by tetrahydrofolate?

What enzymes involve potassium ions $(K^+)$ as cofactors?

What enzymes involve magnesium ions $(Mg^{2+})$ as cofactors?

What vitamin is flavin adenine dinucleotide derived from?

What class of molecule are coenzymes?

What characteristic distinguishes prosthetic groups from coenzymes?

Which of the following best describes the function of the active site of an enzyme?

What is the functional difference between an apoenzyme and a holoenzyme?

According to the classification of enzymes, what type of reaction do hydrolases catalyze?

If an enzyme's active site surface is lined with amino acid residues, what is the primary purpose of these residues?

Why is it essential for all components to be present for an enzyme to function effectively?

In what way may the active site sometimes sequester the substrate?

If an enzyme is classified as a lyase, what type of reaction does it catalyze?

How do enzymes recognize their specific substrates?

What role do metal ions play when they act as cofactors?

If an enzyme is classified as an oxidoreductase, what type of reaction does it catalyze?

If an enzyme is classified as a transferase, what type of reaction does it catalyze?

If an enzyme is classified as an isomerase, what type of reaction does it catalyze?

Given that chymotrypsin is a protease that catalyzes hydrolysis of peptide bonds, what type of amino acids is it most specific for?

How does the enzyme's active site ensure substrate specificity?

What is the role of cosubstrates in enzyme-catalyzed reactions?

Which statement best summarizes how enzymes contribute to metabolic processes?

What determines the specificity of an enzyme for its substrate?

Why is the precise positioning of the substrate within an enzyme's active site critical for catalysis?

How do enzymes affect the equilibrium of a reaction?

What must be overcome for a reaction to occur?

How does the presence of an enzyme affect the Gibbs free energy change (ΔG) of a reaction?

What is the relationship between the activation energy (Ea) of a reaction and its reaction rate?

In enzymatic reactions, what is represented by ES and EP?

What happens to the amino acid side chains of an enzyme if the pH is outside of its optimal range?

Which of the following statements accurately describes the role of enzymes in a chemical reaction?

How is Gibbs free energy related to enthalpy (H), temperature (T), and entropy (S)?

Pepsin, an endopeptidase found in the stomach, is optimally active at what pH?

In a reaction coordinate diagram, what does the transition state represent?

How does the environment impact the reaction?

What are endopeptidases known to do?

Where is G6P, which hydrolyzes gluc-6-phosphate to produce glucose + free phosphate, found?

According to the material, the rate of a reaction will increase when:

Compared to the uncatalyzed reaction, the catalyzed reaction will have a:

In reactions, enzymes are:

According to the image, what is equal to the ground state?

Which statement is correct regarding enzymatic reaction in regards to the substrate, S, becoming a product, P?

According to the image, in a simple reaction, what is the last item to be produced?

When old bonds are broken and new bonds are formed, energy is: