introduction Flashcards

1
Q

What is the substance acted upon by an enzyme called?

A. Product
B. Holoenzyme
C. Substrate
D. Isoenzyme

A

Answer: C
Explanation: The substrate is the substance acted upon by an enzyme.

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2
Q

What happens to enzymes with a small molecular weight when exposed to varying conditions?

A. They become more active
B. They are faster to denature
C. They synthesize in an inactive state
D. They do not require cofactors

A

Answer: B
Explanation: Enzymes with small molecular weight denature faster.

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2
Q

Which of the following best describes the term ‘amphoteric’ in relation to enzymes?

A. Able to react both as an acid or base
B. Easily denatured with high molecular weight
C. Found only in specific tissues
D. Always requiring a cofactor to function

A

Answer: A
Explanation: Amphoteric substances can react both as an acid and a base.

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2
Q

Which site on an enzyme is other than the active site and may lead to inhibition of substrate attachment?

A. Active site
B. Allosteric site
C. Substrate site
D. Product site

A

Answer: B
Explanation: Allosteric sites are locations other than the active site that can affect enzyme activity.

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2
Q

Which of the following is a non-protein organic biochemical that takes part in enzyme reactions?

A. Activators
B. Coenzymes
C. Holoenzyme
D. Apoenzyme

A

Answer: B
Explanation: Coenzymes are non-protein organic molecules essential for enzyme activity.

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2
Q

In which structure of enzymes are the interactions among side chains/groups significant?

A. Primary Structure
B. Secondary Structure
C. Tertiary Structure
D. Quaternary Structure

A

Answer: C
Explanation: The tertiary structure involves interactions among side chains of the polypeptide chain.

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3
Q

What term refers to the combined enzyme and coenzyme?

A. Apoenzyme
B. Holoenzyme
C. Isoenzyme
D. Isoform

A

Answer: B
Explanation: Holoenzyme is the term for the combination of an enzyme and its coenzyme.

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4
Q

Which of the following is an example of an inorganic ionic cofactor?

A. NAD
B. Pyridoxal phosphate
C. Mg++
D. Peptide bond

A

Answer: C
Explanation: Mg++ is an example of an inorganic ionic cofactor, specifically a metal ion.

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5
Q

Which structure of an enzyme consists of helical or beta pleated sheets maintained by hydrogen bonds?

A. Primary Structure
B. Secondary Structure
C. Tertiary Structure
D. Quaternary Structure

A

Answer: B
Explanation: The secondary structure consists of helical or beta pleated sheets maintained by hydrogen bonds.

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6
Q

What is the term for different forms of an enzyme with different genetic origins but catalyze the same reaction?

A. Isoenzymes
B. Isoforms
C. Holoenzymes
D. Apoenzymes

A

Answer: A
Explanation: Isoenzymes are different forms of an enzyme with different genetic origins that catalyze the same reaction.

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7
Q

What is the simplest enzyme structure consisting of a sequence of amino acids?

A. Primary Structure
B. Secondary Structure
C. Tertiary Structure
D. Quaternary Structure

A

Answer: A
Explanation: The primary structure is the simplest enzyme structure, consisting of a sequence of amino acids.

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8
Q

What is the function of a prosthetic group in an enzyme reaction?

A. It can be removed easily by dialysis
B. It is an inorganic ionic cofactor
C. It cannot be removed from its attachment to an enzyme
D. It is always a metal ion
Answer: C

A

Explanation: A prosthetic group cannot be removed from its attachment to an enzyme using dialysis.

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9
Q

Which of the following increases the catalytic activity of an enzyme when it binds to a specific site?

A. Coenzymes
B. Activators
C. Substrates
D. Products

A

Answer: B
Explanation: Activators increase the catalytic activity of an enzyme when they bind to specific sites.

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10
Q

Which structure of an enzyme involves more than one polypeptide chain forming a functional unit?

A. Primary Structure
B. Secondary Structure
C. Tertiary Structure
D. Quaternary Structure

A

Answer: D
Explanation: The quaternary structure involves more than one polypeptide chain forming a functional unit.

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11
Q

What is the term for an enzyme without its cofactor?

A. Apoenzyme
B. Holoenzyme
C. Isoenzyme
D. Prosthetic group

A

Answer: A
Explanation: An apoenzyme is an enzyme without its cofactor.

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12
Q

Which of the following best describes the role of NAD in enzyme reactions?

A. Inorganic ionic cofactor
B. Coenzyme
C. Apoenzyme
D. Substrate

A

Answer: B
Explanation: NAD is a coenzyme, a non-protein organic molecule essential for enzyme activity.

13
Q

In which enzyme structure are covalent disulfide bonds significant?

A. Primary Structure
B. Secondary Structure
C. Tertiary Structure
D. Quaternary Structure

A

Answer: C
Explanation: The tertiary structure involves covalent disulfide bonds among side chains.

14
Q

What type of site on an enzyme allows for the attachment of a substrate?

A. Allosteric site
B. Active site
C. Isoform site
D. Cofactor site

A

Answer: B
Explanation: The active site is where the substrate interacts with the enzyme.

15
Q

What does a high concentration of enzymes in the serum typically indicate?

A. Proper digestion
B. Cellular injury
C. Isoenzyme formation
D. Allosteric inhibition

A

Answer: B
Explanation: High concentrations of enzymes in the serum can indicate cellular injury.

16
Q

What does the term ‘isoforms’ refer to in relation to enzymes?

A. Different forms of an enzyme with different genetic origins
B. Results when an enzyme is subject to different post-translational modifications
C. Enzyme combined with a coenzyme
D. Enzyme without its cofactor

A

Answer: B. Results when an enzyme is subject to different post-translational modifications
Explanation: Isoforms result when an enzyme undergoes different post-translational modifications.