Podcast
Questions and Answers
Which component is NOT part of the catalytic triad in serine proteases?
Which component is NOT part of the catalytic triad in serine proteases?
What defines the substrate specificity of chymotrypsin?
What defines the substrate specificity of chymotrypsin?
In the context of serine proteases, what does the term 'hydrolyze' refer to?
In the context of serine proteases, what does the term 'hydrolyze' refer to?
Which amino acids does chymotrypsin specifically target for cleavage?
Which amino acids does chymotrypsin specifically target for cleavage?
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Which of the following statements about serine proteases is FALSE?
Which of the following statements about serine proteases is FALSE?
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What remains unchanged after chymotrypsin cleaves a peptide bond?
What remains unchanged after chymotrypsin cleaves a peptide bond?
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What residues are consistently assigned the numbers His57, Asp102, and Ser in serine proteases?
What residues are consistently assigned the numbers His57, Asp102, and Ser in serine proteases?
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Which class of enzyme is responsible for the reaction D-Glucose + ATP → D-Glucose-6-phosphate + ADP?
Which class of enzyme is responsible for the reaction D-Glucose + ATP → D-Glucose-6-phosphate + ADP?
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What type of reaction is catalyzed by carboxypeptidase A?
What type of reaction is catalyzed by carboxypeptidase A?
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In the enzyme-catalyzed reaction involving cleavage of a bond, what is the role of Glu (E 270)?
In the enzyme-catalyzed reaction involving cleavage of a bond, what is the role of Glu (E 270)?
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What type of enzyme is responsible for the reaction Maleate → Fumarate?
What type of enzyme is responsible for the reaction Maleate → Fumarate?
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Which of the following enzymes catalyzes a reaction involving carboxylation?
Which of the following enzymes catalyzes a reaction involving carboxylation?
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What type of interaction does Arg (R 145) primarily facilitate in catalysis?
What type of interaction does Arg (R 145) primarily facilitate in catalysis?
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Which of the following accurately describes the role of ligases?
Which of the following accurately describes the role of ligases?
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What is the primary function of the Zn2+ ion in the enzyme's active site?
What is the primary function of the Zn2+ ion in the enzyme's active site?
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Study Notes
Enzymes Fall into 6 Major Classes by Function
- Enzymes are classified into six major classes based on the type of reaction they catalyze.
- Each class catalyzes a specific type of reaction.
- The classes are oxidoreductases, transferases, hydrolases, lyases, isomerases, and ligases.
Examples of Enzyme Classes
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Oxidoreductases: Catalyze oxidation-reduction reactions.
- Example: Alcohol dehydrogenase (oxidation with NAD).
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Transferases: Catalyze the transfer of a functional group from one molecule to another.
- Example: Hexokinase (phosphorylation).
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Hydrolases: Catalyze the hydrolysis of a chemical bond.
- Example: Carboxypeptidase A (peptide bond cleavage).
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Lyases: Catalyze the cleavage of a chemical bond by elimination, leaving a double bond or adding a group to a double bond.
- Example: Pyruvate decarboxylase (decarboxylation).
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Isomerases: Catalyze the isomerization of molecules.
- Example: Malate isomerase (cis-trans isomerization).
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Ligases: Catalyze the joining of two molecules by the formation of a new bond.
- Example: Pyruvate carboxylase (carboxylation).
What Types of Catalysis Can You Identify?
- Glu (E270) in Catalysis: Glu (E270) plays a role in acid-base catalysis.
- Arg (R145) in Catalysis: Arg (R145) is involved in charge-charge interactions in catalysis.
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Description
This quiz explores the six major classes of enzymes based on their functions. Each class plays a pivotal role in various biochemical reactions, ranging from oxidation-reduction to hydrolysis. Test your knowledge on examples and functions of oxidoreductases, transferases, hydrolases, and more.
