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Questions and Answers
Which of the following individuals is NOT involved in the naming of enzymes?
Which of the following individuals is NOT involved in the naming of enzymes?
What is the primary focus of the individuals mentioned?
What is the primary focus of the individuals mentioned?
Which of the following statements about enzyme naming is most likely true?
Which of the following statements about enzyme naming is most likely true?
Which characteristic is most important in the naming of enzymes?
Which characteristic is most important in the naming of enzymes?
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What role do the individuals listed play in the scientific community?
What role do the individuals listed play in the scientific community?
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What is the primary function of coenzymes in redox reactions?
What is the primary function of coenzymes in redox reactions?
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Which of the following statements about dehydrogenases is correct?
Which of the following statements about dehydrogenases is correct?
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Which component is typically involved in redox reactions as a coenzyme?
Which component is typically involved in redox reactions as a coenzyme?
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In redox reactions, which molecule is the most common electron acceptor?
In redox reactions, which molecule is the most common electron acceptor?
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What is NOT a component involved in redox reactions?
What is NOT a component involved in redox reactions?
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What is the primary role of thiamine pyrophosphate (TPP) in enzymatic reactions?
What is the primary role of thiamine pyrophosphate (TPP) in enzymatic reactions?
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How is coenzyme A (CoA) activated?
How is coenzyme A (CoA) activated?
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What does the fourth digit in enzyme classification indicate?
What does the fourth digit in enzyme classification indicate?
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What consequence results from a deficiency of vitamin B1?
What consequence results from a deficiency of vitamin B1?
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Which group is not a type of activation-transfer coenzyme?
Which group is not a type of activation-transfer coenzyme?
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Which EC number corresponds to hydrolases that act on peptide bonds?
Which EC number corresponds to hydrolases that act on peptide bonds?
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What is the primary function of biotin in enzymatic reactions?
What is the primary function of biotin in enzymatic reactions?
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What activity is denoted by the EC number 3.4.11.4?
What activity is denoted by the EC number 3.4.11.4?
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Which component is NOT included in the structure of coenzyme A (CoA)?
Which component is NOT included in the structure of coenzyme A (CoA)?
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Which enzyme classification includes enzymes that cleave polypeptides?
Which enzyme classification includes enzymes that cleave polypeptides?
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What vitamin is coenzyme A derived from?
What vitamin is coenzyme A derived from?
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What is the primary purpose of enzyme subclassification?
What is the primary purpose of enzyme subclassification?
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What dietary factor can lead to biotin deficiency?
What dietary factor can lead to biotin deficiency?
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Which functional group is primarily involved in the activation-transfer process of TPP?
Which functional group is primarily involved in the activation-transfer process of TPP?
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What role does magnesium ion (Mg+2) play in the function of some coenzymes?
What role does magnesium ion (Mg+2) play in the function of some coenzymes?
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What role does water play in reactions involving dehydration and hydration?
What role does water play in reactions involving dehydration and hydration?
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Which of the following enzymes is an example of a lyase?
Which of the following enzymes is an example of a lyase?
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What reaction do aldolases catalyze?
What reaction do aldolases catalyze?
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Which statement best describes the action of lyases in biochemical reactions?
Which statement best describes the action of lyases in biochemical reactions?
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Hydration reactions are primarily characterized by what process?
Hydration reactions are primarily characterized by what process?
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What reaction is catalyzed by enolase?
What reaction is catalyzed by enolase?
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What type of enzyme is an isomerase?
What type of enzyme is an isomerase?
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What process does enolase primarily involve?
What process does enolase primarily involve?
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Which of the following correctly describes an isomer?
Which of the following correctly describes an isomer?
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What is the main role of isomerases in biochemical reactions?
What is the main role of isomerases in biochemical reactions?
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Study Notes
Biochemistry Study Notes
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Enzyme Naming: Enzymes are named after their substrate, ending with "-ase." Examples include ATPase (breaks down ATP) and ATP synthase (synthesizes ATP). Some enzymes are named without relation to their substrates, such as Trypsin (breaks down proteins).
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Enzyme Commission (EC) Number: This number describes the substrate, enzyme, and reaction catalyzed. It does not identify specific enzymes, but rather the reaction. The number is a four-digit code (separated by periods) designed to categorize enzymes into classes, minor classes, subclasses, and sub-classifications.
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Enzyme Classification by Structure: Classification considers whether an enzyme is simple (protein only) or complex (protein + other components). Also distinguished between holoenzymes (complete, active enzyme) and apoenzymes (inactive protein part).
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Enzyme Classification by Function: There are seven main classes of enzymes, ordered: 1) Oxidoreductases, 2) Transferases, 3) Hydrolases, 4) Lyases, 5) Isomerases, 6) Ligases, and 7) Translocases. Each class catalyzes a specific type of reaction.
Oxidoreductases (Detailed)
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Function: Facilitate electron transfer between molecules (e.g., transferring hydrogen atoms). This process is called redox. Often require coenzymes for this.
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Minor Classes: Examples include dehydrogenases (transfer of hydrogen ions or electrons) and oxidases (transferring electrons to oxygen; producing hydrogen peroxide). Peroxidases use hydrogen peroxide to oxidize other molecules. Oxygenases also involve oxygen, but the reduced product is water, not hydrogen peroxide.
Transferases (Detailed)
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Function: Transfer functional groups (like methyl, acetyl, sulfate or phosphate) between molecules.
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Minor Class (Kinases): These transfer phosphate groups; an example is phosphofructokinase which acts in glycolysis.
Hydrolases (Detailed)
- Function: Break down molecules by adding water to a bond. Examples include proteases (break down proteins), lipases (break down lipids), and amylases (break down starch).
Lyases (Detailed)
- Function: Catalyze the addition or removal of functional groups from substrates, often forming or breaking double bonds. Examples include aldolases (cleave carbon-carbon bonds) and enoases (interconvert molecules by forming or breaking double bonds).
Isomerases (Detailed)
- Function: Change the arrangement of atoms within a molecule without changing the overall chemical formula. An example is glucose-6-phosphate isomerase, which changes glucose-6-phosphate to fructose-6-phosphate, both with the same molecular makeup.
Ligases (Detailed)
- Function: Join two molecules together using energy from a compound such as ATP. Pyruvate carboxylase is an example that combines pyruvate and CO2 to form oxaloacetate.
Functional Groups in Catalysis
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Amino Acid Side Chains: Many polar amino acids (Ser, Cys, Lys, & His) act in catalysis due to their functional groups.
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Coenzymes: Organic molecules derived from vitamins; they're essential for various reactions, like activation-transfer or oxidation-reduction processes.
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Activation-Transfer Coenzymes: Often involve covalent bonding.
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Oxidation-Reduction Coenzymes: Participate in redox reactions (electron transfer).
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Description
This quiz explores the roles of various individuals in the naming of enzymes, as well as the fundamental concepts behind enzyme functions and coenzymes in redox reactions. Test your knowledge on enzyme nomenclature, dehydrogenases, and the components involved in these critical biochemical processes.