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General Organic and Biochemistry Study Set 1

Chemistry

Quiz 19 :

Enzymes

Quiz 19 :

Enzymes

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What is an allosteric enzyme?
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Answer:

A

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Which of the following describes how an enzyme can affect the transition state in an enzyme-catalyzed reaction?
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Answer:

E

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Which of the following is a medical use of enzymes?
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Answer:

E

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Elastase is a protease enzyme that cleaves peptide bonds on the carbonyl side of the amino acids glycine and alanine.What products result from treatment of a peptide with the primary structure shown below with elastase? Pro-Gly-Phe-Ala
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Sucrase is an example of an enzyme that displays absolute specificity.What does the term "absolute specificity" indicate about an enzyme?
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About half of the 223 amino acids in the enzyme trypsin are hydrophobic. Where in the tertiary structure of this globular protein are these amino acids most likely to be found?
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What term describes the pH at which an individual enzyme functions best?
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Which of the following best describes the type of binding between an irreversible inhibitor and an enzyme?
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The diagram below shows the energy pathway of an uncatalyzed reaction.How does the energy diagram change when an enzyme is used in the same reaction? img
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Lactase is an enzyme that catalyzes the following reaction.Which statement describing this reaction is FALSE? img
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Trypsin is a protease enzyme that cleaves peptide bonds on the carbonyl side of basic amino acids.Which labeled bond(s) in the peptide below would be cleaved by trypsin? img
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Acetylcholine is a neurotransmitter that transmits a signal from a nerve cell to a muscle cell, causing the muscle to contract.How is the neurotransmitter inactivated so that the muscle can relax?
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Proteases, or proteolytic enzymes, are responsible for which of the following functions?
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In feedback inhibition of an enzyme-catalyzed biosynthetic pathway, what frequently serves as the negative allosteric effector?
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Which of the following correctly describes pepsinogen?
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The pancreatic enzymes trypsin, chymotrypsin, and elastase all hydrolyze peptide bonds on the carbonyl side of several different amino acids in a protein.What term best describes their enzyme specificity?
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Proteolytic digestive enzymes are often produced in an inactive form.What is the name that refers to the inactive form of an enzyme?
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What three structurally similar pancreatic serine proteases function to cleave certain peptide bonds in proteins?
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The rate of an enzyme-catalyzed reaction initially increases with an increase in the substrate concentration, but eventually reaches a maximum value, even though the concentration of substrate continues to increase.Which of the following best explains why?
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The protease enzyme chymotrypsin cleaves peptide bonds on the carbonyl side of aromatic amino acids.Which labeled bond in the peptide below would be cleaved by chymotrypsin? img
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