Answered: 3) An enzyme that converts a cis double…

3) An enzyme that converts a cis double bond to a trans double bond is classified as a(n). A) oxidoreductase B) transferase C) hydrolase D) lyase E) isomerase

Introductory Chemistry: An Active Learning Approach

6th Edition

ISBN:9781305079250

Author:Mark S. Cracolice, Ed Peters

Publisher:Mark S. Cracolice, Ed Peters

Chapter22: Biochemistry

Section: Chapter Questions

Problem 22.3TC

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Concept explainers

Vitamins and Coenzymes

A class of organic compounds needed in the human body for normal activities is known as vitamins. They are characterized into two parts depending upon their solubility in water. They can act as coenzymes, cofactors, or prosthetic groups for enzymes.

Question

4. What are the six classes of enzyme?
5. Explain a competitive inhibitor
In the induced-fit model, what happens to
the shape of the enzyme when the substrate
binds?
A. stays the same
B. adapts to the shape of the
substrate
35) An irreversible inhibitor is one that
A) forms hydrogen bonds with the substrate.
B) binds to the enzyme with hydrophobic
interactions.
C) reacts covalently with the substrate.
D) binds covalently to the enzyme active site.
E) reacts covalently with a cofactor.
47) Metal ions such as Zn²+ and Fe3+ are often
needed by enzymes as
A) isozymes.
B) allosteres.
C) inhibitors.
D) cofactors.
E) substrates.
3) An enzyme that converts a cis double bond to a
trans double bond is classified as a(n).
A) oxidoreductase
B) transferase
C) hydrolase
D) lyase
E) isomerase
3) An enzyme that converts a functional group to
another between two structures
A) oxidoreductase
B) transferase
C) hydrolase
D) lyase
E) isomerase
What is the function of these enzymes:
Oxidoreductase
Transferase
Decarboxylase
32) When an end product from an enzyme-mediated
sequence is also an inhibitor for an earlier step in the
reaction sequence, the process is referred to as
A) feedback control.
B) competitive inhibition.
C) irreversible inhibition.
D) negative catalysis.
E) concentration control.

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Write a brief description of the relationships among each of the following groups of terms or phrases. Answers to the Concept-Linking Exercises are given at the end of the chapter. Enzyme, enzyme substrate, active site, induced fit model
The human body has an average pH of about 7 and a temperature of about 37C. Use graphs to illustrate enzyme activity in the human body as a function of the following: a. Substrate concentration b. Enzyme concentration c. pH include pH optimum value d. Temperature include temperature optimum value
In the multienzyme sequence shown below, molecules of D are able to fit to the enzyme E1 and prevent the conversion of A to B. What is this action of E called? AE1BE2CE3D a. effector inhibition b. allosteric inhibition c. feedback inhibition d. competitive inhibition by nonproduct
Describe the difference between graphs showing temperature versus reaction rate for an enzyme-catalyzed reaction and an uncatalyzed reaction.
The process by which an enzyme acts on the substrate can be described by the: a. lock-and-key model. b. enzyme-and-substrate model. c. enzyme folding model. d. catalytic model.
The site on an enzyme molecule that does the catalytic work is called the: a. binding site. b. allosteric site. c. lock. d. active site.
How is enzyme specificity explained by the lock-and-key theory?
. Describe the lock-and-key model for enzymes. Why are the shapes of the enzyme and its substrate important in this model? What does it mean to say that an enzyme is inhibited by a particular molecule? What happens if this inhibition is irreversible? Can you think of a situation in which it might be advantageous to be able to inhibit an enzyme?
When handling or storing solutions of enzymes, the pH is usually kept near 7.0. Explain why.