Becker's World of the Cell (9th Edition)
Becker's World of the Cell (9th Edition)
9th Edition
ISBN: 9780321934925
Author: Jeff Hardin, Gregory Paul Bertoni
Publisher: PEARSON
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Chapter 6, Problem 6.10PS

What Type of Inhibition? A new mucinase enzyme was recently discovered that breaks down a glycoprotein in mucous membranes and contributes to bacterial vaginosis (J. Clin. Microbiol. 43:5504). You are a research pathologist testing a new inhibitor of this enzyme that you have discovered, and you want to design experiments to understand the nature of this inhibition. You have a supply of the normal glycoprotein substrate, the inhibitor, and an assay to measure product formation.

(a) How might you determine whether inhibition is reversible or irreversible?

(b) If you find that the inhibition is reversible, how would you determine whether the inhibition is competitive or noncompetitive?

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I. Active site analysis. Below is a diagram of a putative active site for Monoamine oxidase. As we learned, the purpose of tertiary structure is to form a scaffold so you can orient just a few amino acids in the right orientation to promote binding and/or catalysis. The position where this occurs is the active site. The amino acid architecture of an active site is designed to bind substrates. Amino acid side chains are capable of hydrogen bonding, ionic and hydrophobic interactions. Fill in each amino acid that you think is suitable for interacting with the part of the substrate it is closest to. Assume the pH will be at 7.0 a.a.#1 a.a.#2 a.a.#6 HO Lond NH₂ НО a.a.#5 OH a.a.#3 a.a.#4
Inhibitor X exerts which of the following effects on the above enzyme (maltase)? (inhibitor X changes maltase activity to a V o  of 0.10 mM per minute when [S] = 0.125 mM, and a V o  of 0.25 mM per minute when [S] = 0.50 mM)
. Propose a chemical mechanism for the reaction catalyzed by the PLP-dependent glatamate 1-semialdehyde aminomutase.
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