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Chapter 4: Problem 8

If you were using aspartate aminotransferase, and the enzyme stopped catalyzing the reaction, what \(t\) wo components of the enzyme reaction would you check?

Short Answer

Expert verified
The two components that should be checked if aspartate aminotransferase has stopped catalyzing the reaction are the availability of substrates (aspartate and alpha-ketoglutarate) and the presence of its co-enzyme pyridoxal phosphate, along with the environmental conditions (pH, temperature).

Step by step solution

01

Understand Enzyme Function

First, it's important to understand the function of aspartate aminotransferase. This enzyme is important for the metabolism of amino acids and it catalyzes the transfer of an amino group from aspartate to alpha-ketoglutarate, thereby creating oxaloacetate and glutamate. If this reaction has stopped, there are several components that might be responsible.
02

Assess Component One - Substrates

The first component to check if the enzyme stopped functioning is the presence and availability of the substrates. In this case, these are aspartate and alpha-ketoglutarate. If either of these is absent or not at a high enough concentration, aspartate aminotransferase won't be able to perform its function.
03

Assess Component Two - Co-enzyme

This enzyme also requires a co-enzyme, pyridoxal phosphate, to function properly. Similar to the substrates, if this co-enzyme is not present, the enzyme can't catalyze the reaction. Additionally, environmental conditions such as temperature or pH can also affect the enzyme's ability to work.

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Most popular questions from this chapter

\(\gamma\)-Aminobutyric acid (GABA) aminotransferase catalyzes a PLP-dependent conversion of GABA to succinic semialdehyde (SSA). a. Draw a mechanism for this reaction. b. Why is only one molecule of succinic semialdehyde formed in the absence of \(\alpha\)-ketoglutarate c. If the reaction were carried out in \({ }^{2} \mathrm{H}_{2}{ }^{18} \mathrm{O}\), what would the products be?

The \((3 S, 4 S)\)-isomer of deuterated compound \(\mathbf{1}\) is a substrate for a dephosphorylase that gives an antielimination to the \(Z\)-isomer (2). The corresponding (3R,4S)-isomer is not a substrate. How do you explain that?

What are the two most important characteristics of an enzyme?

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Compound 3 is a substrate for an enzyme that catalyzes the removal of the \(\mathrm{H}_{\mathrm{S}}\) proton exclusively. If compound 4 is used as the substrate, the deprotonation occurs mostly at \(\mathrm{H}_{\mathrm{S}}\), but a small amount of products are observed from removal of \(\mathrm{H}_{\mathrm{R}}\). This second reaction was shown to be catalyzed by the same enzyme as well. How could this be rationalized?
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