engineering

Glutamate—prephenate aminotransferase

Glutamate—prephenate aminotransferase is a engineering topic covered in the lgStudy science library. This page brings together a partial reference excerpt, illustrations, worked examples, real-world applications and a short study plan, so you can understand Glutamate—prephenate aminotransferase rather than just read about it. In short: In enzymology, glutamate-prephenate aminotransferase (EC 2.6.1.79, also known as prephenate transaminase, PAT, and L-glutamate:prephenate aminotransferase) is an enzyme that catalyzes the chemical reaction L-arogenate + 2-oxoglutarate ⇌ {\displaystyle \rightleftharpoons } prephenate + L-glutamate Thus, the two substrates of this enzyme are L-arogenate and 2-oxoglutarate, whereas its two products are prephenate and L…

Key takeaways

Glutamate—prephenate aminotransferase belongs to engineering; place it in that map before memorising details.
Learn the definition first, then one example that makes the definition concrete.
Connect Glutamate—prephenate aminotransferase to a quantity you can measure, compute or draw — that is where exam questions come from.
Reproduce the core statement of Glutamate—prephenate aminotransferase from memory before moving on to harder problems.

Reference excerpt

L-arogenate + 2-oxoglutarate ⇌ {\displaystyle \rightleftharpoons } prephenate + L-glutamate Thus, the two substrates of this enzyme are L-arogenate and 2-oxoglutarate, whereas its two products are prephenate and L-glutamate. However, in most plant species utilizing this enzyme, the left side of the reaction is strongly favored. Therefore, glutamate is used as the amino donor to convert prephenate into arogenate.

Nomenclature This enzyme belongs to the family of transferases, specifically the transaminases, which transfer nitrogenous groups. The systematic name of this enzyme class is L-arogenate:2-oxoglutarate aminotransferase. Other names in common use include prephenate transaminase (ambiguous), PAT (ambiguous), and L-glutamate:prephenate aminotransferase. It operates in the phenylalanine and tyrosine biosynthesis pathway.

Species distribution The gene which encodes this enzyme has recently been identified in various plant species and microorganisms, meaning that all genes in the pathway have now been identified and accounted for. This pathway occurs in many different plant species. As phenylalanine is an essential amino acid, humans (and other animals) have lost the ability to produce it themselves and must therefore obtain it from their diet. As such, the activity of this enzyme in various plant species affects the survival of animals as well. In these animals, tyrosine is synthesized from phenylalanine via the enzyme phenylalanine hydroxylase, whereas plants have their own method of tyrosine synthesis.

Function Glutamate—prephenate aminotransferase catalyzes the reversible reaction shown below:

, and its primary purpose is to convert prephenate into arogenate via transamination, using glutamate as the amino donor. As stated previously, the left side of the reaction is strongly favored. This is a necessary process for any organism which needs to convert arogenate into phenylalanine or tyrosine, as arogenate is an intermediate in the reactions which synthesize these amino acids, an alternative route to that involving phenylpyruvate and hydroxyphenylpyruvate. In the absence of glutamate, aspartate can act as the amino donor in the reaction without the need for a different enzyme, but this reaction proceeds more slowly. The details of the activity of this enzyme are still somewhat of a mystery.

Structure Little is known about the structure of glutamate-prephenate aminotransferase. However, some data indicates that the enzyme may have an α2-β2 subunit structure.

References and further reading

Worked examples

Example 1 — a first encounter with Glutamate—prephenate aminotransferase

Start with the simplest possible case. Write down what Glutamate—prephenate aminotransferase claims or describes in one sentence, then invent the smallest concrete situation in which that sentence is true. In engineering, the smallest case is usually a single object, a single equation or a single measurement. Check that every symbol or term in your sentence has a meaning in that case.

Example 2 — changing one variable

Take the situation from Example 1 and change exactly one quantity: double it, halve it, or set it to zero. Predict what should happen to Glutamate—prephenate aminotransferase before you calculate. Comparing your prediction with the result is the fastest way to find out whether you understand the idea or only the words.

Example 3 — an exam-style question

Typical questions about Glutamate—prephenate aminotransferase ask you to (a) state it precisely, (b) apply it to given data, and (c) explain a limitation. Practise writing all three answers in under five minutes; the third part is what separates a full-mark answer from an average one.

Applications of Glutamate—prephenate aminotransferase

In research: Glutamate—prephenate aminotransferase appears in engineering research whenever the underlying quantities have to be modelled precisely. Papers usually cite it as a starting assumption and then explore where it breaks down.
In technology and industry: Engineering practice reuses Glutamate—prephenate aminotransferase in design rules, simulations and safety margins. Knowing the idea lets you read a specification sheet and understand why the numbers look the way they do.
In the classroom: Glutamate—prephenate aminotransferase is common in secondary-school and first-year university syllabi. It links to neighbouring topics EC 2.6.1, Enzymes of unknown structure, so understanding it makes those chapters shorter.
In everyday life: Look for Glutamate—prephenate aminotransferase outside the textbook — in sport, cooking, traffic, electronics or the sky above you. An example you found yourself is remembered far longer than one you were given.

Ask Teacher Smith questions about this articleOpens your AI tutor with a question about “Glutamate—prephenate aminotransferase” →

Affiliate

Preply — study more efficiently by working with a personal tutor. 50% off.

How to study Glutamate—prephenate aminotransferase in 20 minutes

Read the reference excerpt below once, without taking notes.
Close the page and write down what Glutamate—prephenate aminotransferase means in your own words.
Compare your version with the excerpt and mark what you missed.
Work through the three examples above with pen and paper.
Explain Glutamate—prephenate aminotransferase out loud to somebody else — or to Teacher Smith in the lgStudy chat.

Frequently asked questions

What is Glutamate—prephenate aminotransferase in simple terms?

In enzymology, glutamate-prephenate aminotransferase (EC 2.6.1.79, also known as prephenate transaminase, PAT, and L-glutamate:prephenate aminotransferase) is an enzyme that catalyzes the chemical reaction L-arogenate + 2-oxoglutarate ⇌ {\displaystyle \rightleftharpoons } prephenate + L-glutamate T…

Why does Glutamate—prephenate aminotransferase matter?

Because it connects several engineering ideas at once: it gives you a definition you can apply, a quantity you can calculate, and a way to check whether a result is plausible.

How should I study Glutamate—prephenate aminotransferase?

Read the excerpt, restate it from memory, then work through the examples and applications listed on this page. The five-step study plan above takes about twenty minutes.

What does this page cover?

It gives you a compact reference excerpt plus original lgStudy explanations, examples, applications and study material on Glutamate—prephenate aminotransferase.