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Histidine transaminase

Histidine transaminase 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 Histidine transaminase rather than just read about it. In short: Histidine transaminase (EC 2.6.1.38) is an enzyme that catalyzes the chemical reaction The two substrates of this enzyme characterised from Escherichia coli and Pseudomonas acidovorans are L-histidine and α-ketoglutaric acid. Its products are imidazole-4-pyruvic acid and L-glutamic acid.

Histidine transaminase — main illustration
Histidine transaminase — illustration

Key takeaways

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

Reference excerpt

Histidine transaminase (EC 2.6.1.38) is an enzyme that catalyzes the chemical reaction

The two substrates of this enzyme characterised from Escherichia coli and Pseudomonas acidovorans are L-histidine and α-ketoglutaric acid. Its products are imidazole-4-pyruvic acid and L-glutamic acid. This enzyme is a transferase, specifically a transaminase, which transfer nitrogenous groups. The systematic name of this enzyme class is L-histidine:2-oxoglutarate aminotransferase. Other names in common use include histidine aminotransferase, and histidine-2-oxoglutarate aminotransferase. It participates in histidine metabolism.

References

Illustrations

Histidine transaminase illustration
Histidine transaminase illustration
Histidine transaminase illustration
Histidine transaminase illustration

Worked examples

Example 1 — a first encounter with Histidine transaminase

Start with the simplest possible case. Write down what Histidine transaminase 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 Histidine transaminase 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 Histidine transaminase 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 Histidine transaminase

In research
Histidine transaminase 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 Histidine transaminase 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
Histidine transaminase is common in secondary-school and first-year university syllabi. It links to neighbouring topics EC 2.6.1, EC 2.6 stubs, Enzymes of unknown structure, so understanding it makes those chapters shorter.
In everyday life
Look for Histidine transaminase 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.
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How to study Histidine transaminase in 20 minutes

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

Frequently asked questions

What is Histidine transaminase in simple terms?

Histidine transaminase (EC 2.6.1.38) is an enzyme that catalyzes the chemical reaction The two substrates of this enzyme characterised from Escherichia coli and Pseudomonas acidovorans are L-histidine and α-ketoglutaric acid. Its products are imidazole-4-pyruvic acid and L-glutamic acid.

Why does Histidine transaminase 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 Histidine transaminase?

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 Histidine transaminase.

Tags

  • EC 2.6.1
  • EC 2.6 stubs
  • Enzymes of unknown structure

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