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Leucocyanidin oxygenase

Leucocyanidin oxygenase 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 Leucocyanidin oxygenase rather than just read about it. In short: In enzymology, a leucocyanidin oxygenase (EC 1.14.20.4) is an enzyme that catalyzes the chemical reaction leucocyanidin + 2-oxoglutarate + O2 ⇌ {\displaystyle \rightleftharpoons } cis- and trans-dihydroquercetins + succinate + CO2 + 2 H2O The 3 substrates of this enzyme are leucocyanidin, 2-oxoglutarate, and O2, whereas its 5 products are cis-dihydroquercetin, trans-dihydroquercetin, succinate, CO2, and H2O. This en…

Key takeaways

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

Reference excerpt

In enzymology, a leucocyanidin oxygenase (EC 1.14.20.4) is an enzyme that catalyzes the chemical reaction

leucocyanidin + 2-oxoglutarate + O2 ⇌ {\displaystyle \rightleftharpoons } cis- and trans-dihydroquercetins + succinate + CO2 + 2 H2O The 3 substrates of this enzyme are leucocyanidin, 2-oxoglutarate, and O2, whereas its 5 products are cis-dihydroquercetin, trans-dihydroquercetin, succinate, CO2, and H2O. This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2 with 2-oxoglutarate as one donor, and incorporation of one atom o oxygen into each donor. The systematic name of this enzyme class is leucocyanidin,2-oxoglutarate:oxygen oxidoreductase. This enzyme is also called leucoanthocyanidin dioxygenase (LDOX) or anthocyanidin synthase (ANS). This enzyme participates in flavonoid biosynthesis. In a broader way, leucocyanidin oxygenase uses flavan-3,4-diols (leucoanthocyanidins) to produce 3-hydroxyanthocyanidins. The gene encoding the enzyme (PpLDOX) has been identified in peach and expression has been studied in Vitis vinifera.

Structural studies As of late 2007, only one structure, in Arabidopsis thaliana, has been solved for this class of enzymes, with the PDB accession code PDB: 2BRT​.

References

Further reading

Worked examples

Example 1 — a first encounter with Leucocyanidin oxygenase

Start with the simplest possible case. Write down what Leucocyanidin oxygenase 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 Leucocyanidin oxygenase 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 Leucocyanidin oxygenase 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 Leucocyanidin oxygenase

In research
Leucocyanidin oxygenase 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 Leucocyanidin oxygenase 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
Leucocyanidin oxygenase is common in secondary-school and first-year university syllabi. It links to neighbouring topics EC 1.14.20, EC 1.14 stubs, Enzymes of known structure, so understanding it makes those chapters shorter.
In everyday life
Look for Leucocyanidin oxygenase 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 Leucocyanidin oxygenase in 20 minutes

  1. Read the reference excerpt below once, without taking notes.
  2. Close the page and write down what Leucocyanidin oxygenase 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 Leucocyanidin oxygenase out loud to somebody else — or to Teacher Smith in the lgStudy chat.

Frequently asked questions

What is Leucocyanidin oxygenase in simple terms?

In enzymology, a leucocyanidin oxygenase (EC 1.14.20.4) is an enzyme that catalyzes the chemical reaction leucocyanidin + 2-oxoglutarate + O2 ⇌ {\displaystyle \rightleftharpoons } cis- and trans-dihydroquercetins + succinate + CO2 + 2 H2O The 3 substrates of this enzyme are leucocyanidin, 2-oxoglut…

Why does Leucocyanidin oxygenase 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 Leucocyanidin oxygenase?

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 Leucocyanidin oxygenase.

Tags

  • EC 1.14.20
  • EC 1.14 stubs
  • Enzymes of known structure
  • Flavanonols metabolism

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