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Glutathionylspermidine amidase

Glutathionylspermidine amidase 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 Glutathionylspermidine amidase rather than just read about it. In short: In enzymology, a glutathionylspermidine amidase (EC 3.5.1.78) is an enzyme that catalyzes the chemical reaction glutathionylspermidine + H2O ⇌ {\displaystyle \rightleftharpoons } glutathione + spermidine Thus, the two substrates of this enzyme are glutathionylspermidine and H2O, whereas its two products are glutathione and spermidine. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen b…

Key takeaways

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

Reference excerpt

In enzymology, a glutathionylspermidine amidase (EC 3.5.1.78) is an enzyme that catalyzes the chemical reaction

glutathionylspermidine + H2O ⇌ {\displaystyle \rightleftharpoons } glutathione + spermidine Thus, the two substrates of this enzyme are glutathionylspermidine and H2O, whereas its two products are glutathione and spermidine. This enzyme belongs to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear amides. The systematic name of this enzyme class is gamma-L-glutamyl-L-cysteinyl-glycine:spermidine amidase. This enzyme is also called glutathionylspermidine amidohydrolase (spermidine-forming). This enzyme participates in glutathione metabolism.

Structural studies As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes PDB: 2IO7​, PDB: 2IO8​, PDB: 2IO9​, PDB: 2IOA​, and PDB: 2IOB​.

References

Bollinger JM, Kwon DS, Huisman GW, Kolter R, Walsh CT (1995). "Glutathionylspermidine metabolism in Escherichia coli. Purification, cloning, overproduction, and characterization of a bifunctional glutathionylspermidine synthetase/amidase". J. Biol. Chem. 270 (23): 14031–41. doi:10.1074/jbc.270.23.14031. PMID 7775463.

Worked examples

Example 1 — a first encounter with Glutathionylspermidine amidase

Start with the simplest possible case. Write down what Glutathionylspermidine amidase 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 Glutathionylspermidine amidase 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 Glutathionylspermidine amidase 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 Glutathionylspermidine amidase

In research
Glutathionylspermidine amidase 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 Glutathionylspermidine amidase 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
Glutathionylspermidine amidase is common in secondary-school and first-year university syllabi. It links to neighbouring topics EC 3.5.1, EC 3.5 stubs, Enzymes of known structure, so understanding it makes those chapters shorter.
In everyday life
Look for Glutathionylspermidine amidase 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 Glutathionylspermidine amidase in 20 minutes

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

Frequently asked questions

What is Glutathionylspermidine amidase in simple terms?

In enzymology, a glutathionylspermidine amidase (EC 3.5.1.78) is an enzyme that catalyzes the chemical reaction glutathionylspermidine + H2O ⇌ {\displaystyle \rightleftharpoons } glutathione + spermidine Thus, the two substrates of this enzyme are glutathionylspermidine and H2O, whereas its two pro…

Why does Glutathionylspermidine amidase 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 Glutathionylspermidine amidase?

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 Glutathionylspermidine amidase.

Tags

  • EC 3.5.1
  • EC 3.5 stubs
  • Enzymes of known structure

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