science

Imine reductase

Imine reductase is a science 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 Imine reductase rather than just read about it. In short: An imine reductase (IRED) is an enzyme that reduces imines to amines. This family of enzymes is employed in the industrial production of amine-containing pharmaceuticals.

Key takeaways

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

Reference excerpt

An imine reductase (IRED) is an enzyme that reduces imines to amines. This family of enzymes is employed in the industrial production of amine-containing pharmaceuticals. The IRED enzymes that are found to catalyze both imine formation and imine reduction are called reductive aminases (RedAms).

Discovery IREDs were originally discovered in 2010 by screening bacterial strains for reducing activity on 2-methyl-1-pyrroline (2-MPN). Based on each member's ability to reduce 2-MPN to (R)- or (S)-2-methylpyrrolidine they are designated as R-selective or S-selective, respectively.

Applications IREDs have been employed to reduce imines formed from ketone-amine mixtures. The conversion is not a genuine reductive amination as only the second half of the two-part reaction is catalyzed. In 2017 an IRED was discovered that catalyzed both steps of reductive amination of a wide scope of ketone-amine pairs. These are dubbed reductive aminases (RedAms). Engineered RedAms have been employed in industrial processes to support production of pharmaceuticals for clinical trials and commercial manufacturing.

Structure IREDs are dimeric enzymes with each protomer having an N-terminal Rossmann nucleotide-binding domain and a C-terminal dimerization domain joined by a long interdomain α-helix. Each protomer's α-helical dimerization domain wraps around the interdomain helix of its dimer partner forming the substrate-binding cleft above the NAD(P)H cofactor binding site in the Rossmann domain. 3-Hydroxybutyrate dehydrogenases have similar N-terminal nucleotide-binding and C-terminal dimerization domains, but do not share the extensive dimerization interface of IREDs.

See also 3-Hydroxybutyrate dehydrogenase Opine dehydrogenase Pyrroline-2-carboxylate reductase Pyrroline-5-carboxylate reductase

References

Illustrations

Worked examples

Example 1 — a first encounter with Imine reductase

Start with the simplest possible case. Write down what Imine reductase claims or describes in one sentence, then invent the smallest concrete situation in which that sentence is true. In science, 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 Imine reductase 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 Imine reductase 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 Imine reductase

In research: Imine reductase appears in science 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 Imine reductase 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: Imine reductase is common in secondary-school and first-year university syllabi. It links to neighbouring topics Enzymes, so understanding it makes those chapters shorter.
In everyday life: Look for Imine reductase 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 Imine reductase in 20 minutes

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

Frequently asked questions

What is Imine reductase in simple terms?

An imine reductase (IRED) is an enzyme that reduces imines to amines. This family of enzymes is employed in the industrial production of amine-containing pharmaceuticals.

Why does Imine reductase matter?

Because it connects several science 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 Imine reductase?

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 Imine reductase.