chemistry

L-amino-acid dehydrogenase

L-amino-acid dehydrogenase is a chemistry 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 L-amino-acid dehydrogenase rather than just read about it. In short: In enzymology, a L-amino-acid dehydrogenase (EC 1.4.1.5) is an enzyme that catalyzes the chemical reaction an L-amino acid + H2O + NAD+ ⇌ a 2-oxo acid + NH3 + NADH + H+ The 3 substrates of this enzyme are L-amino acid, H2O, and NAD+, whereas its 4 products are 2-oxo acid, NH3, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP…

Key takeaways

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

Reference excerpt

In enzymology, a L-amino-acid dehydrogenase (EC 1.4.1.5) is an enzyme that catalyzes the chemical reaction

an L-amino acid + H2O + NAD+ ⇌ a 2-oxo acid + NH3 + NADH + H+ The 3 substrates of this enzyme are L-amino acid, H2O, and NAD+, whereas its 4 products are 2-oxo acid, NH3, NADH, and H+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-amino-acid:NAD+ oxidoreductase (deaminating).

See also Amino acid Dehydrogenase Oxidoreductase Enzyme Nicotinamide adenine dinucleotide Transaminase Oxidative deamination

References

Nisman B, Mager J (February 1952). "Diphosphopyridine nucleotide and phosphate requirement for oxidation of amino-acids by cell-free extracts of obligate anaerobes". Nature. 169 (4293): 243–4. Bibcode:1952Natur.169..243N. doi:10.1038/169243a0. PMID 14910739.

Worked examples

Example 1 — a first encounter with L-amino-acid dehydrogenase

Start with the simplest possible case. Write down what L-amino-acid dehydrogenase claims or describes in one sentence, then invent the smallest concrete situation in which that sentence is true. In chemistry, 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 L-amino-acid dehydrogenase 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 L-amino-acid dehydrogenase 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 L-amino-acid dehydrogenase

In research: L-amino-acid dehydrogenase appears in chemistry 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 L-amino-acid dehydrogenase 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: L-amino-acid dehydrogenase is common in secondary-school and first-year university syllabi. It links to neighbouring topics EC 1.4.1, Enzymes of unknown structure, NADH-dependent enzymes, so understanding it makes those chapters shorter.
In everyday life: Look for L-amino-acid dehydrogenase 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 L-amino-acid dehydrogenase in 20 minutes

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

Frequently asked questions

What is L-amino-acid dehydrogenase in simple terms?

In enzymology, a L-amino-acid dehydrogenase (EC 1.4.1.5) is an enzyme that catalyzes the chemical reaction an L-amino acid + H2O + NAD+ ⇌ a 2-oxo acid + NH3 + NADH + H+ The 3 substrates of this enzyme are L-amino acid, H2O, and NAD+, whereas its 4 products are 2-oxo acid, NH3, NADH, and H+. This en…

Why does L-amino-acid dehydrogenase matter?

Because it connects several chemistry 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 L-amino-acid dehydrogenase?

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 L-amino-acid dehydrogenase.