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Haloacetate dehalogenase

Haloacetate dehalogenase 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 Haloacetate dehalogenase rather than just read about it. In short: In enzymology, a haloacetate dehalogenase (EC 3.8.1.3) is an enzyme that catalyzes the chemical reaction haloacetate + H2O ⇌ {\displaystyle \rightleftharpoons } glycolate + halide Thus, the two substrates of this enzyme are haloacetate and H2O, whereas its two products are glycolate and halide. For example, in the case of fluoroacetate it will produce glycolate and fluoride.

Haloacetate dehalogenase — main illustration
Haloacetate dehalogenase — illustration

Key takeaways

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

Reference excerpt

In enzymology, a haloacetate dehalogenase (EC 3.8.1.3) is an enzyme that catalyzes the chemical reaction

haloacetate + H2O ⇌ {\displaystyle \rightleftharpoons } glycolate + halide Thus, the two substrates of this enzyme are haloacetate and H2O, whereas its two products are glycolate and halide. For example, in the case of fluoroacetate it will produce glycolate and fluoride. This enzyme belongs to the family of hydrolases, one of the largest known enzyme families comprising approximately 1% of the genes in the human genome, exists as a homodimer, and acts specifically on halide bonds in carbon-halide compounds. The systematic name of this enzyme class is haloacetate halidohydrolase. This enzyme is also called monohaloacetate dehalogenase and fluoroacetate dehalogenase. This enzyme participates in gamma-hexachlorocyclohexane degradation and 1,2-dichloroethane degradation.

Reactions Haloacetate dehalogenase is unique because it catalyzes the cleavage of the remarkably stable carbon–fluorine bond of a fluorinated aliphatic compound. In the reaction of L-2-haloacid dehalogenase and fluoroacetate dehalogenase, the carboxylate group performs a nucleophilic attack on the alpha-carbon atom, moving the halogen atom. This action is common to haloalkane dehalogenase and 4-chlorobenzoyl-CoA dehalogenase. DL-2-Haloacid dehalogenase is unique in that a water molecule directly attacks the substrate, displacing the halogen atom.

Significance As fluoroacetate is poisonous and present in plants endemic to Australia, Africa, and Central America, livestock are often killed by fluoroacetate poisoning. Fluoroacetate is lethal to sheep and cattle at doses of 0.25 to 0.5 mg/kg of body weight, and is a problem in the livestock industry. A fluoroacetate dehalogenase gene from the soil bacterium Moraxella species strain B was transferred into the rumen bacterium Butyrivibrio fibrisolvens and expressed in vitro at sufficiently high levels to detoxify fluoroacetate in the surrounding medium. Scientists and farmers want to determine a way to get B. fibrisolvens into either the animals or plants.

Structural studies As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code PDB: 1Y37​.

References

GOLDMAN P (1965). "The Enzymatic Cleavage of the Carbon-Fluorine Bond in Fluoroacetate". J. Biol. Chem. 240 (8): 3434–8. doi:10.1016/S0021-9258(18)97236-4. PMID 14321384. Goldman P, Milne GW (1966). "Carbon-fluorine bond cleavage. II. Studies on the mechanism of the defluorination of fluoroacetate". J. Biol. Chem. 241 (23): 5557–9. doi:10.1016/S0021-9258(18)96379-9. PMID 5928195. The Japan Chemical Journal Forum and Wiley Periodicals, Inc.2008 MacKenzie, D. Trouble in the wind over altered soya beans. New Scientist. Vol 148 (2006), pp12. December 2, 1995 1995 Soy Stats. American Soybean Association Homepage. Plant biotech will hit farming sector radar screen in 1996. BioBusiness. December 8, 1995 Tatsuo Kurihara Journal of Biochemistry. Vol. 131, pp. 671–677 (2002), Regular paper;2002

Illustrations

Haloacetate dehalogenase illustration

Worked examples

Example 1 — a first encounter with Haloacetate dehalogenase

Start with the simplest possible case. Write down what Haloacetate dehalogenase 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 Haloacetate dehalogenase 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 Haloacetate dehalogenase 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 Haloacetate dehalogenase

In research
Haloacetate dehalogenase 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 Haloacetate dehalogenase 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
Haloacetate dehalogenase is common in secondary-school and first-year university syllabi. It links to neighbouring topics EC 3.8.1, Enzymes of known structure, Hydrolase stubs, so understanding it makes those chapters shorter.
In everyday life
Look for Haloacetate dehalogenase 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 Haloacetate dehalogenase in 20 minutes

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

Frequently asked questions

What is Haloacetate dehalogenase in simple terms?

In enzymology, a haloacetate dehalogenase (EC 3.8.1.3) is an enzyme that catalyzes the chemical reaction haloacetate + H2O ⇌ {\displaystyle \rightleftharpoons } glycolate + halide Thus, the two substrates of this enzyme are haloacetate and H2O, whereas its two products are glycolate and halide. For…

Why does Haloacetate dehalogenase 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 Haloacetate dehalogenase?

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 Haloacetate dehalogenase.

Tags

  • EC 3.8.1
  • Enzymes of known structure
  • Hydrolase stubs

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