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Palmitoyl-CoA hydrolase

Palmitoyl-CoA hydrolase 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 Palmitoyl-CoA hydrolase rather than just read about it. In short: Palmitoyl-CoA hydrolase (EC 3.1.2.2) is an enzyme in the family of hydrolases that specifically acts on thioester bonds. It catalyzes the hydrolysis of long chain fatty acyl thioesters of acyl carrier protein or coenzyme A to form free fatty acid and the corresponding thiol: palmitoyl-CoA + H2O = CoA + palmitate It has a strict specificity for thioesters with a chain link greater than C10.

Palmitoyl-CoA hydrolase — main illustration
Palmitoyl-CoA hydrolase — illustration

Key takeaways

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

Reference excerpt

Palmitoyl-CoA hydrolase (EC 3.1.2.2) is an enzyme in the family of hydrolases that specifically acts on thioester bonds. It catalyzes the hydrolysis of long chain fatty acyl thioesters of acyl carrier protein or coenzyme A to form free fatty acid and the corresponding thiol:

palmitoyl-CoA + H2O = CoA + palmitate It has a strict specificity for thioesters with a chain link greater than C10. These enzymes are localized in almost all cellular compartments, such as endoplasmic reticulum, cytosol, mitochondria, and peroxisomes. They are highly regulated by peroxisome proliferator activated receptors, which led to their involvement in lipid metabolism. The enzyme is up-regulated during times of increased fatty acid oxidation, which suggests that this enzyme has a potential role the peroxisomal beta-oxidation. The systematic name is palmitoyl-CoA hydrolase. Other names in common use include long-chain fatty-acyl-CoA hydrolase, palmitoyl coenzyme A hydrolase, palmitoyl thioesterase, palmitoyl coenzyme A hydrolase, palmitoyl-CoA deacylase, palmityl thioesterase, palmityl-CoA deacylase, fatty acyl thioesterase I, and palmityl thioesterase I.

Structural studies

As of late 2007, 3 structures have been solved for this class of enzymes, with PDB accession codes PDB: 1TBU​, PDB: 2Q2B​, and PDB: 2QQ2​.

Mechanism At a subcellular level, palmitoyl-CoA hydrolase is localized in the endoplasmic reticulum, cytosol, mitochondria, and peroxisomes. Studies have shown that in rats that are fed high fat diets, palmitoyl-CoA hydrolase activity in the liver increased. While the details of the mechanism are not known, the results suggest that there is an "induction" mechanism taking place for palmitoyl-CoA hydrolase and peroxisomal beta-oxidation enzymes.

Disease Relevance Diabetes is the most common cause of liver disease in the U.S., type 2 diabetes. Studies have been done to show that, while there is not direct correlation between palmitoyl-CoA hydrolase and diabetes, streptozotocin-induced diabetes significantly decreased rat liver palmitoyl-CoA hydrolase. This led to high levels of fatty acyl-CoA being present in the liver, which shows that a diseased liver cannot regulate the amount of fatty acyl-CoA that is present versus a normal, healthy liver. A defect in acyl-CoA degradation in livers can produce hyperammonemia and hypoglycemia.

References

Barnes EM Jr; Wakil SJ (1968). "Studies on the mechanism of fatty acid synthesis. XIX. Preparation and general properties of palmityl thioesterase". Journal of Biological Chemistry. 243 (11): 2955–62. doi:10.1016/S0021-9258(18)93365-X. PMID 4871199. Berge RK, Farstad M (1981). "Long-chain fatty acyl-CoA hydrolase from rat liver mitochondria". Lipids Part C. Methods in Enzymology. Vol. 71. pp. 234–42. doi:10.1016/0076-6879(81)71030-9. ISBN 9780121819712. PMID 6116156. Miyazawa S, Furuta S, Hashimoto T (1981). "Induction of a novel long-chain acyl-CoA hydrolase in rat liver by administration of peroxisome proliferators". European Journal of Biochemistry. 117 (2): 425–30. doi:10.1111/j.1432-1033.1981.tb06356.x. PMID 6115749. Srere PA, Seubert W, Lynen F (1959). "Palmityl coenzyme A deacylase" (PDF). Biochimica et Biophysica Acta. 33 (2): 313–319. doi:10.1016/0006-3002(59)90118-0. hdl:2027.42/32457. PMID 13670899. Yabusaki KK; Ballou CE (1981). "Long-chain fatty acyl-CoA thioesterases from Mycobacterium smegmatis". Lipids Part C. Methods in Enzymology. Vol. 71. pp. 242–246. doi:10.1016/0076-6879(81)71031-0. ISBN 978-0-12-181971-2. Berge RK, Nilsson A, Husøy AM (1988). "Rapid stimulation of liver palmitoyl-CoA synthetase, carnitine palmitoyltransferase and glycerophosphate acyltransferase compared to peroxisomal β-oxidation and palmitoyl-CoA hydrolase in rats fed high-fat diets". Biochimica et Biophysica Acta (BBA) - Lipids and Lipid Metabolism. 960 (3): 417–26. doi:10.1016/0005-2760(88)90050-1. PMID 2898261. Berge RK, Thomassen MS (1985). "Effects of high fat diets on the activity of palmitoyl-CoA hydrolase in rat liver". Lipids. 20 (1): 49–52. doi:10.1007/bf02534363. PMID 2857471. S2CID 4036488.. Berge RK, Farstad M (1979). "Purification and Characterization of Long-Chain Acyl-CoA Hydrolase from Rat Liver Mitochondria". FEBS Journal. 96 (2): 393–401. doi:10.1111/j.1432-1033.1979.tb13051.x. PMID 37085. Barnes E, Wakil S (1968). "Studies of the Mechanism of Fatty Acid Synthesis". Journal of Biological Chemistry. 243 (11): 2955–2962. doi:10.1016/S0021-9258(18)93365-X. Tolman K, Fonseca V, Dalpiazm A, Tan M (2007). "Spectrum of Liver Disease in Type 2 Diabetes and Management of Patients with Diabetes and Liver Disease". Diabetes Care. 30 (3): 734–743. doi:10.2337/dc06-1539. PMID 17327353. Dang AQ, Fass FH (1984). "Effects of Streptozotocin-Induced Diabetes on Microsomal Long-Chain Fatty Acyl-CoA Synthetase and Hydrolase". Lipids. 19 (8): 578–582. doi:10.1007/bf02534714. PMID 6148682. S2CID 4045839. Tilton G, Shockey J, Browse J (2004). "Biochemical and Molecular Characterization of ACH2, an Acyl-CoA Thioesterase from Arabidopsis thaliana". Journal of Biological Chemistry. 279 (9): 7487–7494. doi:10.1074/jbc.M309532200. PMID 14660652.

Worked examples

Example 1 — a first encounter with Palmitoyl-CoA hydrolase

Start with the simplest possible case. Write down what Palmitoyl-CoA hydrolase 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 Palmitoyl-CoA hydrolase 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 Palmitoyl-CoA hydrolase 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 Palmitoyl-CoA hydrolase

In research
Palmitoyl-CoA hydrolase 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 Palmitoyl-CoA hydrolase 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
Palmitoyl-CoA hydrolase is common in secondary-school and first-year university syllabi. It links to neighbouring topics EC 3.1.2, EC 3.1 stubs, Enzymes of known structure, so understanding it makes those chapters shorter.
In everyday life
Look for Palmitoyl-CoA hydrolase 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 Palmitoyl-CoA hydrolase in 20 minutes

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

Frequently asked questions

What is Palmitoyl-CoA hydrolase in simple terms?

Palmitoyl-CoA hydrolase (EC 3.1.2.2) is an enzyme in the family of hydrolases that specifically acts on thioester bonds. It catalyzes the hydrolysis of long chain fatty acyl thioesters of acyl carrier protein or coenzyme A to form free fatty acid and the corresponding thiol: palmitoyl-CoA + H2O = C…

Why does Palmitoyl-CoA hydrolase 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 Palmitoyl-CoA hydrolase?

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 Palmitoyl-CoA hydrolase.

Tags

  • EC 3.1.2
  • EC 3.1 stubs
  • Enzymes of known structure

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