hydroxyacyl-CoA dehydrogenase
अंतिम अद्यतन 25 जुलाई 2023
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The HADH gene provides instructions for making an enzyme called 3-hydroxyacyl-CoA dehydrogenase that is important for converting certain fats to energy. This enzyme is involved in a process called fatty acid oxidation, in which several enzymes work in a step-wise fashion to break down (metabolize) fats and convert them to energy. The role of 3-hydroxyacyl-CoA dehydrogenase is to metabolize groups of fats called medium-chain fatty acids and short-chain fatty acids. These fatty acids are found in foods such as milk and certain oils and are produced when larger fatty acids are metabolized.
Normal function
The HADH gene provides instructions for making an enzyme called 3-hydroxyacyl-CoA dehydrogenase that is important for converting certain fats to energy. This enzyme is involved in a process called fatty acid oxidation, in which several enzymes work in a step-wise fashion to break down (metabolize) fats and convert them to energy. The role of 3-hydroxyacyl-CoA dehydrogenase is to metabolize groups of fats called medium-chain fatty acids and short-chain fatty acids. These fatty acids are found in foods such as milk and certain oils and are produced when larger fatty acids are metabolized.
3-hydroxyacyl-CoA dehydrogenase functions in mitochondria, the energy-producing centers within cells. This enzyme is especially important for the normal functioning of the heart, liver, kidneys, muscles, and pancreas. The pancreas makes enzymes that help digest food, and it also produces insulin, which controls how much sugar (glucose) is passed from the blood into cells for conversion to energy.
3-hydroxyacyl-CoA dehydrogenase is essential in the process that converts medium-chain and short-chain fatty acids to ketones, the major source of energy used by the heart and muscles. During prolonged periods without food (fasting) or when energy demands are increased, ketones are also important for the liver and other tissues.
Conditions referring to this gene or chromosome
Other names
HAD
HADH1
HADHSC
HCDH_HUMAN
HHF4
hydroxyacyl-Coenzyme A dehydrogenase
L-3-hydroxyacyl-Coenzyme A dehydrogenase
L-3-hydroxyacyl-Coenzyme A dehydrogenase, short chain
M/SCHAD
medium and short chain L-3-hydroxyacyl-coenzyme A dehydrogenase
MGC8392
SCHAD
short chain 3-hydroxyacyl-CoA dehydrogenase
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अधिक पठन और संदर्भ
- hydroxyacyl-CoA dehydrogenase; MedlinePlus, National Library of Medicine.
- Bennett MJ, Russell LK, Tokunaga C, Narayan SB, Tan L, Seegmiller A, Boriack RL, Strauss AW. Reye-like syndrome resulting from novel missense mutations in mitochondrial medium- and short-chain l-3-hydroxy-acyl-CoA dehydrogenase. Mol Genet Metab. 2006 Sep-Oct;89(1-2):74-9. doi: 10.1016/j.ymgme.2006.04.004. Epub 2006 May 24.
- Clayton PT, Eaton S, Aynsley-Green A, Edginton M, Hussain K, Krywawych S, Datta V, Malingre HE, Berger R, van den Berg IE. Hyperinsulinism in short-chain L-3-hydroxyacyl-CoA dehydrogenase deficiency reveals the importance of beta-oxidation in insulin secretion. J Clin Invest. 2001 Aug;108(3):457-65. doi: 10.1172/JCI11294.
- Hussain K, Clayton PT, Krywawych S, Chatziandreou I, Mills P, Ginbey DW, Geboers AJ, Berger R, van den Berg IE, Eaton S. Hyperinsulinism of infancy associated with a novel splice site mutation in the SCHAD gene. J Pediatr. 2005 May;146(5):706-8. doi: 10.1016/j.jpeds.2005.01.032.
- Kapoor RR, James C, Flanagan SE, Ellard S, Eaton S, Hussain K. 3-Hydroxyacyl-coenzyme A dehydrogenase deficiency and hyperinsulinemic hypoglycemia: characterization of a novel mutation and severe dietary protein sensitivity. J Clin Endocrinol Metab. 2009 Jul;94(7):2221-5. doi: 10.1210/jc.2009-0423. Epub 2009 May 5.
- Molven A, Matre GE, Duran M, Wanders RJ, Rishaug U, Njolstad PR, Jellum E, Sovik O. Familial hyperinsulinemic hypoglycemia caused by a defect in the SCHAD enzyme of mitochondrial fatty acid oxidation. Diabetes. 2004 Jan;53(1):221-7. doi: 10.2337/diabetes.53.1.221.
- Yang SY, He XY, Schulz H. 3-Hydroxyacyl-CoA dehydrogenase and short chain 3-hydroxyacyl-CoA dehydrogenase in human health and disease. FEBS J. 2005 Oct;272(19):4874-83. doi: 10.1111/j.1742-4658.2005.04911.x.
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