dihydrolipoamide dehydrogenase
آخر تحديث 3 Apr 2025
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ال DLD gene provides instructions for making an enzyme called dihydrolipoamide dehydrogenase. This enzyme forms one part (subunit), called the E3 component, of several groups of enzymes that work together (enzyme complexes). These complexes are essential for the breakdown of certain molecules to produce energy in cells.
Normal function
ال DLD gene provides instructions for making an enzyme called dihydrolipoamide dehydrogenase. This enzyme forms one part (subunit), called the E3 component, of several groups of enzymes that work together (enzyme complexes). These complexes are essential for the breakdown of certain molecules to produce energy in cells.
Branched-chain alpha-keto acid dehydrogenase, or BCKD, is one of the enzyme complexes that include dihydrolipoamide dehydrogenase. The BCKD enzyme complex performs one step in the breakdown of three protein building blocks (amino acids). These amino acids—leucine, isoleucine, and valine—are obtained from the diet. They are present in many kinds of food, particularly protein-rich foods such as milk, meat, and eggs. The breakdown of these amino acids produces molecules that can be used for energy.
Dihydrolipoamide dehydrogenase is also part of the pyruvate dehydrogenase (PDH) complex. This enzyme complex plays an important role in the production of energy for cells. It converts a molecule called pyruvate, which is formed from the breakdown of carbohydrates, into another molecule called acetyl-CoA. Dihydrolipoamide dehydrogenase performs one step of this chemical reaction. The conversion of pyruvate is essential to begin the series of chemical reactions that ultimately produces adenosine triphosphate (ATP), the cell's main energy source.
Dihydrolipoamide dehydrogenase is part of a third enzyme complex involved in cellular energy production. This complex, called alpha-ketoglutarate dehydrogenase (αKGDH), converts a molecule called α-ketoglutarate to another molecule called succinyl-CoA. Further steps in this process generate ATP for cells to use as energy.
Conditions referring to this gene or chromosome
Other names
DIA1
diaphorase
dihydrolipoamide dehydrogenase (E3 component of pyruvate dehydrogenase complex, 2-oxo-glutarate complex, branched chain keto acid dehydrogenase complex)
dihydrolipoyl dehydrogenase
DLDH
DLDH_HUMAN
E3 component of pyruvate dehydrogenase
GCSL
glycine cleavage system L protein
LAD
lipoamide dehydrogenase
lipoamide reductase
lipoamide reductase (NADH)
lipoyl dehydrogenase
PHE3
pyruvate dehydrogenase component E3
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قراءة إضافية ومراجع
- dihydrolipoamide dehydrogenase; MedlinePlus, National Library of Medicine.
- Ambrus A, Adam-Vizi V. Molecular dynamics study of the structural basis of dysfunction and the modulation of reactive oxygen species generation by pathogenic mutants of human dihydrolipoamide dehydrogenase. Arch Biochem Biophys. 2013 Oct 15;538(2):145-55. doi: 10.1016/j.abb.2013.08.015. Epub 2013 Sep 3.
- Biochemistry (fifth edition, 2002): The Formation of Acetyl Coenzyme A from Pyruvate
- Brautigam CA, Chuang JL, Tomchick DR, Machius M, Chuang DT. Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations. J Mol Biol. 2005 Jul 15;350(3):543-52. doi: 10.1016/j.jmb.2005.05.014.
- Cerna L, Wenchich L, Hansikova H, Kmoch S, Peskova K, Chrastina P, Brynda J, Zeman J. Novel mutations in a boy with dihydrolipoamide dehydrogenase deficiency. Med Sci Monit. 2001 Nov-Dec;7(6):1319-25.
- Feigenbaum AS, Robinson BH. The structure of the human dihydrolipoamide dehydrogenase gene (DLD) and its upstream elements. Genomics. 1993 Aug;17(2):376-81. doi: 10.1006/geno.1993.1335.
- Hong YS, Kerr DS, Liu TC, Lusk M, Powell BR, Patel MS. Deficiency of dihydrolipoamide dehydrogenase due to two mutant alleles (E340K and G101del). Analysis of a family and prenatal testing. Biochim Biophys Acta. 1997 Dec 31;1362(2-3):160-8. doi: 10.1016/s0925-4439(97)00073-2.
- Patel MS, Korotchkina LG, Sidhu S. Interaction of E1 and E3 components with the core proteins of the human pyruvate dehydrogenase complex. J Mol Catal B Enzym. 2009 Nov 1;61(1-2):2-6. doi: 10.1016/j.molcatb.2009.05.001.
- Saada A, Aptowitzer I, Link G, Elpeleg ON. ATP synthesis in lipoamide dehydrogenase deficiency. Biochem Biophys Res Commun. 2000 Mar 16;269(2):382-6. doi: 10.1006/bbrc.2000.2310.
- Shaag A, Saada A, Berger I, Mandel H, Joseph A, Feigenbaum A, Elpeleg ON. Molecular basis of lipoamide dehydrogenase deficiency in Ashkenazi Jews. Am J Med Genet. 1999 Jan 15;82(2):177-82.
- Shany E, Saada A, Landau D, Shaag A, Hershkovitz E, Elpeleg ON. Lipoamide dehydrogenase deficiency due to a novel mutation in the interface domain. Biochem Biophys Res Commun. 1999 Aug 19;262(1):163-6. doi: 10.1006/bbrc.1999.1133.
تاريخ المقال
المقال متاح أيضًا باللغة الإنجليزية, الألمانية, إسبانية, الفرنسية, إيطالي, البرتغالية, الهندية, العبرية, العربية ,، و السويدية.
3 Apr 2025 | أحدث إصدار
1 Sept 2014 | نُشر في الأصل
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