二氢硫辛酰胺脱氢酶[1](英语:Dihydrolipoamide dehydrogenase,又称为硫辛酰胺脱氢酶,EC 1.8.1.4)是以NAD+为辅基接受质子与电子的一种脱氢酶,是大小为51千道尔顿亚基的同二聚体,其中每个都与一分子的黄素腺嘌呤二核苷酸以共价键的形式相连。在哺乳动物的线粒体三羧酸循环中,该酶与丙酮酸脱氢酶和二氢硫辛酰基乙酰基转基酶一起组成中丙酮酸脱氢酶复合体,同时该酶亦是α-酮戊二酸脱氢酶复合体中的一个组分。二氢硫辛酰胺脱氢酶的主要任务是负责将复合物中另一组分硫辛酰胺转乙酰基酶(或二氢硫辛酰琥珀酰转移酶)的辅基二氢硫辛酰胺脱氢从而转化为氧化型硫辛酰胺,该酶也是线粒体甘氨酸剪切体系的组分。
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- Silverberg MS, Cho JH, Rioux JD, et al.. Ulcerative colitis-risk loci on chromosomes 1p36 and 12q15 found by genome-wide association study.. Nat. Genet. 2009, 41 (2): 216–20. doi:10.1038/ng.275. PMC 2652837. PMID 19122664.
- Scherer SW, Cheung J, MacDonald JR, et al.. Human chromosome 7: DNA sequence and biology.. Science. 2003, 300 (5620): 767–72. doi:10.1126/science.1083423. PMC 2882961. PMID 12690205.
- Brautigam CA, Chuang JL, Tomchick DR, et al.. Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations.. J. Mol. Biol. 2005, 350 (3): 543–52. doi:10.1016/j.jmb.2005.05.014. PMID 15946682.
- , Barrett JC, Lee JC, et al.. Genome-wide association study of ulcerative colitis identifies three new susceptibility loci, including the HNF4A region.. Nat. Genet. 2009, 41 (12): 1330–4. doi:10.1038/ng.483. PMID 19915572.
- Reed LJ, Hackert ML. Structure-function relationships in dihydrolipoamide acyltransferases.. J. Biol. Chem. 1990, 265 (16): 8971–4. PMID 2188967.
- Ciszak EM, Makal A, Hong YS, et al.. How dihydrolipoamide dehydrogenase-binding protein binds dihydrolipoamide dehydrogenase in the human pyruvate dehydrogenase complex.. J. Biol. Chem. 2006, 281 (1): 648–55. doi:10.1074/jbc.M507850200. PMID 16263718.
- Asano K, Matsushita T, Umeno J, et al.. A genome-wide association study identifies three new susceptibility loci for ulcerative colitis in the Japanese population.. Nat. Genet. 2009, 41 (12): 1325–9. doi:10.1038/ng.482. PMID 19915573.
- Odièvre MH, Chretien D, Munnich A, et al.. A novel mutation in the dihydrolipoamide dehydrogenase E3 subunit gene (DLD) resulting in an atypical form of alpha-ketoglutarate dehydrogenase deficiency.. Hum. Mutat. 2005, 25 (3): 323–4. doi:10.1002/humu.9319. PMID 15712224.
- Brautigam CA, Wynn RM, Chuang JL, et al.. Structural insight into interactions between dihydrolipoamide dehydrogenase (E3) and E3 binding protein of human pyruvate dehydrogenase complex.. Structure. 2006, 14 (3): 611–21. doi:10.1016/j.str.2006.01.001. PMID 16442803.
- Kim H. Activity of human dihydrolipoamide dehydrogenase is largely reduced by mutation at isoleucine-51 to alanine.. J. Biochem. Mol. Biol. 2006, 39 (2): 223–7. PMID 16584639.
- Sugden MC, Holness MJ. Recent advances in mechanisms regulating glucose oxidation at the level of the pyruvate dehydrogenase complex by PDKs.. Am. J. Physiol. Endocrinol. Metab. 2003, 284 (5): E855–62. doi:10.1152/ajpendo.00526.2002. PMID 12676647.
- Wang YC, Wang ST, Li C, et al.. The role of amino acids T148 and R281 in human dihydrolipoamide dehydrogenase.. J. Biomed. Sci. 2008, 15 (1): 37–46. doi:10.1007/s11373-007-9208-9. PMID 17960497.
- Brown AM, Gordon D, Lee H, et al.. Association of the dihydrolipoamide dehydrogenase gene with Alzheimer's disease in an Ashkenazi Jewish population.. Am. J. Med. Genet. B Neuropsychiatr. Genet. 2004, 131B (1): 60–6. doi:10.1002/ajmg.b.30008. PMID 15389771.
- Babady NE, Pang YP, Elpeleg O, Isaya G. Cryptic proteolytic activity of dihydrolipoamide dehydrogenase.. Proc. Natl. Acad. Sci. U.S.A. 2007, 104 (15): 6158–63. doi:10.1073/pnas.0610618104. PMID 17404228.
- Wang YC, Wang ST, Li C, et al.. The role of N286 and D320 in the reaction mechanism of human dihydrolipoamide dehydrogenase (E3) center domain.. J. Biomed. Sci. 2007, 14 (2): 203–10. doi:10.1007/s11373-006-9136-0. PMID 17171578.
- Foster LJ, Rudich A, Talior I, et al.. Insulin-dependent interactions of proteins with GLUT4 revealed through stable isotope labeling by amino acids in cell culture (SILAC).. J. Proteome Res. 2006, 5 (1): 64–75. doi:10.1021/pr0502626. PMID 16396496.
- Kim H. Asparagine-473 residue is important to the efficient function of human dihydrolipoamide dehydrogenase.. J. Biochem. Mol. Biol. 2005, 38 (2): 248–52. PMID 15826505.
- Hiromasa Y, Fujisawa T, Aso Y, Roche TE. Organization of the cores of the mammalian pyruvate dehydrogenase complex formed by E2 and E2 plus the E3-binding protein and their capacities to bind the E1 and E3 components.. J. Biol. Chem. 2004, 279 (8): 6921–33. doi:10.1074/jbc.M308172200. PMID 14638692.
- Wynn RM, Kato M, Machius M, et al.. Molecular mechanism for regulation of the human mitochondrial branched-chain alpha-ketoacid dehydrogenase complex by phosphorylation.. Structure. 2004, 12 (12): 2185–96. doi:10.1016/j.str.2004.09.013. PMID 15576032.
- Martins-de-Souza D, Gattaz WF, Schmitt A, et al.. Proteome analysis of schizophrenia patients Wernicke's area reveals an energy metabolism dysregulation.. BMC Psychiatry. 2009, 9: 17. doi:10.1186/1471-244X-9-17. PMC 2684104. PMID 19405953.
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二氢硫辛酰胺脱氢酶引用了美国国家医学图书馆提供的資料,这些資料属于公共领域。