二氢硫辛酰胺脱氢酶

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PDB渲染的1zy8 有效结构 PDB 直系同源检索：PDBe, RCSB PDB查询代码列表

1ZMC, 1ZMD, 1ZY8, 2F5Z

标识代号 DLD; DLDH; E3; GCSL; LAD; PHE3 扩展标识遗传学：238331 鼠基因：107450 同源基因：84 GeneCards: DLD Gene EC编号 1.8.1.4 基因本体论描述分子功能 · dihydrolipoyl dehydrogenase activity

· electron carrier activity · oxidoreductase activity · lipoamide binding · flavin adenine dinucleotide binding

· NAD binding 细胞成分 · cytoplasm

· mitochondrion · mitochondrial matrix · flagellum · acrosomal matrix · oxoglutarate dehydrogenase complex

· pyruvate dehydrogenase complex 生物过程 · pyruvate metabolic process

· tricarboxylic acid cycle · 2-oxoglutarate metabolic process · mitochondrial electron transport, NADH to ubiquinone · proteolysis · lysine catabolic process · gastrulation · aging · branched chain family amino acid catabolic process · lipoate metabolic process · regulation of acetyl-CoA biosynthetic process from pyruvate · cellular nitrogen compound metabolic process · regulation of membrane potential · cell redox homeostasis · sperm capacitation

· dihydrolipoamide metabolic process Sources: Amigo / QuickGO 直系同源体物种人类鼠类 Entrez 1738 13382 Ensembl ENSG00000091140 ENSMUSG00000020664 UniProt P09622 O08749 mRNA序列 NM_000108 NM_007861.4 蛋白序列 NP_000099 NP_031887.2 基因位置 Chr 7: 107.53 – 107.57 Mb Chr 12: 32.02 – 32.04 Mb PubMed查询 [1] [2] This box: view talk edit 二氢硫辛酰胺脱氢酶命名系统命名缩写识别码 EC编号 1.8.1.4 CAS号 9001-18-7 数据库 IntEnz IntEnz浏览 BRENDA BRENDA入口 ExPASy NiceZyme浏览 KEGG KEGG入口 MetaCyc 代谢路径 PRIAM 概述 PDB RCSB PDB PDBe PDBsum 基因本体 AmiGO / EGO 搜索 PMC 相关文献 PubMed 相关文献

二氢硫辛酰胺脱氢酶（EC 1.8.1.4，英语：Dihydrolipoamide dehydrogenase，缩写DLD，又称为线粒体二氢硫辛酸脱氢酶，dihydrolipoyl dehydrogenase, mitochondrial）是一种由人类基因DLD[1][2][3][4]所编码的黄素蛋白，其作用是将二氢硫辛酰胺脱氢从而转化为氧化型硫辛酰胺。

DLD作为一种线粒体蛋白质，在真核生物的能量代谢中起到重要作用，它至少参与了五种多酶复合体，且为复合体完成反应所必需的组份[5]。另外，DLD作为一种黄素蛋白氧化还原酶，以FAD为辅基接受质子与电子催化二硫键的形成。

DLD是大小为51千道尔顿亚基的同二聚体，其中每个亚基都与一分子的FAD以共价键的形式相连[6]。

硫辛酰胺

二氢硫辛酰胺

目录 1 功能 2 参考文献 3 深入阅读 4 外部链接 5 参考来源功能

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。

参考文献 ↑ Entrez Gene: dihydrolipoamide dehydrogenase. ↑ Otulakowski G, Robinson BH. Isolation and sequence determination of cDNA clones for porcine and human lipoamide dehydrogenase. Homology to other disulfide oxidoreductases. J. Biol. Chem.. December 1987, 262 (36): 17313–8. PMID 3693355. ↑ Pons G, Raefsky-Estrin C, Carothers DJ, Pepin RA, Javed AA, Jesse BW, Ganapathi MK, Samols D, Patel MS. [http//www.ncbi.nlm.nih.gov/pmc/articles/PMC279783/ Cloning and cDNA sequence of the dihydrolipoamide dehydrogenase component human alpha-ketoacid dehydrogenase complexes]. Proc. Natl. Acad. Sci. U.S.A.. March 1988, 85 (5): 1422–6. doi:10.1073/pnas.85.5.1422. PMID 3278312. PMC 279783. ↑ Scherer SW, Otulakowski G, Robinson BH, Tsui LC. Localization of the human dihydrolipoamide dehydrogenase gene (DLD) to 7q31----q32. Cytogenet. Cell Genet.. 1991, 56 (3-4): 176–7. doi:10.1159/000133081. PMID 2055113. ↑ Babady NE, Pang YP, Elpeleg O, Isaya G. [http//www.ncbi.nlm.nih.gov/pmc/articles/PMC1851069/ Cryptic proteolytic activity of dihydrolipoamide dehydrogenase]. Proceedings of the National Academy of Sciences of the United States of America. 2007, 104 (15): 6158–63. doi:10.1073/pnas.0610618104. PMID 17404228. PMC 1851069. ↑ Ciszak EM, Makal A, Hong YS, Vettaikkorumakankauv AK, Korotchkina LG, Patel MS. How dihydrolipoamide dehydrogenase-binding protein binds dihydrolipoamide dehydrogenase in the human pyruvate dehydrogenase complex. The Journal of Biological Chemistry. 2006, 281 (1): 648–55. doi:10.1074/jbc.M507850200. PMID 16263718. 深入阅读 Silverberg MS, Cho JH, Rioux JD, et al.. [http//www.ncbi.nlm.nih.gov/pmc/articles/PMC2652837/ 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. PMID 19122664. PMC 2652837. Scherer SW, Cheung J, MacDonald JR, et al.. [http//www.ncbi.nlm.nih.gov/pmc/articles/PMC2882961/ Human chromosome 7: DNA sequence and biology.]. Science. 2003, 300 (5620): 767–72. doi:10.1126/science.1083423. PMID 12690205. PMC 2882961. 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. OdiÃ¨vre 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.. [http//www.ncbi.nlm.nih.gov/pmc/articles/PMC2684104/ 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. PMID 19405953. PMC 2684104. 外部链接 MeSH（医学主题词）上面的Dihydrolipoamide+dehydrogenase

二氢硫辛酰胺脱氢酶引用了美国国家医学图书馆提供的资料，这些资料属于公共领域。

蛋白质数据库图集模板:PDB Gallery/1738 以硫为供体的氧化还原酶类（EC 1.8） 1.8.1：以NAD或NADP为受体二氢硫辛酰胺脱氢酶 · 谷胱甘肽还原酶 · 硫氧还蛋白还原酶 1.8.2：以细胞色素为受体亚硫酸盐脱氢酶 · 硫代硫酸盐脱氢酶 1.8.3：以氧气为受体亚硫酸盐氧化酶 1.8.4：以二硫化物为受体谷胱甘肽高胱氨酸转氢酶 1.8.5：以醌类化合物为受体谷胱甘肽脱氢酶 (抗坏血酸盐) 1.8.98：以其他已知物质为受体辅酶B-辅酶M异二硫化物还原酶 1.8.99：以其他物质为受体亚硫酸盐还原酶

EC 1.1/2/3/4/5/6/7/8/9/10/11/12/13/14/15/16/17/18/19/20/21/22 · 2.1/2/3/4/5/6/7(2.7.10/11-12)/8/9 · 3.1/2/3/4(3.4.21/22/23/24)/5/6/7/8/9/10/11/12/13 ·

4.1/2/3/4/5/6 · 5.1/2/3/4/5 · 6.1/2/3/4/5/6 醛/酮氧化还原酶（EC 1.2） 1.2.1：以NAD或NADP为受体醛脱氢酶：乙醛脱氢酶（ALDH2） · 长链醛脱氢酶甘油醛-3-磷酸脱氢酶 1.2.2：以细胞色素为受体甲酸脱氢酶 (细胞色素) 1.2.3：以氧气为受体醛氧化酶 1.2.4：以二硫化物为受体酮戊二酸脱氢酶 · 丙酮酸脱氢酶 · 支链α-酮酸脱氢酶复合物（BCKDHA、BCKDHB、DBT、DLD） 1.2.7：以铁硫蛋白为受体丙酮酸合酶 1.2.99：其它一氧化碳脱氢酶

EC 1.1/2/3/4/5/6/7/8/9/10/11/12/13/14/15/16/17/18/19/20/21/22 · 2.1/2/3/4/5/6/7(2.7.10/11-12)/8/9 · 3.1/2/3/4(3.4.21/22/23/24)/5/6/7/8/9/10/11/12/13 ·

4.1/2/3/4/5/6 · 5.1/2/3/4/5 · 6.1/2/3/4/5/6 蛋白质：黄素蛋白乙酰乳酸合酶 · 酰基辅酶A脱氢酶 · 凋亡诱导因子 · 丁酰辅酶A脱氢酶 · 隐花色素 · 细胞色素b5还原酶 · 二氢硫辛酰胺脱氢酶 · 黄素氧还蛋白 · 高铁血红蛋白还原酶 · 亚甲基四氢叶酸还原酶 · NADH脱氢酶 · NADPH氧化酶 · 硝酸盐还原酶 · 肌氨酸氧化酶 · 硫氧还蛋白还原酶酶：多酶复合体光合作用光合反应中心复合蛋白 · 光合体系脱氢酶丙酮酸脱氢酶复合体（E1、E2、E3） · α-酮戊二酸脱氢酶复合体（OGDH、DLST、DLD） · 支链α-酮酸脱氢酶复合体（BCKDHA、BCKDHB、DBT、DLD）其他 CAD（氨甲酰磷酸合成酶II、天冬氨酸转氨甲酰酶、二氢乳清酸酶） · 胆固醇侧链裂解酶 · 细胞色素b6f复合体 · 电子传递链 · 脂肪酸合酶复合体 · 甘氨酸脱羧酶复合体 · 线粒体三功能蛋白（HADHA、HADHB） · 磷酸烯醇式丙酮酸糖磷酸转移酶系统 · 聚酮合成酶 · 蔗糖酶-异麦芽糖酶复合体 · 色氨酸合成酶阅论改糖酵解代谢途径葡萄糖己糖激酶葡萄糖-6-磷酸葡萄糖-6-磷酸异构酶果糖-6-磷酸磷酸果糖激酶1 果糖-1,6-双磷酸果糖二磷酸醛缩酶

ATP ADP

二羟丙酮磷酸甘油醛-3-磷酸磷酸丙糖异构酶甘油醛-3-磷酸甘油醛-3-磷酸脱氢酶 1,3-双磷酸甘油酸

NAD+ + Pi NADH + H+

2 磷酸甘油酸激酶 3-磷酸甘油酸磷酸甘油酸变位酶 2-磷酸甘油酸磷酸烯醇式丙酮酸水合酶（烯醇化酶）磷酸烯醇式丙酮酸丙酮酸激酶丙酮酸 ADP ATP

H2O

ADP ATP

2 参考来源维基百科-二氢硫辛酰胺脱氢酶出自A+医学百科 “二氢硫辛酰胺脱氢酶”条目 http://www.a-hospital.com/w/%E4%BA%8C%E6%B0%A2%E7%A1%AB%E8%BE%9B%E9%85%B0%E8%83%BA%E8%84%B1%E6%B0%A2%E9%85%B6 转载请保留此链接 关于“二氢硫辛酰胺脱氢酶”的留言：

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