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维基百科

二氢硫辛酰胺脱氢酶

二氢硫辛酰胺脱氢酶EC 1.8.1.4,英語: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

二氢硫辛酰胺脱氢酶
PDB渲染的1zy8
有效结构
PDB 直系同源检索:PDBe, RCSB
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編號 1.8.1.4
直系同源体
物种 人类 小鼠
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]
二氢硫辛酰胺脱氢酶
识别码
EC編號 1.8.1.4
CAS号 9001-18-7
数据库
IntEnz IntEnz浏览
BRENDA英语BRENDA BRENDA入口
ExPASy英语ExPASy NiceZyme浏览
KEGG KEGG入口
MetaCyc英语MetaCyc 代谢路径
PRIAM英语PRIAM_enzyme-specific_profiles 概述
PDB RCSB PDB PDBj PDBe PDBsum
基因本体 AmiGO / EGO

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還原酶,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]

功能

哺乳动物线粒体三羧酸循环中,该酶与丙酮酸脱氢酶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

  1. ^ Entrez Gene: dihydrolipoamide dehydrogenase. (原始内容于2010-03-06). 
  2. ^ 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. 
  3. ^ Pons G, Raefsky-Estrin C, Carothers DJ, Pepin RA, Javed AA, Jesse BW, Ganapathi MK, Samols D, Patel MS. 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. PMC 279783 . PMID 3278312. doi:10.1073/pnas.85.5.1422. 
  4. ^ 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. PMID 2055113. doi:10.1159/000133081. 
  5. ^ Babady NE, Pang YP, Elpeleg O, Isaya G. Cryptic proteolytic activity of dihydrolipoamide dehydrogenase. Proceedings of the National Academy of Sciences of the United States of America. 2007, 104 (15): 6158–63. PMC 1851069 . PMID 17404228. doi:10.1073/pnas.0610618104. 
  6. ^ 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. PMID 16263718. doi:10.1074/jbc.M507850200. 

深入阅读

  • 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. PMC 2652837 . PMID 19122664. doi:10.1038/ng.275. 
  • Scherer SW, Cheung J, MacDonald JR; et al. Human chromosome 7: DNA sequence and biology.. Science. 2003, 300 (5620): 767–72. PMC 2882961 . PMID 12690205. doi:10.1126/science.1083423. 
  • 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. PMID 15946682. doi:10.1016/j.jmb.2005.05.014. 
  • , 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. PMID 19915572. doi:10.1038/ng.483. 
  • 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. PMID 16263718. doi:10.1074/jbc.M507850200. 
  • 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. PMID 19915573. doi:10.1038/ng.482. 
  • 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. PMID 15712224. doi:10.1002/humu.9319. 
  • 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. PMID 16442803. doi:10.1016/j.str.2006.01.001. 
  • 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. PMID 12676647. doi:10.1152/ajpendo.00526.2002. 
  • 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. PMID 17960497. doi:10.1007/s11373-007-9208-9. 
  • 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. PMID 15389771. doi:10.1002/ajmg.b.30008. 
  • 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. PMID 17404228. doi:10.1073/pnas.0610618104. 
  • 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. PMID 17171578. doi:10.1007/s11373-006-9136-0. 
  • 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. PMID 16396496. doi:10.1021/pr0502626. 
  • 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. PMID 14638692. doi:10.1074/jbc.M308172200. 
  • 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. PMID 15576032. doi:10.1016/j.str.2004.09.013. 
  • 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. PMC 2684104 . PMID 19405953. doi:10.1186/1471-244X-9-17. 

外部链接

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


二氢硫辛酰胺脱氢酶, 此條目需要擴充, 2011年9月15日, 请協助改善这篇條目, 更進一步的信息可能會在討論頁或扩充请求中找到, 请在擴充條目後將此模板移除, 英語, 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, 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, pdb渲染的1zy8有效结构pdb, 直系同源. 此條目需要擴充 2011年9月15日 请協助改善这篇條目 更進一步的信息可能會在討論頁或扩充请求中找到 请在擴充條目後將此模板移除 二氢硫辛酰胺脱氢酶 EC 1 8 1 4 英語 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 二氢硫辛酰胺脱氢酶PDB渲染的1zy8有效结构PDB 直系同源检索 PDBe RCSBPDB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 GeneEC編號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 processSources Amigo QuickGO直系同源体物种人类小鼠Entrez173813382EnsemblENSG00000091140ENSMUSG00000020664UniProtP09622O08749mRNA序列NM 000108NM 007861 4蛋白序列NP 000099NP 031887 2基因位置Chr 7 107 53 107 57 MbChr 12 32 02 32 04 MbPubMed查询 1 2 查论编二氢硫辛酰胺脱氢酶命名系统命名缩写识别码EC編號 1 8 1 4CAS号 9001 18 7数据库IntEnz IntEnz浏览BRENDA 英语 BRENDA BRENDA入口ExPASy 英语 ExPASy NiceZyme浏览KEGG KEGG入口MetaCyc 英语 MetaCyc 代谢路径PRIAM 英语 PRIAM enzyme specific profiles 概述PDB RCSB PDB PDBj PDBe PDBsum基因本体 AmiGO EGO搜索PMC 相关文献PubMed 相关文献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還原酶 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 外部链接功能 编辑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a 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 编辑 Entrez Gene dihydrolipoamide dehydrogenase 原始内容存档于2010 03 06 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 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 PMC 279783 PMID 3278312 doi 10 1073 pnas 85 5 1422 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 PMID 2055113 doi 10 1159 000133081 Babady NE Pang YP Elpeleg O Isaya G Cryptic proteolytic activity of dihydrolipoamide dehydrogenase Proceedings of the National Academy of Sciences of the United States of America 2007 104 15 6158 63 PMC 1851069 PMID 17404228 doi 10 1073 pnas 0610618104 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 PMID 16263718 doi 10 1074 jbc M507850200 深入阅读 编辑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 PMC 2652837 PMID 19122664 doi 10 1038 ng 275 引文格式1维护 显式使用等标签 link Scherer SW Cheung J MacDonald JR et al Human chromosome 7 DNA sequence and biology Science 2003 300 5620 767 72 PMC 2882961 PMID 12690205 doi 10 1126 science 1083423 引文格式1维护 显式使用等标签 link 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 PMID 15946682 doi 10 1016 j jmb 2005 05 014 引文格式1维护 显式使用等标签 link 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 PMID 19915572 doi 10 1038 ng 483 引文格式1维护 显式使用等标签 link 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 PMID 16263718 doi 10 1074 jbc M507850200 引文格式1维护 显式使用等标签 link 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 PMID 19915573 doi 10 1038 ng 482 引文格式1维护 显式使用等标签 link OdiA 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 PMID 15712224 doi 10 1002 humu 9319 引文格式1维护 显式使用等标签 link 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 PMID 16442803 doi 10 1016 j str 2006 01 001 引文格式1维护 显式使用等标签 link 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 PMID 12676647 doi 10 1152 ajpendo 00526 2002 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 PMID 17960497 doi 10 1007 s11373 007 9208 9 引文格式1维护 显式使用等标签 link 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 PMID 15389771 doi 10 1002 ajmg b 30008 引文格式1维护 显式使用等标签 link 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 PMID 17404228 doi 10 1073 pnas 0610618104 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 PMID 17171578 doi 10 1007 s11373 006 9136 0 引文格式1维护 显式使用等标签 link 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 PMID 16396496 doi 10 1021 pr0502626 引文格式1维护 显式使用等标签 link 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 PMID 14638692 doi 10 1074 jbc M308172200 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 PMID 15576032 doi 10 1016 j str 2004 09 013 引文格式1维护 显式使用等标签 link 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 PMC 2684104 PMID 19405953 doi 10 1186 1471 244X 9 17 引文格式1维护 显式使用等标签 link 外部链接 编辑醫學主題詞表 MeSH 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資料 这些資料属于公共领域 取自 https zh wikipedia org w index php title 二氢硫辛酰胺脱氢酶 amp oldid 63236660, 维基百科,wiki,书籍,书籍,图书馆,

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