ジヒドロリ・アミドデヒドロゲナーゼ、ジヒドロリ・アミド脱水素酵素
- 関
- diaphorase
Wikipedia preview
出典(authority):フリー百科事典『ウィキペディア(Wikipedia)』「2013/08/29 06:11:03」(JST)
[Wiki en表示]
Dihydrolipoamide dehydrogenase |
PDB rendering based on 1zy8. |
Available structures |
PDB |
Ortholog search: PDBe, RCSB |
List of PDB id codes |
1ZMC, 1ZMD, 1ZY8, 2F5Z, 3RNM
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Identifiers |
Symbols |
DLD; DLDD; DLDH; E3; GCSL; LAD; PHE3 |
External IDs |
OMIM: 238331 MGI: 107450 HomoloGene: 84 GeneCards: DLD Gene |
EC number |
1.8.1.4 |
Gene Ontology |
Molecular function |
• dihydrolipoyl dehydrogenase activity
• flavin adenine dinucleotide binding
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Cellular component |
• nucleus
• nucleolus
• mitochondrion
• mitochondrial matrix
• acrosomal matrix
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Biological process |
• pyruvate metabolic process
• tricarboxylic acid cycle
• mitochondrial electron transport, NADH to ubiquinone
• proteolysis
• lysine catabolic process
• gastrulation
• branched-chain amino acid catabolic process
• regulation of acetyl-CoA biosynthetic process from pyruvate
• cellular nitrogen compound metabolic process
• regulation of membrane potential
• small molecule metabolic process
• cell redox homeostasis
• sperm capacitation
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Sources: Amigo / QuickGO |
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Orthologs |
Species |
Human |
Mouse |
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Entrez |
1738 |
13382 |
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Ensembl |
ENSG00000091140 |
ENSMUSG00000020664 |
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UniProt |
P09622 |
O08749 |
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RefSeq (mRNA) |
NM_000108 |
NM_007861 |
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RefSeq (protein) |
NP_000099 |
NP_031887 |
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Location (UCSC) |
Chr 7:
107.53 – 107.57 Mb |
Chr 12:
31.33 – 31.35 Mb |
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PubMed search |
[1] |
[2] |
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dihydrolipoyl dehydrogenase |
Identifiers |
EC number |
1.8.1.4 |
CAS number |
9001-18-7 |
Databases |
IntEnz |
IntEnz view |
BRENDA |
BRENDA entry |
ExPASy |
NiceZyme view |
KEGG |
KEGG entry |
MetaCyc |
metabolic pathway |
PRIAM |
profile |
PDB structures |
RCSB PDB PDBe PDBsum |
Gene Ontology |
AmiGO / EGO |
Search |
PMC |
articles |
PubMed |
articles |
NCBI |
proteins |
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Dihydrolipoamide dehydrogenase (DLD), also known as dihydrolipoyl dehydrogenase, mitochondrial, is an enzyme that in humans is encoded by the DLD gene.[1][2][3][4] DLD is a flavoprotein enzyme that oxidizes dihydrolipoamide to lipoamide.
Contents
- 1 Function
- 2 Clinical significance
- 3 Interactive pathway map
- 4 Enzyme regulation
- 5 See also
- 6 References
- 7 Further reading
- 8 External links
Function[edit source | edit]
This gene encodes the L protein of the mitochondrial glycine cleavage system. The L protein, also named dihydrolipoamide dehydrogenase, is also a component of the pyruvate dehydrogenase complex, the alpha-ketoglutarate dehydrogenase complex, and the branched-chain alpha-keto acide dehydrogenase complex.[1]
Clinical significance[edit source | edit]
Mutations in this gene have been identified in patients with E3-deficient maple syrup urine disease and lipoamide dehydrogenase deficiency.[1]
Interactive pathway map[edit source | edit]
Click on genes, proteins and metabolites below to link to respective articles. [§ 1]
- ^ The interactive pathway map can be edited at WikiPathways: "TCACycle_WP78".
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Click on genes, proteins and metabolites below to link to respective articles. [§ 1]
Glycolysis and Gluconeogenesis edit
- ^ The interactive pathway map can be edited at WikiPathways: "GlycolysisGluconeogenesis_WP534".
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Enzyme regulation[edit source | edit]
This protein may use the morpheein model of allosteric regulation. [5]
See also[edit source | edit]
References[edit source | edit]
- ^ a b c "Entrez Gene: dihydrolipoamide dehydrogenase".
- ^ Otulakowski G, Robinson BH (December 1987). "Isolation and sequence determination of cDNA clones for porcine and human lipoamide dehydrogenase. Homology to other disulfide oxidoreductases". J. Biol. Chem. 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 (March 1988). "Cloning and cDNA sequence of the dihydrolipoamide dehydrogenase component human alpha-ketoacid dehydrogenase complexes". Proc. Natl. Acad. Sci. U.S.A. 85 (5): 1422–6. doi:10.1073/pnas.85.5.1422. PMC 279783. PMID 3278312.
- ^ Scherer SW, Otulakowski G, Robinson BH, Tsui LC (1991). "Localization of the human dihydrolipoamide dehydrogenase gene (DLD) to 7q31----q32". Cytogenet. Cell Genet. 56 (3-4): 176–7. doi:10.1159/000133081. PMID 2055113.
- ^ T. Selwood and E. K. Jaffe. (2011). "Dynamic dissociating homo-oligomers and the control of protein function.". Arch. Biochem. Biophys. 519 (2): 131–43. doi:10.1016/j.abb.2011.11.020. PMC 3298769. PMID 22182754.
Further reading[edit source | edit]
- Silverberg MS, Cho JH, Rioux JD, et al. (2009). "Ulcerative colitis-risk loci on chromosomes 1p36 and 12q15 found by genome-wide association study.". Nat. Genet. 41 (2): 216–20. doi:10.1038/ng.275. PMC 2652837. PMID 19122664.
- Scherer SW, Cheung J, MacDonald JR, et al. (2003). "Human chromosome 7: DNA sequence and biology.". Science 300 (5620): 767–72. doi:10.1126/science.1083423. PMC 2882961. PMID 12690205.
- Brautigam CA, Chuang JL, Tomchick DR, et al. (2005). "Crystal structure of human dihydrolipoamide dehydrogenase: NAD+/NADH binding and the structural basis of disease-causing mutations.". J. Mol. Biol. 350 (3): 543–52. doi:10.1016/j.jmb.2005.05.014. PMID 15946682.
- , Barrett JC, Lee JC, et al. (2009). "Genome-wide association study of ulcerative colitis identifies three new susceptibility loci, including the HNF4A region.". Nat. Genet. 41 (12): 1330–4. doi:10.1038/ng.483. PMID 19915572.
- Reed LJ, Hackert ML (1990). "Structure-function relationships in dihydrolipoamide acyltransferases.". J. Biol. Chem. 265 (16): 8971–4. PMID 2188967.
- Ciszak EM, Makal A, Hong YS, et al. (2006). "How dihydrolipoamide dehydrogenase-binding protein binds dihydrolipoamide dehydrogenase in the human pyruvate dehydrogenase complex.". J. Biol. Chem. 281 (1): 648–55. doi:10.1074/jbc.M507850200. PMID 16263718.
- Asano K, Matsushita T, Umeno J, et al. (2009). "A genome-wide association study identifies three new susceptibility loci for ulcerative colitis in the Japanese population.". Nat. Genet. 41 (12): 1325–9. doi:10.1038/ng.482. PMID 19915573.
- Odièvre MH, Chretien D, Munnich A, et al. (2005). "A novel mutation in the dihydrolipoamide dehydrogenase E3 subunit gene (DLD) resulting in an atypical form of alpha-ketoglutarate dehydrogenase deficiency.". Hum. Mutat. 25 (3): 323–4. doi:10.1002/humu.9319. PMID 15712224.
- Brautigam CA, Wynn RM, Chuang JL, et al. (2006). "Structural insight into interactions between dihydrolipoamide dehydrogenase (E3) and E3 binding protein of human pyruvate dehydrogenase complex.". Structure 14 (3): 611–21. doi:10.1016/j.str.2006.01.001. PMID 16442803.
- Kim H (2006). "Activity of human dihydrolipoamide dehydrogenase is largely reduced by mutation at isoleucine-51 to alanine.". J. Biochem. Mol. Biol. 39 (2): 223–7. PMID 16584639.
- Sugden MC, Holness MJ (2003). "Recent advances in mechanisms regulating glucose oxidation at the level of the pyruvate dehydrogenase complex by PDKs.". Am. J. Physiol. Endocrinol. Metab. 284 (5): E855–62. doi:10.1152/ajpendo.00526.2002. PMID 12676647.
- Wang YC, Wang ST, Li C, et al. (2008). "The role of amino acids T148 and R281 in human dihydrolipoamide dehydrogenase.". J. Biomed. Sci. 15 (1): 37–46. doi:10.1007/s11373-007-9208-9. PMID 17960497.
- Brown AM, Gordon D, Lee H, et al. (2004). "Association of the dihydrolipoamide dehydrogenase gene with Alzheimer's disease in an Ashkenazi Jewish population.". Am. J. Med. Genet. B Neuropsychiatr. Genet. 131B (1): 60–6. doi:10.1002/ajmg.b.30008. PMID 15389771.
- Babady NE, Pang YP, Elpeleg O, Isaya G (2007). "Cryptic proteolytic activity of dihydrolipoamide dehydrogenase.". Proc. Natl. Acad. Sci. U.S.A. 104 (15): 6158–63. doi:10.1073/pnas.0610618104. PMC 1851069. PMID 17404228.
- Wang YC, Wang ST, Li C, et al. (2007). "The role of N286 and D320 in the reaction mechanism of human dihydrolipoamide dehydrogenase (E3) center domain.". J. Biomed. Sci. 14 (2): 203–10. doi:10.1007/s11373-006-9136-0. PMID 17171578.
- Foster LJ, Rudich A, Talior I, et al. (2006). "Insulin-dependent interactions of proteins with GLUT4 revealed through stable isotope labeling by amino acids in cell culture (SILAC).". J. Proteome Res. 5 (1): 64–75. doi:10.1021/pr0502626. PMID 16396496.
- Kim H (2005). "Asparagine-473 residue is important to the efficient function of human dihydrolipoamide dehydrogenase.". J. Biochem. Mol. Biol. 38 (2): 248–52. PMID 15826505.
- Hiromasa Y, Fujisawa T, Aso Y, Roche TE (2004). "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. 279 (8): 6921–33. doi:10.1074/jbc.M308172200. PMID 14638692.
- Wynn RM, Kato M, Machius M, et al. (2004). "Molecular mechanism for regulation of the human mitochondrial branched-chain alpha-ketoacid dehydrogenase complex by phosphorylation.". Structure 12 (12): 2185–96. doi:10.1016/j.str.2004.09.013. PMID 15576032.
- Martins-de-Souza D, Gattaz WF, Schmitt A, et al. (2009). "Proteome analysis of schizophrenia patients Wernicke's area reveals an energy metabolism dysregulation.". BMC Psychiatry 9: 17. doi:10.1186/1471-244X-9-17. PMC 2684104. PMID 19405953.
External links[edit source | edit]
- Dihydrolipoamide dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH)
This article incorporates text from the United States National Library of Medicine, which is in the public domain.
PDB gallery
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1zy8: The crystal structure of dihydrolipoamide dehydrogenase and dihydrolipoamide dehydrogenase-binding protein (didomain) subcomplex of human pyruvate dehydrogenase complex.
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2f5z: Crystal Structure of Human Dihydrolipoamide Dehydrogenase (E3) Complexed to the E3-Binding Domain of Human E3-Binding Protein
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1zmc: Crystal Structure of Human dihydrolipoamide dehydrogenase complexed to NAD+
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1zmd: Crystal Structure of Human dihydrolipoamide dehydrogenase complexed to NADH
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Oxidoreductases: sulfur oxidoreductases (EC 1.8)
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1.8.1: NAD or NADP |
- Dihydrolipoamide dehydrogenase
- Glutathione reductase
- Thioredoxin reductase
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1.8.2: cytochrome |
- Sulfite dehydrogenase
- Thiosulfate dehydrogenase
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1.8.3: oxygen |
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1.8.4: disulfide |
- Glutathione-homocystine transhydrogenase
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1.8.5: quinone |
- Glutathione dehydrogenase (ascorbate)
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1.8.98: Other, known |
- CoB-CoM heterodisulfide reductase
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1.8.99: Other |
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- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
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Aldehyde/oxo oxidoreductases (EC 1.2)
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1.2.1: NAD or NADP |
- Aldehyde dehydrogenase: Acetaldehyde dehydrogenase
- Long-chain-aldehyde dehydrogenase
- Glyceraldehyde 3-phosphate dehydrogenase
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1.2.2: cytochrome |
- Formate dehydrogenase (cytochrome)
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1.2.3: oxygen |
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1.2.4: disulfide |
- Oxoglutarate dehydrogenase
- Pyruvate dehydrogenase
- Branched-chain alpha-keto acid dehydrogenase complex
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1.2.7: iron-sulfur protein |
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- B
- enzm
- 1.1
- 2
- 3
- 4
- 5
- 6
- 7
- 8
- 10
- 11
- 13
- 14
- 15-18
- 2.1
- 3.1
- 4.1
- 5.1
- 6.1-3
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Protein: flavoproteins
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- Acetolactate synthase
- Acyl CoA dehydrogenase
- Apoptosis-inducing factor
- Butyryl CoA dehydrogenase
- Cryptochrome
- Cytochrome b5 reductase
- Dihydrolipoamide dehydrogenase
- Flavodoxin
- Methemoglobin reductase
- Methylenetetrahydrofolate reductase
- NADH dehydrogenase
- NADPH oxidase
- Nitrate reductase
- Sarcosine oxidase
- Thioredoxin reductase
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Enzymes: multienzyme complexes
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Photosynthesis |
Photosynthetic reaction center complex proteins · Photosystem (I, II)
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Dehydrogenase |
Pyruvate dehydrogenase complex (E1, E2, E3) · Oxoglutarate dehydrogenase (OGDH, DLST, DLD) · Branched-chain alpha-keto acid dehydrogenase complex (BCKDHA, BCKDHB, DBT, DLD)
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Other |
CAD (Carbamoyl phosphate synthase II, Aspartate carbamoyltransferase, Dihydroorotase) · Cholesterol side-chain cleavage enzyme · Cytochrome b6f complex · Electron transport chain · Fatty acid synthetase complex · Glycine decarboxylase complex · Mitochondrial trifunctional protein (HADHA, HADHB) · Phosphoenolpyruvate sugar phosphotransferase system · Polyketide synthase · Sucrase-isomaltase complex · Tryptophan synthase
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Glycolysis Metabolic Pathway |
Glucose |
Hexokinase |
Glucose 6-phosphate |
Glucose-6-phosphate isomerase |
Fructose 6-phosphate |
phosphofructokinase-1 |
Fructose 1,6-bisphosphate |
Fructose-bisphosphate aldolase |
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ATP |
ADP |
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ATP |
ADP |
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Dihydroxyacetone phosphate |
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Glyceraldehyde 3-phosphate |
Triosephosphate isomerase |
Glyceraldehyde 3-phosphate |
Glyceraldehyde-3-phosphate dehydrogenase |
1,3-Bisphosphoglycerate |
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NAD+ + Pi |
NADH + H+ |
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+ |
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2 |
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2 |
Phosphoglycerate kinase |
3-Phosphoglycerate |
Phosphoglycerate mutase |
2-Phosphoglycerate |
Phosphopyruvate hydratase(Enolase) |
Phosphoenolpyruvate |
Pyruvate kinase |
Pyruvate |
ADP |
ATP |
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H2O |
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ADP |
ATP |
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2 |
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2 |
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2 |
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2 |
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mt, k, c/g/r/p/y/i, f/h/s/l/o/e, a/u, n, m
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k, cgrp/y/i, f/h/s/l/o/e, au, n, m, epon
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m (A16/C10), i (k, c/g/r/p/y/i, f/h/s/o/e, a/u, n, m)
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UpToDate Contents
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English Journal
- Mutagenesis of conserved active site residues of dihydrolipoamide succinyltransferase enhances the accumulation of α-ketoglutarate in Yarrowia lipolytica.
- Guo H1,2, Madzak C3, Du G1,2, Zhou J4,5.
- Applied microbiology and biotechnology.Appl Microbiol Biotechnol.2015 Oct 1. [Epub ahead of print]
- α-Ketoglutarate (α-KG) is an important intermediate in the tricarboxylic acid cycle and has broad applications. The mitochondrial ketoglutarate dehydrogenase (KGDH) complex catalyzes the oxidation of α-KG to succinyl-CoA. Disruption of KGDH, which may enhance the accumulation of α-KG theoretical
- PMID 26428234
- PROTEOMIC ANALYSIS OF UBIQUITINATED PROTEINS FROM DELTAMETHRIN-RESISTANT AND SUSCEPTIBLE STRAINS OF THE DIAMONDBACK MOTH, Plutella Xylostella L.
- Cheng L1, Du Y1, Hu J1, Jiao D1, Li J1, Zhou Z1, Xu Q2, Li F3.
- Archives of insect biochemistry and physiology.Arch Insect Biochem Physiol.2015 Oct;90(2):70-88. doi: 10.1002/arch.21245. Epub 2015 May 15.
- Ubiquitin, a small protein consisting of 76 amino acids, acts in protein degradation, DNA repair, signal transduction, transcriptional regulation, and receptor control through endocytosis. Using proteomics, we compared the differentially ubiquitinated proteins between a deltamethrin-resistant (DR) s
- PMID 25983007
- Detoxification of hexavalent chromium by Leucobacter sp. uses a reductase with specificity for dihydrolipoamide.
- Sarangi A1, Krishnan C1.
- Journal of basic microbiology.J Basic Microbiol.2015 Sep 17. doi: 10.1002/jobm.201500285. [Epub ahead of print]
- Leucobacter sp. belongs to the metal stressed community and possesses higher tolerance to metals including chromium and can detoxify toxic hexavalent chromium by reduction to less toxic trivalent chromium. But, the mechanism of reduction of hexavalent chromium by Leucobacter sp. has not been studied
- PMID 26377775
Japanese Journal
- 低強度・長時間水泳運動トレーニングによりラット骨格筋で発現するタンパク質のプロテオミクス ; 2D-DIGE解析
- 山口 航,藤本 恵理,樋口 満 [他],田畑 泉
- 体力科學 60(5), 511-518, 2011-10-01
- … All proteins were identified by MALDI-TOF/MS. Conclusion: The proteomic 2D-DIGE analysis following LIT identified expressions of skeletal muscle proteins, includingATPsynα, UQCRC1, dihydrolipoamide dehydrogenase, dihydrolipoamide acetyltransferase, that were not previously reported to change their expressions after exercise-training. …
- NAID 10030027192
- Nongradient blue native gel analysis of serum proteins and in-gel detection of serum esterase activities
- THANGTHAENG Nopporn,SUMIEN Nathalie,FORSTER Michael J.,SHAH Ruchir A.,YAN Liang-Jun
- Journal of chromatography. B, Analytical technologies in the biomedical and life sciences 879(5), 386-394, 2011-02-15
- NAID 10029517013
Related Links
- di·hy·dro·lip·o·am·ide de·hy·dro·gen·ase (dī-hī'drō-lip-ō-am'id dē-hī'drō-jen-ās'), A flavoenzyme oxidizing dihydrolipoamide at the expense of NAD +; completes the oxidative decarboxylation of pyruvate; a part of several enzyme ...
- The official name of this gene is “dihydrolipoamide dehydrogenase.” DLD is the gene's official symbol. The DLD gene is also known by other names, listed below. Read more about gene names and symbols on the About page.
Related Pictures
![The interactive pathway map can be](https://1mg.info/0/7/r/0250.jpg)
![Alpha-ketoglutarate dehydrogenase: a](https://1mg.info/0/7/r/0251.jpg)
![Dihydrolipoamide Dehydrogenase (Lipoamide](https://1mg.info/0/7/r/0252.jpg)
![of dihydrolipoamide dehydrogenase](https://1mg.info/0/7/r/0253.jpg)
![Dihydrolipoamide dehydrogenase](https://1mg.info/0/7/r/0254.jpg)
★リンクテーブル★
[★]
- 英
- dihydrolipoamide dehydrogenase
- 同
- ジヒドロリポアミドデヒドロゲナーゼ、リポアミド還元酵素(NADH) lipoamide reductase(NADH)、ジアホラーゼ diaphorase
[★]
ジアホラーゼ、ジアフォラーゼ
- 関
- dihydrolipoamide dehydrogenase
[★]
- 英
- dihydrolipoamide dehydrogenase
- 関
- ジヒドロリポアミド脱水素酵素
[★]
脱水素酵素 デヒドロゲナーゼ
[★]
脱水素酵素 デヒドロゲナーゼ
[★]
ジヒドロリポアミド