Dihydrolipoamide dehydrogenase

Dihydrolipoamide dehydrogenase
PDB rendering based on 1zy8.
Available structures PDB 1ZMC, 1ZMD, 1ZY8, 2F5Z
Identifiers
Symbols	DLD; 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 • electron carrier activity • oxidoreductase activity • lipoamide binding • flavin adenine dinucleotide binding • NAD binding Cellular component • cytoplasm • mitochondrion • mitochondrial matrix • flagellum • acrosomal matrix • oxoglutarate dehydrogenase complex • pyruvate dehydrogenase complex Biological process • 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
Orthologs
Species	Human	Mouse
Entrez	1738	13382
Ensembl	ENSG00000091140	ENSMUSG00000020664
UniProt	P09622	O08749
RefSeq (mRNA)	NM_000108	NM_007861.4
RefSeq (protein)	NP_000099	NP_031887.2
Location (UCSC)	Chr 7: 107.53 – 107.57 Mb	Chr 12: 32.02 – 32.04 Mb
PubMed search	[1]	[2]

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

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 degrades lipoamide, and produces dihydrolipoamide.

• 

  Lipoamide

• 

  Dihydrolipoamide

Function

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

Mutations in this gene have been identified in patients with E3-deficient maple syrup urine disease and lipoamide dehydrogenase deficiency.^[1]

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles.^[5]

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Citric_acid_cycle edit

See also

• Lipoic acid

References

1. ^ ^{a b c} "Entrez Gene: dihydrolipoamide dehydrogenase". http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1738. 
2. ^ 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. 
3. ^ 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=279783. 
4. ^ 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. PMID 2055113. 
5. ^ The interactive pathway map can be edited at WikiPathways: "TCACycle_WP78". http://www.wikipathways.org/index.php/Pathway:WP78. 

Further reading

• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2652837. 
• 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2882961. 
• 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. 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. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=2684104. 

External links

• MeSH Dihydrolipoamide+dehydrogenase

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

This oxidoreductase article is a stub. You can help Wikipedia by expanding it.v · Categories: Human proteins Glycolysis Moonlighting proteins Oxidoreductase stubs Wikimedia Foundation. 2010. Игры ⚽ Поможем решить контрольную работу Sharon Draper Hemaris diffinis Look at other dictionaries: dihydrolipoamide dehydrogenase — A flavoenzyme oxidizing dihydrolipoamide at the expense of NAD+; completes the oxidative decarboxylation of pyruvate; a part of several enzyme complexes ( e.g., α ketoglutarate dehydrogenase complex). Decreased activity leads to neuronal loss in …   Medical dictionary Dihydrolipoamide — IUPAC name 6,8 dimercaptooctanamide …   Wikipedia dihydrolipoamide — noun A molecule produced by the action of dihydrolipoyl dehydrogenase upon lipoamide …   Wiktionary dihydrolipoamide S-acetyltransferase — An enzyme catalyzing the transfer of an acetyl grout from S6 acetyldihydrolipoamide to coenzyme A. A part of many enzyme complexes ( e.g., pyruvate dehydrogenase complex). SYN: lipoate acetyltransferase, thioltransacetylase A …   Medical dictionary NADH dehydrogenase — Structure of NADH dehydrogenase Identifiers EC number 1.6.5.3 …   Wikipedia lipoamide dehydrogenase — SYN: dihydrolipoamide dehydrogenase. * * * lipo·am·ide de·hy·dro·gen·ase (lip″o amґīd de hiґdro jən″ās) erroneous name for dihydrolipoyl dehydrogenase …   Medical dictionary lipoyl dehydrogenase — SYN: dihydrolipoamide dehydrogenase …   Medical dictionary Pyruvate dehydrogenase — Crystallographic structure of pyruvate dehydrogenase (PDH). PH is a six domain dimer with α (blue), α’ (yellow), β (red), and β’ (teal) regions denoted by the different colors. Thiamine pyrophosphate (TPP) is shown in grey ball and stick form,… …   Wikipedia Dihydrolipoyl-Dehydrogenase — Vorhandene Strukturdaten …   Deutsch Wikipedia lipoamide dehydrogenase — An enzyme that regenerates lipoamide from the reduced form dihydrolipoamide …   Dictionary of molecular biology 18+ © Academic, 2000-2024 Contact us: Technical Support, Advertising Dictionaries export, created on PHP, Joomla, Drupal, WordPress, MODx. Mark and share Search through all dictionaries Translate… Search Internet Share the article and excerpts Direct link … Do a right-click on the link above and select “Copy Link”