Dihydrolipoamide dehydrogenase

Last updated
DLD
PDB 1zy8 EBI.png
Available structures
PDB Ortholog search: PDBe RCSB
Identifiers
Aliases DLD , DLDD, DLDH, E3, GCSL, LAD, PHE3, dihydrolipoamide dehydrogenase, Dihydrolipoamide dehydrogenase, OGDC-E3
External IDs OMIM: 238331; MGI: 107450; HomoloGene: 84; GeneCards: DLD; OMA:DLD - orthologs
Orthologs
SpeciesHumanMouse
Entrez
Ensembl
UniProt
RefSeq (mRNA)

NM_001289752
NM_000108
NM_001289750
NM_001289751

NM_007861

RefSeq (protein)

NP_000099
NP_001276679
NP_001276680
NP_001276681

NP_031887

Location (UCSC) Chr 7: 107.89 – 107.93 Mb Chr 12: 31.38 – 31.4 Mb
PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Dihydrolipoamide dehydrogenase (DLD), also known as dihydrolipoyl dehydrogenase, mitochondrial, is an enzyme that in humans is encoded by the DLD gene. [5] [6] [7] [8] DLD is a flavoprotein enzyme that oxidizes dihydrolipoamide to lipoamide.

Contents

Dihydrolipoamide dehydrogenase (DLD) is a mitochondrial enzyme that plays a vital role in energy metabolism in eukaryotes. This enzyme is required for the complete reaction of at least five different multi-enzyme complexes. [9] Additionally, DLD is a flavoenzyme oxidoreductase that contains a reactive disulfide bridge and a FAD cofactor that are directly involved in catalysis. The enzyme associates into tightly bound homodimers required for its enzymatic activity. [10]

Structure

The protein encoded by the DLD gene comes together with another protein to form a dimer in the central metabolic pathway. Several amino acids within the catalytic pocket have been identified as important to DLD function, including R281 and N473. [11] [12] Although the overall fold of the human enzyme is similar to that of yeast, the human structure is different in that it has two loops that extend from the general protein structure and into the FAD binding sites when bound the NAD+ molecule, required for catalysis, is not close to the FAD moiety. However, when NADH is bound instead, it is stacked directly op top of the FAD central structure. The current hE3 structures show directly that the disease-causing mutations occur at three locations in the human enzyme: the dimer interface, the active site, and the FAD and NAD(+)-binding sites. [13]

Function

The DLD homodimer functions as the E3 component of the pyruvate, α-ketoglutarate, α-adipate and branched-chain amino acid-dehydrogenase complexes and the glycine cleavage system, all in the mitochondrial matrix. In these complexes, DLD converts dihydrolipoic acid and NAD+ into lipoic acid and NADH. [14] DLD also has diaphorase activity, being able to catalyze the oxidation of NADH to NAD+ by using different electron acceptors such as O2, labile ferric iron, nitric oxide, and ubiquinone. [9] DLD is thought to have a pro-oxidant role by reducing oxygen to a superoxide or ferric to ferrous iron, which then catalyzes production of hydroxyl radicals. [15] [16] Diaphorase activity of DLD may have an antioxidant role through its ability to scavenge nitric oxide and to reduce ubiquinone to ubiquinol. [17] [18] [19] The dihyrolipamide dehydrogenase gene is known to have multiple splice variants.

Moonlighting function

Certain DLD mutations can simultaneously induce the loss of a primary metabolic activity and the gain of a moonlighting proteolytic activity. The moonlighting proteolytic activity of DLD is revealed by conditions that destabilize the DLD homodimer and decrease its DLD activity. [9] Acidification of the mitochondrial matrix, as a result of ischemia-reperfusion injury, can disrupt the quaternary structure of DLD leading to decreased dehydrogenase activity and increased diaphorase activity. [20] The moonlighting proteolytic activity of DLD could also arise under pathological conditions. Proteolytic activity can further complicate the reduction in energy metabolism and an increase in oxidative damage as a result of decreased DLD activity and an increase in diaphorase activity respectively. [19] With its proteolytic function, DLD removes a functionally vital domain from the N-terminus of frataxin, a mitochondrial protein involved in iron metabolism and antioxidant protection. [21] [22]

Clinical significance

In humans, mutations in DLD are linked to a severe disorder of infancy with failure to thrive, hypotonia, and metabolic acidosis. [23] DLD deficiency manifests itself in a great degree of variability, which has been attributed to varying effects of different DLD mutations on the stability of the protein and its ability to dimerize or interact with other components of the three α-ketoacid dehydrogenase complexes. [23] With its proteolytic function, DLD causes a deficiency in frataxin, which leads to the neurodegenerative and cardiac disease, Friedreich's ataxia. [24]

Interactive pathway map

Click on genes, proteins and metabolites below to link to respective articles. [§ 1]
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TCACycle WP78.png Go to articleGo to articleGo to articleGo to articleGo to HMDBGo to articleGo to articleGo to articleGo to HMDBGo to HMDBGo to articleGo to WikiPathwaysGo to articleGo to articleGo to articleGo to WikiPathwaysGo to articleGo to articleGo to articleGo to articleGo to articleGo to articleGo to articleGo to articleGo to articleGo to articleGo to articleGo to articleGo to articleGo to articleGo to articleGo to articleGo to articleGo to articleGo to articleGo to WikiPathwaysGo to articleGo to articleGo to articleGo to HMDBGo to articleGo to articleGo to articleGo to articleGo to articleGo to WikiPathwaysGo to articleGo to WikiPathwaysGo to HMDBGo to articleGo to WikiPathwaysGo to articleGo to HMDBGo to articleGo to articleGo to articleGo to articleGo to articleGo to articleGo to articleGo to articleGo to articleGo to article
|alt=TCACycle_WP78 edit]]
TCACycle_WP78 edit
  1. The interactive pathway map can be edited at WikiPathways: "TCACycle_WP78".
Click on genes, proteins and metabolites below to link to respective articles. [§ 1]
[[File:
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WP534.png go to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to articlego to WikiPathwaysgo to articlego to Entrezgo to article
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Glycolysis and Gluconeogenesis edit
  1. The interactive pathway map can be edited at WikiPathways: "GlycolysisGluconeogenesis_WP534".

Enzyme regulation

This protein may use the morpheein model of allosteric regulation. [25]

See also

Related Research Articles

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References

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  2. 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000020664 Ensembl, May 2017
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  4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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  9. 1 2 3 Babady NE, Pang YP, Elpeleg O, Isaya G (April 2007). "Cryptic proteolytic activity of dihydrolipoamide dehydrogenase". Proceedings of the National Academy of Sciences of the United States of America. 104 (15): 6158–63. Bibcode:2007PNAS..104.6158B. doi: 10.1073/pnas.0610618104 . PMC   1851069 . PMID   17404228.
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  15. Petrat F, Paluch S, Dogruöz E, Dörfler P, Kirsch M, Korth HG, et al. (November 2003). "Reduction of Fe(III) ions complexed to physiological ligands by lipoyl dehydrogenase and other flavoenzymes in vitro: implications for an enzymatic reduction of Fe(III) ions of the labile iron pool". The Journal of Biological Chemistry. 278 (47): 46403–13. doi: 10.1074/jbc.M305291200 . PMID   12963736.
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  18. Olsson JM, Xia L, Eriksson LC, Björnstedt M (April 1999). "Ubiquinone is reduced by lipoamide dehydrogenase and this reaction is potently stimulated by zinc". FEBS Letters. 448 (1): 190–2. Bibcode:1999FEBSL.448..190O. doi: 10.1016/s0014-5793(99)00363-4 . PMID   10217438. S2CID   34370150.
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Further reading

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