oxidoreductase activity, acting on a sulfur group of donors, NAD(P) as acceptor
electron transfer activity
protein binding
Cellular component
oxoglutarate dehydrogenase complex
myelin sheath
pyruvate dehydrogenase complex
cilium
acrosomal matrix
nucleoplasm
mitochondrial matrix
mitochondrion
acrosomal vesicle
cytoplasmic vesicle
motile cilium
cell projection
nucleus
Biological process
mitochondrial acetyl-CoA biosynthetic process from pyruvate
regulation of membrane potential
human ageing
branched-chain amino acid catabolic process
tricarboxylic acid cycle
2-oxoglutarate metabolic process
lysine catabolic process
regulation of acetyl-CoA biosynthetic process from pyruvate
cell redox homeostasis
proteolysis
lipoate metabolic process
dihydrolipoamide metabolic process
gastrulation
pyruvate metabolic process
sperm capacitation
acetyl-CoA biosynthetic process from pyruvate
mitochondrial electron transport, NADH to ubiquinone
cellular nitrogen compound metabolic process
histone succinylation
Sources:Amigo / QuickGO
Orthologs
Species
Human
Mouse
Entrez
1738
13382
Ensembl
ENSG00000091140
ENSMUSG00000020664
UniProt
P09622
O08749
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.
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]
Lipoamide
Dihydrolipoamide
^ abcGRCh38: Ensembl release 89: ENSG00000091140 – Ensembl, May 2017
^ abcGRCm38: Ensembl release 89: ENSMUSG00000020664 – Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"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". The Journal of Biological Chemistry. 262 (36): 17313–8. doi:10.1016/S0021-9258(18)45379-3. PMID 3693355.
^Pons G, Raefsky-Estrin C, Carothers DJ, Pepin RA, Javed AA, Jesse BW, et al. (March 1988). "Cloning and cDNA sequence of the dihydrolipoamide dehydrogenase component human alpha-ketoacid dehydrogenase complexes". Proceedings of the National Academy of Sciences of the United States of America. 85 (5): 1422–6. Bibcode:1988PNAS...85.1422P. 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". Cytogenetics and Cell Genetics. 56 (3–4): 176–7. doi:10.1159/000133081. hdl:10722/42531. PMID 2055113.
^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.
^Ciszak EM, Makal A, Hong YS, Vettaikkorumakankauv AK, Korotchkina LG, Patel MS (January 2006). "How dihydrolipoamide dehydrogenase-binding protein binds dihydrolipoamide dehydrogenase in the human pyruvate dehydrogenase complex". The Journal of Biological Chemistry. 281 (1): 648–55. doi:10.1074/jbc.M507850200. PMID 16263718.
and 21 Related for: Dihydrolipoamide dehydrogenase information
Dihydrolipoamidedehydrogenase (DLD), also known as dihydrolipoyl dehydrogenase, mitochondrial, is an enzyme that in humans is encoded by the DLD gene...
MS (2006). "How dihydrolipoamidedehydrogenase-binding protein binds dihydrolipoamidedehydrogenase in the human pyruvate dehydrogenase complex". Journal...
dehydrogenase system, which includes three different enzymes: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2), dihydrolipoamide dehydrogenase...
Dihydrolipoamide is a molecule oxidized by dihydrolipoyl dehydrogenase in order to produce lipoamide. Lipoamide is subsequently used as a cofactor for...
pyruvate dehydrogenase complex. These complexes have three central subunits: E1-3, which are the decarboxylase, lipoyl transferase, and dihydrolipoamide dehydrogenase...
transacetylase (or dihydrolipoamide acetyltransferase) is an enzyme component of the multienzyme pyruvate dehydrogenase complex. The pyruvate dehydrogenase complex...
(Jan 2006). "How dihydrolipoamidedehydrogenase-binding protein binds dihydrolipoamidedehydrogenase in the human pyruvate dehydrogenase complex". The Journal...
alpha-ketoglutarate dehydrogenase complex. Evidence for direct association of the alpha-ketoglutarate dehydrogenase and dihydrolipoamidedehydrogenase components"...
Pyruvate dehydrogenase is an enzyme that catalyzes the reaction of pyruvate and a lipoamide to give the acetylated dihydrolipoamide and carbon dioxide...
responsible for encoding dihydrolipoamidedehydrogenase, a flavoprotein component known as E3, required by the pyruvate dehydrogenase complex. The LIAS gene...
high level resistance to phosphine have been identified in the dihydrolipoamidedehydrogenase gene. Identification of this gene now allows rapid molecular...
alpha-ketoglutarate dehydrogenase complex. Evidence for direct association of the alpha-ketoglutarate dehydrogenase and dihydrolipoamidedehydrogenase components"...
Distribution), a Linux distribution produced from 1992 to 1999 Dihydrolipoamidedehydrogenase Digital Life Design, a conference network DLD (software), a...
Elpeleg, O.; Isaya, G. (2007). "Cryptic proteolytic activity of dihydrolipoamidedehydrogenase". Proceedings of the National Academy of Sciences. 104 (15):...
glycine encephalopathy.: 790 There is a fourth unit in the GCS: dihydrolipoamidedehydrogenase or GCSL. However, to date there have been no mutations in GCSL...
alpha-ketoglutarate dehydrogenase complex. Evidence for direct association of the alpha-ketoglutarate dehydrogenase and dihydrolipoamidedehydrogenase components"...
Memorial Sloan Kettering Cancer Center Thesis Identification and Characterization of the Proteolytic Activity of DihydrolipoamideDehydrogenase (2007)...
dihydrolipoyl transacylase (E2; MIM 248610), and a homodimeric dihydrolipoamidedehydrogenase (E3; MIM 238331). The reaction is irreversible and constitutes...
disulfide oxidoreductases, especially dihydrolipoamidedehydrogenase (DLDH) (EC 1.8.1.4) of the pyruvate dehydrogenase complex. The amino acid sequence of...