MGP Database

New search | Record Overview | Ontology/Pathway Information | Domain Information | UniProt Annotations | Related Proteins
MGP000838

UniProt Annotations

Entry Information
Gene Namedihydrolipoamide dehydrogenase
Protein EntryDLDH_HUMAN
UniProt IDP09622
SpeciesHuman
Comments
Comment typeDescription
Alternative ProductsEvent=Alternative splicing; Named isoforms=3; Name=1; IsoId=P09622-1; Sequence=Displayed; Name=2; IsoId=P09622-2; Sequence=VSP_055855; Note=No experimental confirmation available.; Name=3; IsoId=P09622-3; Sequence=VSP_055856; Note=No experimental confirmation available.;
Catalytic ActivityProtein N(6)-(dihydrolipoyl)lysine + NAD(+) = protein N(6)-(lipoyl)lysine + NADH.
CofactorName=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250}; Note=Binds 1 FAD per subunit. {ECO:0000250};
DiseaseDihydrolipoamide dehydrogenase deficiency (DLDD) [MIM:246900]: An autosomal recessive metabolic disorder characterized biochemically by a combined deficiency of the branched-chain alpha-keto acid dehydrogenase complex (BCKDC), pyruvate dehydrogenase complex (PDC), and alpha-ketoglutarate dehydrogenase complex (KGDC). Clinically, affected individuals have lactic acidosis and neurologic deterioration due to sensitivity of the central nervous system to defects in oxidative metabolism. {ECO:0000269|PubMed:8506365, ECO:0000269|PubMed:8968745, ECO:0000269|PubMed:9934985}. Note=The disease is caused by mutations affecting the gene represented in this entry.
FunctionLipoamide dehydrogenase is a component of the glycine cleavage system as well as of the alpha-ketoacid dehydrogenase complexes. Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction.
MiscellaneousThe active site is a redox-active disulfide bond.
PtmTyrosine phosphorylated. {ECO:0000250}.
Sequence CautionSequence=BAD92940.1; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
SimilarityBelongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. {ECO:0000305}.
Subcellular LocationMitochondrion matrix.
SubunitHomodimer. Eukaryotic pyruvate dehydrogenase complexes are organized about a core consisting of the oligomeric dihydrolipoamide acetyl-transferase, around which are arranged multiple copies of pyruvate dehydrogenase, dihydrolipoamide dehydrogenase and protein X bound by non-covalent bonds. {ECO:0000269|PubMed:15946682, ECO:0000269|PubMed:16442803}.
  logo