LMPD Database

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LMP007129

UniProt Annotations

Entry Information
Gene Namedihydrolipoyl dehydrogenase
Protein EntryDLDH_YEAST
UniProt IDP09624
SpeciesYeast (S288c)
Comments
Comment typeDescription
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};
FunctionLipoamide dehydrogenase is a component of the alpha- ketoacid dehydrogenase complexes. This includes the pyruvate dehydrogenase complex, which catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). Acts also as component of the glycine cleavage system (glycine decarboxylase complex), which catalyzes the degradation of glycine.
MiscellaneousPresent with 24600 molecules/cell in log phase SD medium. {ECO:0000269|PubMed:14562106}.
MiscellaneousThe active site is a redox-active disulfide bond.
SimilarityBelongs to the class-I pyridine nucleotide-disulfide oxidoreductase family. {ECO:0000305}.
Subcellular LocationMitochondrion matrix.
SubunitLPD1 is a homodimer. Eukaryotic pyruvate dehydrogenase (PDH) complexes are organized as a core consisting of the oligomeric dihydrolipoamide acetyl-transferase (E2), around which are arranged multiple copies of pyruvate dehydrogenase (E1), dihydrolipoamide dehydrogenase (E3) and protein X (E3BP) bound by non-covalent bonds. LPD1 is a component of the glycine decarboxylase complex (GDC), which is composed of four proteins: P, T, L and H. {ECO:0000269|PubMed:7498764, ECO:0000269|PubMed:9538259, ECO:0000269|Ref.9}.