Dihydrolipoyl Succinyltransferase (DLST)

DLST; Dihydrolipoamide S-Succinyltransferase; Dihydrolipoyllysine-residue succinyltransferase component of 2-oxoglutarate dehydrogenase complex, mitochondrial

Dihydrolipoyl Succinyltransferase (DLST)
The alpha-keto acid dehydrogenase complexes (pyruvate dehydrogenase complex, alpha-ketoglutarate dehydrogenase complex, and branched chain alpha-keto acid dehydrogenase complex) are a family of multienzyme complexes.
Dihydrolipoamide succinyltransferase, which is a component of the structural core of the alpha-keto glutarate dehydrogenase complex, was studied by Nakano et al. (1993), who isolated a cDNA from a human fibroblast cDNA library. Amino acid sequence analysis supported their previous observation (Nakano et al., 1993) that human dihydrolipoamide succinyltransferase lacks a sequence motif for an E1 and/or E3 binding site. By Northern blot analysis, Ali et al. (1994) detected ubiquitous expression of DLST in peripheral tissues and brain.

Organism species: Homo sapiens (Human)

Organism species: Mus musculus (Mouse)

Organism species: Rattus norvegicus (Rat)