Recombinant Mouse Dihydrolipoyllysine-residue acetyltransferase component of pyruvate dehydrogenase complex, mitochondrial (Dlat)

Function

The pyruvate dehydrogenase (PDH) complex, catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links cytoplasmic glycolysis and the mitochondrial tricarboxylic acid (TCA) cycle. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and dihydrolipoamide dehydrogenase (E3);. Within this complex, the catalytic function of this enzyme is to accept, and to transfer to coenzyme A, acetyl groups from acetyl-lipoyl moiety generated by the pyruvate dehydrogenase, leading to acetyl-CoA formation

Subcellular Location

Mitochondrion matrix

Subunit

Part of the pyruvate dehydrogenase (PDH) complex that is a multi-enzyme complex composed of multiple copies of three enzymes, pyruvate dehydrogenase (subunits PDH1A and PDHB, E1 component), dihydrolipoamide acetyltransferase (DLAT, E2 component), and dihydrolipoamide dehydrogenase (DLD, E3 component) to which is added an additional protein the E3-binding protein (PDHX, E3BP) (By similarity). In terms of structural architecture, the E2 and E3BP components assemble into a 60meric central core with icosahedral symmetry (By similarity). The central core is decorated with E1 and E3 proteins (By similarity). Currently, two alternative models for the E2:E3BP stoichiometry are considered as being either 48:12 (E2(48)-E3BP(12)) or 40:20 (E2(40)-E3BP(20)). Interacts with PDK2 and PDK3. Interacts with SIRT4. Interacts with PDHB (By similarity)

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