Subunit and catalytic component stoichiometries of an in vitro reconstituted human pyruvate dehydrogenase complex
CA Brautigam, RM Wynn, JL Chuang… - Journal of biological …, 2009 - ASBMB
The human pyruvate dehydrogenase complex (PDC) is a 9.5-megadalton catalytic machine
that employs three catalytic components, ie pyruvate dehydrogenase (E1p), dihydrolipoyl
transacetylase (E2p), and dihydrolipoamide dehydrogenase (E3), to carry out the oxidative
decarboxylation of pyruvate. The human PDC is organized around a 60-meric dodecahedral
core comprising the C-terminal domains of E2p and a noncatalytic component, E3-binding
protein (E3BP), which specifically tethers E3 dimers to the PDC. A central issue concerning …
that employs three catalytic components, ie pyruvate dehydrogenase (E1p), dihydrolipoyl
transacetylase (E2p), and dihydrolipoamide dehydrogenase (E3), to carry out the oxidative
decarboxylation of pyruvate. The human PDC is organized around a 60-meric dodecahedral
core comprising the C-terminal domains of E2p and a noncatalytic component, E3-binding
protein (E3BP), which specifically tethers E3 dimers to the PDC. A central issue concerning …
