The lipoyl domain and its role in thiamin diphosphate-dependent oxidative decarboxylation.

Abstract

In most cells the oxidative decarboxylation of 2-oxo acids is carried out by multienzyme complexes of unusually elaborate structure. They comprise three different enzymes and are assembled round a core consisting of multiple copies of the lipoate acyltransferase (E2) subunit arranged with octahedral (24-mer) or icosahedral (60-mer) symmetry (for recent… (More)

Topics

Cite this paper

@article{Perham1992TheLD, title={The lipoyl domain and its role in thiamin diphosphate-dependent oxidative decarboxylation.}, author={Richard N. Perham and A C Borges and F. Dardel and Lisa Graham and C. F. Hawkins and E D Laue and Len C. Packman}, journal={Journal of nutritional science and vitaminology}, year={1992}, volume={Spec No}, pages={457-60} }