Use of trypsin and lipoamidase to study the role of lipoic acid moieties in the pyruvate and alpha-ketoglutarate dehydrogenase complexes of Escherichia coli.

Abstract

The relationships between release of (3)H-labeled lipoyl moieties by trypsin and lipoamidase and accompanying loss of overall enzymatic activity of the Escherichia coli pyruvate and alpha-ketoglutarate dehydrogenase complexes were studied. Trypsin releases lipoyl domains together with their covalently attached lipoyl moieties from the "inner" core of the… (More)

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Cite this paper

@article{Stepp1981UseOT, title={Use of trypsin and lipoamidase to study the role of lipoic acid moieties in the pyruvate and alpha-ketoglutarate dehydrogenase complexes of Escherichia coli.}, author={L R Stepp and Dennis M Bleile and Donald K. McRorie and Flora H Pettit and Lester Reed}, journal={Biochemistry}, year={1981}, volume={20 16}, pages={4555-60} }