Three-dimensional structure of a lipoyl domain fromthe dihydrolipoyl acetyltransferase component of the pyruvate dehydrogenase multienzyme complex of Escherichia coli-Reference-Cited by-同舟云学术

Three-dimensional structure of a lipoyl domain fromthe dihydrolipoyl acetyltransferase component of the pyruvate dehydrogenase multienzyme complex of Escherichia coli

Published:1995-01 Issue:2 Volume:248 Page:328-343
ISSN:0022-2836
Container-title:Journal of Molecular Biology
language:en
Short-container-title:Journal of Molecular Biology

Author:

Green James D.F.,Laue Ernest D.,Perham Richard N.,Ali Sohail T.,Guest John R.

Publisher

Elsevier BV

Subject

Molecular Biology,Structural Biology

Reference59 articles.

1. Isolation and characterization of lipoylated and unlipoylated domains of the E2p subunit of the pyruvate dehydrogenase complex of Escherichia coli;Ali;Biochem. J.,1990

2. Two lipoyl domains in the dihydrolipoamide acetyltransferase chain of the pyruvate dehydrogenase multienzyme complex of Streptococcus faecalis;Allen;FEBS Letters,1991

3. Reductive acetylation of tandemly repeated lipoyl domains in the pyruvate dehydrogen ase multienzyme complex of Escherichia coli is random order;Allen;J. Mol. Biol.,1989

4. A two-dimensional nuclear overhauser enhancement experiment for the elucidation of the complete 1H-1H cross-relaxation networks in biological macromolecules;Anil;Biochem. Biophys. Res. Commun.,1980

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