Structure and symmetry of B. stearothermophilus pyruvate dehydrogenase multienzyme complex and implications for eucaryote evolution-Reference-Cited by-同舟云学术

Structure and symmetry of B. stearothermophilus pyruvate dehydrogenase multienzyme complex and implications for eucaryote evolution

Published:1979-05 Issue:1 Volume:17 Page:85-93
ISSN:0092-8674
Container-title:Cell
language:en
Short-container-title:Cell

Author:

Henderson Christopher E.,Perham Richard N.,Finch John T.

Publisher

Elsevier BV

Subject

General Biochemistry, Genetics and Molecular Biology

Reference35 articles.

1. Selective inactivation of the transacylase components of the 2-oxo acid dehydrogenase multienzyme complexes of Escherichia coli;Brown;Biochem. J.,1976

2. Acyl group and electron pair relay system: a network of interacting lipoyl moieties in the pyruvate and α-ketoglutarate dehydrogenase complexes from Escherichia coli;Collins,1977

3. Evidence for two lipoic acid residues per lipoate acetyltransferase chain in the pyruvate dehydrogenase multienzyme complex of Escherichia coli;Danson;Biochem. J.,1976

4. Intramolecular coupling of active sites in the pyruvate dehydrogenase multienzyme complex of Escherichia coli;Danson;Biochem. J.,1978

5. Molecular weight and symmetry of the pyruvate dehydrogenase multienzyme complex of Escherichia coli;Danson;J. Mol. Biol.,1979

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