Self-assembly and catalytic activity of the pyruvate dehydrogenase multienzyme complex of Escherichia coli

Studies of the self-assembly of pyruvate dehydrogenase of Escherichia coli show that the catalytic activity is proportional to the state of assembly and uncover a novel functional connection of active sites in this multienzyme complex.

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Bibliographic Details
Published in:Nature (London) 1977-07, Vol.268 (5618), p.313-316
Main Authors: Bates, David L, Danson, Michael J, Hale, Geoffrey, Hooper, Elizabeth A, Perham, Richard N
Format: Article
Language:English
Subjects:
Acetyltransferases - metabolism
Binding Sites
Catalysis
Dihydrolipoamide Dehydrogenase - metabolism
Escherichia coli - enzymology
Humanities and Social Sciences
multidisciplinary
Peptides - metabolism
Protein Conformation
Pyruvate Dehydrogenase Complex - metabolism
Science
Science (multidisciplinary)
Structure-Activity Relationship
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Description
Summary:Studies of the self-assembly of pyruvate dehydrogenase of Escherichia coli show that the catalytic activity is proportional to the state of assembly and uncover a novel functional connection of active sites in this multienzyme complex.
ISSN:0028-0836
1476-4687
DOI:10.1038/268313a0