Regulatory properties of pyridine-nucleotide transhydrogenase from pseudomonas-aeruginosa - Active enzyme ultracentrifugation studies

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State: Public
Version: author
Serval ID
serval:BIB_F6311A53CBC5
Type
Article: article from journal or magazin.
Collection
Publications
Title
Regulatory properties of pyridine-nucleotide transhydrogenase from pseudomonas-aeruginosa - Active enzyme ultracentrifugation studies
Journal
Biochemistry
Author(s)
Widmer F., Kaplan N.O.
ISSN
0006-2960
Publication state
Published
Issued date
1976
Peer-reviewed
Oui
Volume
15
Number
21
Pages
4699-4703
Language
english
Abstract
Active enzyme ultracentrifugation studies of the pyridine nucleotide transhydrogenase from Pseudomonas aeruginosa (EC 1.6.1.1.) show that the enzymatic reaction is catalyzed by a molecular species characterized by an S20,W value of about 34 S, whatever the reduced substrate may be (tri- or diphosphopyridine nucleotide). The filamentous aggregated form of the enzyme (S20,W = 121 S and higher), identified by previous investigations (Cohen, P. T., and Kaplan, N. O. (1970), J. Biol. Chem. 245, 2825-2836; Louie, D. D., Kaplan, N. O., and Mc Lean, J. D. (1972), J. Mol. Biol. 70, 651-664), appears, therefore, to be an inactive species. The physiological implications of the enzyme are discussed. Several lines of evidence lead to the conclusion that the transhydrogenase might act as an essential link between carbohydrate catabolism and the respiratory chain.
Keywords
Macromolecular Substances, Molecular Weight, Nad, NADH, NADPH Oxidoreductases/*metabolism, Nadp, Pseudomonas aeruginosa/*enzymology, Ultracentrifugation
Pubmed
Web of science
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13/08/2015 8:53
Last modification date
20/08/2019 17:22
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