Alpha-keto acid dehydrogenase complexes. X. Regulation of the activity of the pyruvate dehydrogenase complex from beef kidney mitochondria by phosphorylation and dephosphorylation.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 62 ·No. 1 ·1969-01-00 ·Pages 234-41

Linn TC, Pettit FH, Reed LJ

Abstract

This paper reports the discovery that the activity of the multienzyme pyruvate dehydrogenase complex from beef kidney mitochondria is regulated by a phosphorylation-dephosphorylation reaction sequence. The site of this regulation is the pyruvate dehydrogenase component of the complex. Phosphorylation and concomitant inactivation of pyruvate dehydrogenase are catalyzed by an ATP-specific kinase (i.e., a pyruvate dehydrogenase kinase), and dephosphorylation and concomitant reactivation are catalyzed by a phosphatase (i.e., a pyruvate dehydrogenase phosphatase). The kinase and the phosphatase appear to be regulatory subunits of the pyruvate dehydrogenase complex.

MeSH Terms

Animals Catalysis Cattle Kidney/enzymology Magnesium Oxidative Phosphorylation Phosphoric Monoester Hydrolases Phosphotransferases Pyruvate Oxidase/metabolism Ultracentrifugation

Chemicals

Pyruvate Oxidase Phosphotransferases Phosphoric Monoester Hydrolases Magnesium

Authors & Affiliations

3 authors, click to expand affiliations / ORCID

Linn T C

Pettit F H

Reed L J

References (13)

13 references, click to expand

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Article Info

Journal

Proceedings of the National Academy of Sciences of the United States of America

Abbr.

Proc Natl Acad Sci U S A

ISSN

0027-8424

DOI

10.1073/pnas.62.1.234

Published

1969-01-00

Pages

234-41

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC285978

Subset

External Links

PubMed source DOI: 10.1073/pnas.62.1.234 PMC Full Text View journal details

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Alpha-keto acid dehydrogenase complexes. X. Regulation of the activity of the pyruvate dehydrogenase complex from beef kidney mitochondria by phosphorylation and dephosphorylation.

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