Protein phosphorylation by inorganic pyrophosphate in yeast mitochondria.

Abstract:

:Inorganic pyrophosphate can function as phosphate donor in protein phosphorylation reactions in yeast mitochondria. It was shown that, when PPi substitutes for ATP as inhibitor of the pyruvate dehydrogenase reaction, maximal activity is reached after a lag-period of 30-60 minutes. 32P-labeling of peptides shows that [32P]PPi gives about 25% of the labeling obtained by [gamma-32P]ATP in the protein kinase reaction. The PPi dependent phosphorylation is increased several fold by the presence of cold ATP.

authors

da Silva LP,Lindahl M,Lundin M,Baltscheffsky H

doi

10.1016/0006-291x(91)91043-c

subject

Has Abstract

pub_date

1991-08-15 00:00:00

pages

1359-64

issue

3

eissn

0006-291X

issn

1090-2104

pii

0006-291X(91)91043-C

journal_volume

178

pub_type

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