Journal ArticleDOI
Amino acid sequence at the phosphorylated site of rat liver pyruvate kinase.
Bror Edlund,Jill Andersson,Vincent P.K. Titanji,Ulla Dahlqvist,Pia Ekman,Örjan Zetterqvist,Lorentz Engström +6 more
TLDR
One dominating peptic phosphopeptide was obtained from rat liver pyruvate kinase (type L) phosphorylated by cyclic 3′,5′-AMP-stimulated protein kinase from the same tissue.About:
This article is published in Biochemical and Biophysical Research Communications.The article was published on 1975-12-15. It has received 50 citations till now. The article focuses on the topics: Pyruvate dehydrogenase kinase & Pyruvate kinase.read more
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Book ChapterDOI
The role of cyclic-AMP-dependent protein kinase in the regulation of glycogen metabolism in mammalian skeletal muscle.
TL;DR: The role of cyclic-AMP-dependent protein kinase in the regulation of glycogen metabolism in mammalian skeletal muscle is discussed, which determines the time at which dephosphorylation of the β subunit and inactivation of the enzyme can become rapid through phosphorylations of the α subunit.
Journal ArticleDOI
Multiple pathway signal transduction by the cAMP-dependent protein kinase.
Donal A. Walsh,S. M. Van Patten +1 more
TL;DR: This review focuses on the first simple question that must be addressed, namely, how might proteins vary as substrates for the cAMP‐dependent protein kinase and what ramifications might such variations have for the consequential events within the cell.
Journal ArticleDOI
The isolation, characterization, and sequence of the pyruvate kinase gene of Saccharomyces cerevisiae.
TL;DR: The Saccharomyces cerevisiae gene encoding the glycolytic enzyme pyruvate kinase has been isolated by complementation of a pyk mutant with DNA from a wild type yeast genomic library and appears to be a common consensus site for yeast RNA polymerase II transcriptional starts.
Journal ArticleDOI
Optimal spatial requirements for the location of basic residues in peptide substrates for the cyclic AMP-dependent protein kinase.
TL;DR: Direct binding studies of N alpha-[3H]acetyl peptides to catalytic subunit of cyclic AMP-dependent protein kinase revealed a correlation between binding affinity and the ability to serve as substrate for the enzyme.
Journal ArticleDOI
The minimum substrate of cyclic AMP-stimulated protein kinase, as studied by synthetic peptides representing the phosphorylatable site of pyruvate kinase (type L) of rat liver.
TL;DR: Synthetic peptides, representing part of the phosphorylatable site of rat liver pyruvate kinase, were phosphorylated by (32P)ATP and the catalytic subunit of cyclic AMP-stimulated protein kinase.
References
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Journal ArticleDOI
Phosphorylation of purified rat liver pyruvate kinase by cyclic 3′,5′-AMP-stimulated protein kinase
TL;DR: The results suggest that the L type of rat liver pyruvate kinase belongs to the enzymes whose activity is regulated by phosphorylation-dephosphorylation reactions.
Journal ArticleDOI
The hormonal control of activity of skeletal muscle phosphorylase kinase. Amino-acid sequences at the two sites of action of adenosine-3':5'-monophosphate-dependent protein kinase.
TL;DR: The results and an inspection of the rate of phosphorylation of a number of skeletal muscle proteins, including each enzyme of the glycolytic pathway, lead to the conclusion that cyclic-AMP-dependent protein kinase is an extremely specific enzyme.
Journal ArticleDOI
Amino acid sequence of a (32P)phosphopeptide from pig liver pyruvate kinase phosphorylated by cyclic 3′,5′-AMP-stimulated protein kinase and γ-(32P)ATP
TL;DR: P pig liver pyruvate kinase (type L) was 32 P-labelled by incubation with ( 32 P)ATP and cyclic 3′,5′-AMP-stimulated protein kinase from the same source.
Journal ArticleDOI
Bovine brain Na+,K+-stimulated ATP phosphohydrolase studied by a rapid-mixing technique. K+-stimulated liberation of [32P] orthophosphate from [32P] phosphoenzyme and resolution of the dephosphorylation into two phases.
TL;DR: It was concluded that this K+-stimulated dephosphorylation and liberation of [32P]orthophosphate from the [ 32P]phosphoenzyme was rapid enough to participate in the Na+,K+- Stimulated hydrolysis of ATP.