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[phosphorylase] phosphatase activity

Known as: glycogen phosphorylase phosphatase activity, phosphorylase phosphatase activity, phosphorylase a phosphohydrolase activity 
Catalysis of the reaction: [phosphorylase a] + 4 H2O = 2 [phosphorylase b] + 4 phosphate. [EC:3.1.3.17, MetaCyc:PHOSPHORYLASE-PHOSPHATASE-RXN]
National Institutes of Health

Papers overview

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Highly Cited
1996
Highly Cited
1996
Two protein phosphatase 2A (PP2A) holoenzymes were isolated from rabbit skeletal muscle containing, in addition to the catalytic… Expand
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Highly Cited
1995
Highly Cited
1995
The p53 binding protein, termed p53BP2, was identified as a protein interacting with protein phosphatase 1 (PP1) in the yeast two… Expand
Highly Cited
1992
Highly Cited
1992
GCN2 is a protein kinase in Saccharomyces cerevisiae that is required for increased expression of the transcriptional activator… Expand
Highly Cited
1991
Highly Cited
1991
The fission yeast mutant dis3-54 is defective in mitosis and fails in chromosome disjunction. Its phenotype is similar to that of… Expand
Highly Cited
1990
Highly Cited
1990
PTPA, a specific phosphotyrosyl phosphatase activator of the PCSH2 and PCSL protein phosphatases, was purified up to apparent… Expand
Highly Cited
1988
Highly Cited
1988
The inhibitory effect of a marine-sponge toxin, okadaic acid, was examined on type 1, type 2A, type 2B and type 2C protein… Expand
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Highly Cited
1985
Highly Cited
1985
Protein phosphatases-2A0, 2A1 and 2A2 have been purified to homogeneity from rabbit skeletal muscle. Approximately 1 mg of… Expand
Highly Cited
1976
Highly Cited
1976
Using substrates purified from liver, the apparent Km values of synthase phosphatase ([UDPglucose--glycogen glucosyltransferase-D… Expand
Highly Cited
1975
Highly Cited
1975
Partially purified rabbit skeletal muscle phosphorylase phosphatase (EC 3.1.3.17; phosphoprotein phosphohydrolase) was… Expand
Highly Cited
1962
Highly Cited
1962
Glycogen phosphorylase in skeletal muscle exists as phosphorylase a, fully active, and phosphorylase b, active only in the… Expand
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