Literature summary for 2.4.1.1 extracted from

Lin, K.; Hwang, P.K.; Fletterick, R.J.
Mechanism of regulation in yeast glycogen phosphorylase (1995), J. Biol. Chem., 270, 26833-26839.

Search for more literature for 2.4.1.1

Activating Compound

Activating Compound	Comment	Organism	Structure
Phosphorylase kinase	1000fold increase in activity after phosphorylation	Saccharomyces cerevisiae

Cloned(Commentary)

Cloned (Comment)	Organism
expression of wild-type and N-terminal deletion mutant glycogen phosphorylase in Escherichia coli	Saccharomyces cerevisiae

Inhibitors

Inhibitors	Comment	Organism	Structure
glucose 6-phosphate	-	Saccharomyces cerevisiae

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
0.86	-	glucose 1-phosphate	-	Saccharomyces cerevisiae

Organism

Organism	UniProt	Comment	Textmining
Saccharomyces cerevisiae	-	-	-

Posttranslational Modification

Posttranslational Modification	Comment	Organism
side-chain modification	-	Saccharomyces cerevisiae

Cofactor

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	1 pyridoxal 5'-phosphate/subunit	Saccharomyces cerevisiae

Ki Value [mM]

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism	Structure
0.29	-	glucose 6-phosphate	unphosphorylated glycogen phosphorylase	Saccharomyces cerevisiae
4.8	-	glucose 6-phosphate	phosphorylated glycogen phosphorylase	Saccharomyces cerevisiae

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Release 2023.1 (January 2023)