Literature summary for 2.4.1.1 extracted from

Chen, G.S.; Segel, I.H.
Purification and properties of glycogen phosphorylase from Escherichia coli (1968), Arch. Biochem. Biophys., 127, 175-186.

Activating Compound

Activating Compound	Comment	Organism
5'-AMP	activation	Escherichia coli
5'-AMP	in both directions	Escherichia coli
CNO-	slight activation	Escherichia coli
additional information	not activated by 2'-AMP, 3'-AMP, ADP, adenosine	Escherichia coli
additional information	not activated by ATP, cAMP	Escherichia coli
Na2SO4	activation	Escherichia coli

Inhibitors	Comment	Organism
ADPglucose	competitive inhibition	Escherichia coli
Ag+	strong inhibition	Escherichia coli
alpha-Amylose	-	Escherichia coli
beta-Amylose	-	Escherichia coli
Ca2+	weak	Escherichia coli
CN-	-	Escherichia coli
Cu2+	1 mM, strong inhibition	Escherichia coli
D-glucose	non-competitive	Escherichia coli
Fe2+	weak inhibition	Escherichia coli
glucose 1-phosphate	above 2 mM; substrate inhibition	Escherichia coli
Hg2+	1 mM, strong inhibition	Escherichia coli
iodoacetamide	weak	Escherichia coli
iodoacetate	weak inhibition	Escherichia coli
K2S2O8	-	Escherichia coli
KNO3	-	Escherichia coli
additional information	not inhibited by Mg2+ and Mn2+	Escherichia coli
N-ethylmaleimide	weak	Escherichia coli
p-chloromercuribenzoate	1 mM, 55% inhibition	Escherichia coli
TDPglucose	competitive inhibition	Escherichia coli
UDPglucose	-	Escherichia coli
Zn2+	strong inhibition	Escherichia coli

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
additional information	-	additional information	0.46% glycogen, with AMP, 0.67% glycogen, without AMP	Escherichia coli
1	-	Glucose-1-phosphate	-	Escherichia coli

Metals/Ions	Comment	Organism	Structure
additional information	not activated by Cl-	Escherichia coli
NaF	activation, maximal at 200 mM	Escherichia coli

Organism	UniProt	Comment	Textmining
Escherichia coli	-	K-12	-

Purification (Comment)	Organism
pH 5.3, protamine sulfate, ammonium sulfate, DEAE-cellulose, Sephadex G-200	Escherichia coli

Specific Activity Minimum [µmol/min/mg]	Specific Activity Maximum [µmol/min/mg]	Comment	Organism
0.118	-	-	Escherichia coli

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.
glycogen + glucose 1-phosphate	-	Escherichia coli	glycogen + phosphate	-	r
[(1->4)-alpha-D-glucosyl]n + phosphate	favoured reaction	Escherichia coli	[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate	-	r
[(1->4)-alpha-D-glucosyl]n + phosphate	polyglucose primer required	Escherichia coli	[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate	-	r
[(1->4)-alpha-D-glucosyl]n + phosphate	catalyzes incorporation of glucose into alpha-1,4-glucosidic linkage on exterior chains of primer, glycogen synthesis is preferred	Escherichia coli	[(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate	-	r

pH Optimum Minimum	pH Optimum Maximum	Comment	Organism
6.7	6.9	glycogen	Escherichia coli

pH Minimum	pH Maximum	Comment	Organism
6	7.5	approx. half-maximal activity at pH 6.0 and 7.5	Escherichia coli

Cofactor	Comment	Organism	Structure
pyridoxal 5'-phosphate	requirement	Escherichia coli

Ki Value [mM]	Ki Value maximum [mM]	Inhibitor	Comment	Organism
0.7	-	ADP-glucose	-	Escherichia coli
1	-	TDP-glucose	-	Escherichia coli
2	-	UDP-glucose	-	Escherichia coli
2.5	-	glucose	-	Escherichia coli