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Literature summary extracted from

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

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.4.1.1 5'-AMP activation Escherichia coli
2.4.1.1 5'-AMP in both directions Escherichia coli
2.4.1.1 CNO- slight activation Escherichia coli
2.4.1.1 additional information not activated by 2'-AMP, 3'-AMP, ADP, adenosine Escherichia coli
2.4.1.1 additional information not activated by ATP, cAMP Escherichia coli
2.4.1.1 Na2SO4 activation Escherichia coli

Inhibitors

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

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.1.1 additional information
-
additional information 0.46% glycogen, with AMP, 0.67% glycogen, without AMP Escherichia coli
2.4.1.1 1
-
Glucose-1-phosphate
-
Escherichia coli

Metals/Ions

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

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.1 Escherichia coli
-
K-12
-

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.4.1.1 0.118
-
-
Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.1 glycogen + glucose 1-phosphate
-
Escherichia coli glycogen + phosphate
-
r
2.4.1.1 [(1->4)-alpha-D-glucosyl]n + phosphate favoured reaction Escherichia coli [(1->4)-alpha-D-glucosyl]n-1 + alpha-D-glucose 1-phosphate
-
r
2.4.1.1 [(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
2.4.1.1 [(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

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.1 6.7 6.9 glycogen Escherichia coli

pH Range

EC Number pH Minimum pH Maximum Comment Organism
2.4.1.1 6 7.5 approx. half-maximal activity at pH 6.0 and 7.5 Escherichia coli

Cofactor

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

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.4.1.1 0.7
-
ADP-glucose
-
Escherichia coli
2.4.1.1 1
-
TDP-glucose
-
Escherichia coli
2.4.1.1 2
-
UDP-glucose
-
Escherichia coli
2.4.1.1 2.5
-
glucose
-
Escherichia coli