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Literature summary extracted from

  • Krebs, E.G.; Love, D.S.; Bratvold, G.E.; Trayser, K.A.; Meyer, W.L.; Fischer, E.H.
    Purification and properties of rabbit skeletal muscle phosphorylase b kinase (1964), Biochemistry, 3, 1022-1033.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.11.19 adenosine 3',5'-monophosphate i.e. cAMP, activation of nonactivated enzyme, not alone, only in the presence of Mg2+ or Mn2+ Oryctolagus cuniculus
2.7.11.19 adenosine 3',5'-monophosphate no enhancement or inhibition of this activation by various nucleotides and other compounds, overview Oryctolagus cuniculus
2.7.11.19 Ca2+-dependent protease proteolytic activation of nonactivated enzyme Oryctolagus cuniculus
2.7.11.19 Ca2+-dependent protease i.e. kinase-activating factor Oryctolagus cuniculus
2.7.11.19 glycogen activation Oryctolagus cuniculus
2.7.11.19 glycogen pH-dependent Oryctolagus cuniculus
2.7.11.19 heparin activation Oryctolagus cuniculus
2.7.11.19 heparin pH-dependent Oryctolagus cuniculus
2.7.11.19 additional information phosphorylation by protein kinases Oryctolagus cuniculus
2.7.11.19 additional information no activation by g poly-aspartic acid, hexametaphosphate, yeast nucleic acid, at pH 6.8 Oryctolagus cuniculus
2.7.11.19 additional information No activation by substrates of phosphorylase b reaction, i.e. AMP or glucose 1-phosphate Oryctolagus cuniculus
2.7.11.19 additional information the nonactivated enzyme is activated either by limited proteolysis Oryctolagus cuniculus
2.7.11.19 Trypsin at low concentration Oryctolagus cuniculus
2.7.11.19 Trypsin proteolytic activation of nonactivated enzyme Oryctolagus cuniculus

General Stability

EC Number General Stability Organism
2.7.11.19 Unstable in the presence of Mg2+ Oryctolagus cuniculus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.11.19 ATP otherwise activating; total inhibition if ATP concentration exceeds that of divalent cation (i.e. Mg2+) Oryctolagus cuniculus
2.7.11.19 glucose less effective than glucose 6-phosphate, pH 8.2 Oryctolagus cuniculus
2.7.11.19 glucose 6-phosphate pH 8.2 Oryctolagus cuniculus
2.7.11.19 heparin depending on pH it inhibits or activates nonactivated enzyme Oryctolagus cuniculus
2.7.11.19 Hexametaphosphate pH 8.2 Oryctolagus cuniculus
2.7.11.19 additional information no inhibition by glucose 1-phosphate (gammadelta subunit complex); no inhibition by spermidine, spermine, F-; no inhibition by UDPglucose Oryctolagus cuniculus
2.7.11.19 Polyaspartic acid pH 8.2 Oryctolagus cuniculus
2.7.11.19 protamine pH 8.2 Oryctolagus cuniculus
2.7.11.19 Zn2+
-
 Oryctolagus cuniculus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.7.11.19 additional information
-
 additional information pH-dependence of kinetic parameters Oryctolagus cuniculus
2.7.11.19 0.01
-
 phosphorylase b pH 7.5, in the presence of glycogen Oryctolagus cuniculus
2.7.11.19 0.015 0.017 phosphorylase b activated enzyme, pH 8.2 Oryctolagus cuniculus
2.7.11.19 0.03 0.037 ATP pH 8.5 Oryctolagus cuniculus
2.7.11.19 0.03 0.037 ATP phosphorylase b Oryctolagus cuniculus
2.7.11.19 0.03 0.037 ATP activated enzyme, pH 7.5 Oryctolagus cuniculus
2.7.11.19 0.04
-
 phosphorylase b before activation, pH 8.2 Oryctolagus cuniculus
2.7.11.19 0.12
-
 phosphorylase b pH 7.5 Oryctolagus cuniculus
2.7.11.19 0.125
-
 phosphorylase b before activation, pH 7.5 Oryctolagus cuniculus
2.7.11.19 0.24
-
 ATP nonactivated enzyme, pH 7.5 Oryctolagus cuniculus
2.7.11.19 0.25
-
 phosphorylase b pH 7.6 Oryctolagus cuniculus
2.7.11.19 0.38
-
 ATP activated enzyme, pH 7.5 Oryctolagus cuniculus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.11.19 Mg2+ requirement Oryctolagus cuniculus
2.7.11.19 Mg2+ major role of Mg2+: cosubstrate in Mg2+-ATP complex Oryctolagus cuniculus
2.7.11.19 Mn2+ requirement Oryctolagus cuniculus
2.7.11.19 Mn2+ can substitute for Mg2+ Oryctolagus cuniculus
2.7.11.19 phosphate requirement, phosphate containing enzyme Oryctolagus cuniculus

Organism

EC Number Organism UniProt Comment Textmining
2.7.11.19 Oryctolagus cuniculus
-
 New Zealand white (female)
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.7.11.19 as nonactivated enzyme Oryctolagus cuniculus
2.7.11.19 to near homogeneity (phosphorylase b is a persistent contaminant) Oryctolagus cuniculus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.7.11.19 skeletal muscle
-
 Oryctolagus cuniculus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.7.11.19 additional information
-
-
 Oryctolagus cuniculus

Storage Stability

EC Number Storage Stability Organism
2.7.11.19 Frozen, at least 6 months Oryctolagus cuniculus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.11.19 ATP + phosphorylase b cosubstrate: Mg-ATP complex Oryctolagus cuniculus ADP + phosphorylase a
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.7.11.19 30
-
 assay at Oryctolagus cuniculus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.7.11.19 additional information
-
-
 Oryctolagus cuniculus

Cofactor

EC Number Cofactor Comment Organism Structure
2.7.11.19 ADP activation Oryctolagus cuniculus
2.7.11.19 ADP can partially replace ATP in the activation of nonactivated enzyme Oryctolagus cuniculus
2.7.11.19 ATP activation of nonactivated enzyme by phosphorylation of subunits A and B, not C Oryctolagus cuniculus