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Literature summary for 2.7.11.19 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

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

General Stability

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

Inhibitors

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

KM Value [mM]

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

Metals/Ions

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

Organism

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

Purification (Commentary)

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

Source Tissue

Source Tissue Comment Organism Textmining
skeletal muscle
-
Oryctolagus cuniculus
-

Specific Activity [micromol/min/mg]

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

Storage Stability

Storage Stability Organism
Frozen, at least 6 months Oryctolagus cuniculus

Substrates and Products (Substrate)

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

Temperature Optimum [°C]

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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
-
Oryctolagus cuniculus

Cofactor

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