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Literature summary extracted from

  • Chan, K.F.J.; Graves, D.J.
    Rabbit skeletal muscle phosphorylase kinase. Catalytic and regulatory properties of the active alpha gamma delta and gamma delta complexes (1982), J. Biol. Chem., 257, 5948-5955.
    View publication on PubMed

Activating Compound

EC Number Activating Compound Comment Organism Structure
2.7.11.19 1,2-dimethoxyethane activation, 10% v/v, stimulates phosphorylase kinase and alphagammadelta (not gammadelta) subunit complex Oryctolagus cuniculus
2.7.11.19 Catalytic subunit of cAMP-dependent protein kinase activation of nonactivated enzyme Oryctolagus cuniculus
2.7.11.19 Catalytic subunit of cAMP-dependent protein kinase or alphagammadelta subunit complex Oryctolagus cuniculus
2.7.11.19 glycogen activation Oryctolagus cuniculus
2.7.11.19 glycogen stimulates phosphorylase kinase and alphagammadelta (not gammadelta) subunit complex Oryctolagus cuniculus
2.7.11.19 heparin activation Oryctolagus cuniculus
2.7.11.19 heparin stimulates only holoenzyme, not subunit complexes Oryctolagus cuniculus

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.7.11.19 1,2-dimethoxyethane above 10% v/v, stimulates below Oryctolagus cuniculus
2.7.11.19 ADP gammadelta subunit complex Oryctolagus cuniculus
2.7.11.19 EGTA alphagammadelta and gammadelta subunit complexes less sensitive than holoenzyme; Ca2+ restores; effect on kinetic parameters Oryctolagus cuniculus
2.7.11.19 glucose 6-phosphate not (gammadelta subunit complex) Oryctolagus cuniculus
2.7.11.19 GTP gammadelta subunit complex Oryctolagus cuniculus
2.7.11.19 Histone VIIS gammadelta subunit complex Oryctolagus cuniculus
2.7.11.19 ITP not (gammadelta subunit complex) Oryctolagus cuniculus
2.7.11.19 Mn2+ free Mn2+ Oryctolagus cuniculus
2.7.11.19 additional information no inhibition by CTP, caffeine, cAMP, cGMP, IMP, glucose 6-phosphate (gammadelta subunit complex); no inhibition by glucose 1-phosphate (gammadelta subunit complex) Oryctolagus cuniculus
2.7.11.19 UTP weak, gammadelta subunit complex 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 kinetic properties of subunit complexes at pH 6.8 and 8.5 Oryctolagus cuniculus
2.7.11.19 0.08
-
 MgATP2- phosphorylase b, activated enzyme Oryctolagus cuniculus
2.7.11.19 0.094
-
 phosphorylase b pH 8.2, gammadelta subunit complex Oryctolagus cuniculus
2.7.11.19 0.11
-
 phosphorylase b pH 8.2, alphagammadelta subunit complex Oryctolagus cuniculus
2.7.11.19 0.22
-
 ATP pH 8.2, nonactivated enzyme Oryctolagus cuniculus
2.7.11.19 0.25
-
 phosphorylase b pH 8.2, nonactivated enzyme Oryctolagus cuniculus
2.7.11.19 0.5
-
 ATP pH 8.2, alphagammadelta subunit complex Oryctolagus cuniculus
2.7.11.19 0.95
-
 ATP pH 8.2, gammadelta subunit complex Oryctolagus cuniculus

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.7.11.19 Mg2+ requirement Oryctolagus cuniculus
2.7.11.19 Mg2+ 10 mM 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 Mn2+ free Mn2+ inhibits Oryctolagus cuniculus
2.7.11.19 Mn2+ at equimolar concentration of metal ion and ATP Mn2+ more effective than Mg2+ Oryctolagus cuniculus
2.7.11.19 Mn2+ optimal at ATP:Mg ratio of 1:1 Oryctolagus cuniculus
2.7.11.19 phosphate alphagammadelta complex undergoes autophosphorylation: up to 4.2 mol phosphate/mol complex incorporated into alpha subunit Oryctolagus cuniculus
2.7.11.19 phosphate requirement, phosphate containing enzyme Oryctolagus cuniculus
2.7.11.19 phosphate gammadelta subunit complex cannot phosphorylate itself but phosphorylates and activates native enzyme, even in the presence of EGTA or protein kinase inhibitor Oryctolagus cuniculus

Organism

EC Number Organism UniProt Comment Textmining
2.7.11.19 Oryctolagus cuniculus
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.7.11.19 2 ATP + phosphorylase b = 2 ADP + phosphorylase a mechanism Oryctolagus cuniculus
a

Source Tissue

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.7.11.19 ATP + alphagammadelta subunit complex autophosphorylation, by incorporation of phosphate into alpha subunit Oryctolagus cuniculus ADP + activated alphagammadelta subunit complex
-
 ?
2.7.11.19 ATP + phosphorylase b cosubstrate: Mg-ATP complex Oryctolagus cuniculus ADP + phosphorylase a
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.7.11.19 91.4
-
 phosphorylase b nonactivated enzyme Oryctolagus cuniculus
2.7.11.19 99
-
 phosphorylase b alphagammadelta subunit complex Oryctolagus cuniculus
2.7.11.19 104
-
 phosphorylase b gammadelta subunit complex Oryctolagus cuniculus