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Literature summary for 2.7.11.19 extracted from

  • Cohen, P.; Klee, C.B.; Picton, C.; Shenolikar, S.
    Calcium control of muscle phosphorylase kinase through the combined action of calmodulin and troponin (1980), Ann. N. Y. Acad. Sci., 356, 151-161.
    View publication on PubMed
Search for more literature for 2.7.11.19

Activating Compound

Activating Compound Comment Organism Structure
Artificial thin filaments activation, made by mixing actin, tropomyosin and troponin complex Rattus norvegicus
Artificial thin filaments activation, made by mixing actin, tropomyosin and troponin complex Oryctolagus cuniculus
Catalytic subunit of cAMP-dependent protein kinase activation of nonactivated enzyme Rattus norvegicus
Catalytic subunit of cAMP-dependent protein kinase activation of nonactivated enzyme Oryctolagus cuniculus
Catalytic subunit of cAMP-dependent protein kinase at low Mg2+-concentration, 2 phosphorylation sites, one Ser residue on alpha and beta subunit each Rattus norvegicus
Catalytic subunit of cAMP-dependent protein kinase at low Mg2+-concentration, 2 phosphorylation sites, one Ser residue on alpha and beta subunit each Oryctolagus cuniculus
Catalytic subunit of cGMP-dependent protein kinase not Rattus norvegicus
Catalytic subunit of cGMP-dependent protein kinase not Oryctolagus cuniculus
additional information no activation by parvalbumin Rattus norvegicus
additional information no activation by parvalbumin Oryctolagus cuniculus
additional information the nonactivated enzyme is activated either by limited proteolysis Rattus norvegicus
additional information the nonactivated enzyme is activated either by limited proteolysis Oryctolagus cuniculus
troponin C activation Rattus norvegicus
troponin C activation Oryctolagus cuniculus
troponin C presumably key event in vivo, coupling glycogenolysis and muscle contraction Rattus norvegicus
troponin C presumably key event in vivo, coupling glycogenolysis and muscle contraction Oryctolagus cuniculus
troponin C can replace extrinsic calmodulin Rattus norvegicus
troponin C can replace extrinsic calmodulin Oryctolagus cuniculus
Trypsin proteolytic activation of nonactivated enzyme Rattus norvegicus
Trypsin proteolytic activation of nonactivated enzyme Oryctolagus cuniculus
Trypsin accompanied by loss of absolute requirement for Ca2+, activates holoenzyme and alphagammadelta subunit complex, not gammadelta complex Rattus norvegicus
Trypsin accompanied by loss of absolute requirement for Ca2+, activates holoenzyme and alphagammadelta subunit complex, not gammadelta complex Oryctolagus cuniculus
Trypsin strong, by limited proteolysis of alpha and beta subunits Rattus norvegicus
Trypsin strong, by limited proteolysis of alpha and beta subunits Oryctolagus cuniculus

Inhibitors

Inhibitors Comment Organism Structure
Antibodies to delta subunit of phosphorylase kinase
-
 Rattus norvegicus
Antibodies to rat testis calmodulin calmodulin or troponin (the latter at high concentrations) reverses Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
glycogen particle together with other enzymes of glycogen metabolism linked together on glycogen particles Rattus norvegicus
-
-
glycogen particle together with other enzymes of glycogen metabolism linked together on glycogen particles Oryctolagus cuniculus
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ delta-subunit confers Ca2+-sensitivity to the phosphorylase kinase reaction Rattus norvegicus
Ca2+ delta-subunit confers Ca2+-sensitivity to the phosphorylase kinase reaction Oryctolagus cuniculus
Ca2+ requirement (trypsin activation leads to loss of absolute requirement) Rattus norvegicus
Ca2+ requirement (trypsin activation leads to loss of absolute requirement) Oryctolagus cuniculus
Mg2+ requirement Rattus norvegicus
Mg2+ requirement Oryctolagus cuniculus
Mg2+ major role of Mg2+: cosubstrate in Mg2+-ATP complex Rattus norvegicus
Mg2+ major role of Mg2+: cosubstrate in Mg2+-ATP complex Oryctolagus cuniculus
phosphate requirement, phosphate containing enzyme Rattus norvegicus
phosphate requirement, phosphate containing enzyme Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + glycogen synthase Rattus norvegicus decreases activity of this substrate ?
-
 ?
ATP + glycogen synthase Oryctolagus cuniculus decreases activity of this substrate ?
-
 ?
ATP + phosphorylase b Rattus norvegicus stimulates glycogenolysis in skeletal muscle ?
-
 ?
ATP + phosphorylase b Oryctolagus cuniculus stimulates glycogenolysis in skeletal muscle ?
-
 ?
ATP + phosphorylase b Rattus norvegicus regulates conversion of inactive phosphorylase b into active phosphorylase a ?
-
 ?
ATP + phosphorylase b Oryctolagus cuniculus regulates conversion of inactive phosphorylase b into active phosphorylase a ?
-
 ?

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
skeletal muscle
-
 Rattus norvegicus
-
skeletal muscle
-
 Oryctolagus cuniculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + glycogen synthase decreases activity of this substrate Rattus norvegicus ?
-
 ?
ATP + glycogen synthase decreases activity of this substrate Oryctolagus cuniculus ?
-
 ?
ATP + glycogen synthase
-
 Rattus norvegicus ADP + phosphoglycogen synthase
-
 ?
ATP + glycogen synthase
-
 Oryctolagus cuniculus ADP + phosphoglycogen synthase
-
 ?
ATP + phosphorylase b cosubstrate: Mg-ATP complex Rattus norvegicus ADP + phosphorylase a
-
 ?
ATP + phosphorylase b cosubstrate: Mg-ATP complex Oryctolagus cuniculus ADP + phosphorylase a
-
 ?
ATP + phosphorylase b stimulates glycogenolysis in skeletal muscle Rattus norvegicus ?
-
 ?
ATP + phosphorylase b stimulates glycogenolysis in skeletal muscle Oryctolagus cuniculus ?
-
 ?
ATP + phosphorylase b regulates conversion of inactive phosphorylase b into active phosphorylase a Rattus norvegicus ?
-
 ?
ATP + phosphorylase b regulates conversion of inactive phosphorylase b into active phosphorylase a Oryctolagus cuniculus ?
-
 ?

Subunits

Subunits Comment Organism
More the delta subunit is firmly bound to holoenzyme whereas delta' subunit (i.e. calmodulin) is bound only in the presence of Ca2+ Rattus norvegicus
More the delta subunit is firmly bound to holoenzyme whereas delta' subunit (i.e. calmodulin) is bound only in the presence of Ca2+ Oryctolagus cuniculus

Cofactor

Cofactor Comment Organism Structure
Calmodulin requirement Rattus norvegicus
Calmodulin requirement Oryctolagus cuniculus
Calmodulin calmodulin containing enzyme i.e. tightly bound delta subunit Rattus norvegicus
Calmodulin calmodulin containing enzyme i.e. tightly bound delta subunit Oryctolagus cuniculus
Calmodulin in the presence of Ca2+ phosphorylase kinase binds a second molecule calmodulin (i.e. delta' subunit) producing additional activation Rattus norvegicus
Calmodulin in the presence of Ca2+ phosphorylase kinase binds a second molecule calmodulin (i.e. delta' subunit) producing additional activation Oryctolagus cuniculus