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Literature summary for 2.7.11.19 extracted from

  • Kumar, P.; Brushia, R.J.; Hoye, E.; Walsh, D.A.
    Baculovirus-mediated overexpression of the phosphorylase b kinase holoenzyme and alpha gamma delta and gamma delta subcomplexes (2004), Biochemistry, 43, 10247-10254.
    View publication on PubMed
Search for more literature for 2.7.11.19

Cloned(Commentary)

Cloned (Comment) Organism
cooverexpression with the beta subunit of the rabbit enzyme with the rat holoenzyme and rat alphagammadelta and gammadelta subunit complexes in Spodoptera frugiperda Sf9 cells via the baculovirus infection system, resulting in formation of subunit subcomplexes, overview Oryctolagus cuniculus
subcloning of subunits in Escherichia coli, overexpression of the soluble holoenzyme and of soluble trimeric alphagammadelta and dimeric gammadelta subunit subcomplexes, as well as coexpression with the beta subunit of the rabbit enzyme also resulting in subunit complex formation, in Spodoptera frugiperda Sf9 cells via the baculovirus infection system Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activates, dependent on, required for binding of calmodulin Oryctolagus cuniculus
Ca2+ activates, dependent on, required for binding of calmodulin Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-
Rattus norvegicus Q64649 alpha subunit of the skeletal muscle enzyme
-

Posttranslational Modification

Posttranslational Modification Comment Organism
additional information the native and the recombinant enzyme performs autophosphorylation of its alpha and beta subunits Oryctolagus cuniculus
phosphoprotein regulation by de-/phosphorylation performed by cAMP-dependent protein kinase, EC 2.7.11.11 Rattus norvegicus

Purification (Commentary)

Purification (Comment) Organism
native enzyme from skeletal muscle, recombinant enzyme subunit subcomplexes from Sf9 insect cells Oryctolagus cuniculus
recombinant holoenzyme and enzyme subunit subcomplexes from Sf9 insect cells Rattus norvegicus

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
-
 activity of purified native and recombinant enzymes and subunit subcomplexes at different pH Rattus norvegicus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information the enzyme performs autophosphorylation Oryctolagus cuniculus ?
-
 ?
additional information the enzyme performs autophosphorylation Rattus norvegicus ?
-
 ?

Subunits

Subunits Comment Organism
hexadecamer (alphabetagammadelta)4 Rattus norvegicus
More the delta subunit is identical with calmodulin Rattus norvegicus

Synonyms

Synonyms Comment Organism
PhK
-
 Oryctolagus cuniculus
PhK
-
 Rattus norvegicus
Phosphorylase b kinase
-
 Oryctolagus cuniculus
Phosphorylase b kinase
-
 Rattus norvegicus
SkM Phk
-
 Oryctolagus cuniculus
SkM Phk
-
 Rattus norvegicus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
30
-
 autophosphorylation reaction at Oryctolagus cuniculus
30
-
 autophosphorylation reaction at Rattus norvegicus

pH Range

pH Minimum pH Maximum Comment Organism
additional information
-
 activity of purified native and recombinant enzymes and subunit subcomplexes at different pH, the latter show higher activity at pH 6.8, while the native enzyme shows higher activity at pH 8.2 Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
ATP
-
 Oryctolagus cuniculus
ATP
-
 Rattus norvegicus
Calmodulin Ca2+-dependent binding, identical with the delta subunit Oryctolagus cuniculus
Calmodulin Ca2+-dependent binding, identical with the delta subunit Rattus norvegicus