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Literature summary for 2.7.11.19 extracted from

  • Reimann, E.M.; Titani, K.; Ericsson, L.H.; Wade, R.D.; Fischer, E.H.; Walsh, K.A.
    Homology of the gamma subunit of phosphorylase b kinase with cAMP-dependent protein kinase (1984), Biochemistry, 23, 4185-4192.
    View publication on PubMed
Search for more literature for 2.7.11.19

Metals/Ions

Metals/Ions Comment Organism Structure
Calcium dependent on Oryctolagus cuniculus
Mg2+ requirement Oryctolagus cuniculus
Mg2+ major role of Mg2+: cosubstrate in Mg2+-ATP complex Oryctolagus cuniculus
phosphate requirement, phosphate containing enzyme Oryctolagus cuniculus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
44673
-
 x * 44673, calculation from amino acid sequence Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-
Oryctolagus cuniculus P00518
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Oryctolagus cuniculus

Source Tissue

Source Tissue Comment Organism Textmining
skeletal muscle
-
 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
-
 ?

Subunits

Subunits Comment Organism
? x * 44673, calculation from amino acid sequence Oryctolagus cuniculus
More gamma subunit Oryctolagus cuniculus
More homology with catalytic subunit of cAMP dependent protein kinase Oryctolagus cuniculus

Synonyms

Synonyms Comment Organism
phosphorylase B kinase gamma catalytic chain, skeletal muscle isoform
-
 Oryctolagus cuniculus