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Literature summary for 2.7.11.19 extracted from

  • Dasgupta, M.; Blumenthal, D.K.
    Characterization of the regulatory domain of the gamma-subunit of phosphorylase kinase. The two noncontiguous calmodulin-binding subdomains are also autoinhibitory (1995), J. Biol. Chem., 270, 22283-22289.
    View publication on PubMed
Search for more literature for 2.7.11.19

Inhibitors

Inhibitors Comment Organism Structure
additional information gamma subunit with autoinhibitory domains; regions of the gamma-subunit represented by PhK5 and PhK13 work in concert as regulatory subdomains that transduce Ca2+-induced conformational changes in the delta-subunit to the catalytic gamma-subunit through a pseudosubstrate autoinhibitory mechanism Oryctolagus cuniculus
Synthetic peptide PhK13 derived from gamma subunit region, residues 302-326; kinetic; synergistic with PhK5 Oryctolagus cuniculus
Synthetic peptide PhK5 derived from gamma subunit region, residues 342-366; kinetic; synergistic with PhK13 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
phosphate requirement, phosphate containing enzyme Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
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-
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Oryctolagus cuniculus P00518
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-

Source Tissue

Source Tissue Comment Organism Textmining
skeletal muscle
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 Oryctolagus cuniculus
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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
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 ?

Synonyms

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

Temperature Optimum [°C]

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