Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.7.11.19 extracted from

  • Priddy, T.S.; Price, E.S.; Johnson, C.K.; Carlson, G.M.
    Single molecule analyses of the conformational substrates of calmodulin bound to the phosphorylase kinase complex (2007), Protein Sci., 16, 1017-1023.
    View publication on PubMedView publication on EuropePMC

Activating Compound

Activating Compound Comment Organism Structure
Calmodulin influences the conformational substrates of the subunits, overview Oryctolagus cuniculus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activates, the four integral delta subunits of the phosphorylase kinase complex are identical to calmodulin and confer Ca2+ sensitivity to the enzyme, but bind independently of Ca2+, Ca2+ influences the conformational substrates of the subunits, overview Oryctolagus cuniculus
Mg2+
-
Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
New Zealand white rabbits
-

Source Tissue

Source Tissue Comment Organism Textmining
psoas
-
Oryctolagus cuniculus
-

Subunits

Subunits Comment Organism
More conformational substrates of PhK subunit bound or unbound to calmodulin and Ca2+, overview Oryctolagus cuniculus

Synonyms

Synonyms Comment Organism
PhK
-
Oryctolagus cuniculus

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
22
-
assay at room temperature Oryctolagus cuniculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.8 7 assay at Oryctolagus cuniculus

Cofactor

Cofactor Comment Organism Structure
ATP
-
Oryctolagus cuniculus