Literature summary for 2.7.11.19 extracted from

Priddy, T.S.; MacDonald, B.A.; Heller, W.T.; Nadeau, O.W.; Trewhella, J.; Carlson, G.M.
Ca2+-induced structural changes in phosphorylase kinase detected by small-angle X-ray scattering (2005), Protein Sci., 14, 1039-1048.

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Metals/Ions

Metals/Ions	Comment	Organism	Structure
Ca2+	activates, binding structure modeling, Ca2+-binding induces structural perturbation of the subunits and promotes redistribution of density throughout the lobes and bridges of the enzyme structure	Oryctolagus cuniculus

Molecular Weight [Da]

Molecular Weight [Da]	Molecular Weight Maximum [Da]	Comment	Organism
1300000	-	-	Oryctolagus cuniculus

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
ATP + glycogen phosphorylase b	Oryctolagus cuniculus	-	ADP + glycogen phosphorylase a	-	?

Organism

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

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 + glycogen phosphorylase b	-	Oryctolagus cuniculus	ADP + glycogen phosphorylase a	-	?

Subunits

Subunits	Comment	Organism
hexadecamer	(alphabetagammadelta)4	Oryctolagus cuniculus
More	calmodulin is identical with the delta subunit, X-ray light-scattering structure modeling of unactivated enzyme or enzyme after structural changes induced by Ca2+-binding, structure analysis, overview	Oryctolagus cuniculus

Synonyms

Synonyms	Comment	Organism
PhK	-	Oryctolagus cuniculus

Cofactor

Cofactor	Comment	Organism	Structure
ATP	-	Oryctolagus cuniculus
Calmodulin	identical with the delta subunit	Oryctolagus cuniculus

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Release 2023.1 (January 2023)