Literature summary extracted from

Paudel, H.K.; Carlson, G.M.
Inhibition of the catalytic subunit of phosphorylase kinase by its alpha/beta subunits (1987), J. Biol. Chem., 262, 11912-11915.

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
2.7.11.19	additional information	phosphorylase kinase alpha and beta subunits suppress catalytic activity of gamma subunit in holoenzyme	Oryctolagus cuniculus

Metals/Ions

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

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.7.11.19	Oryctolagus cuniculus	-	new Zealand white	-

Purification (Commentary)

EC Number	Purification (Comment)	Organism
2.7.11.19	isolation of denatured subunits (from nonactivated enzyme)	Oryctolagus cuniculus

Source Tissue

EC Number	Source Tissue	Comment	Organism	Textmining
2.7.11.19	skeletal muscle	-	Oryctolagus cuniculus	-

Substrates and Products (Substrate)

EC Number	Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
2.7.11.19	ATP + phosphorylase b	cosubstrate: Mg-ATP complex	Oryctolagus cuniculus	ADP + phosphorylase a	-	?

Temperature Optimum [°C]

EC Number	Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
2.7.11.19	30	-	assay at	Oryctolagus cuniculus

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Release 2023.1 (January 2023)