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

BRENDA support

Literature summary for 2.7.11.19 extracted from

  • Carlson, G.M.; Bechtel, P.J.; Graves, D.J.
    Chemical and regulatory properties of phosphorylase kinase and cyclic AMP-dependent protein kinase (1979), Adv. Enzymol. Relat. Areas Mol. Biol., 50, 41-115.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
Catalytic subunit of cAMP-dependent protein kinase activation of nonactivated enzyme Mus musculus
Catalytic subunit of cAMP-dependent protein kinase activation of nonactivated enzyme Oryctolagus cuniculus
Catalytic subunit of cAMP-dependent protein kinase activation of nonactivated enzyme Calliphoridae
Catalytic subunit of cAMP-dependent protein kinase activation of nonactivated enzyme Squalus acanthias
glycogen activation Mus musculus
glycogen activation Oryctolagus cuniculus
glycogen activation Calliphoridae
glycogen activation Squalus acanthias
heparin activation Mus musculus
heparin activation Oryctolagus cuniculus
heparin activation Calliphoridae
heparin activation Squalus acanthias
heparin pH-dependent Mus musculus
heparin pH-dependent Oryctolagus cuniculus
heparin pH-dependent Calliphoridae
heparin pH-dependent Squalus acanthias
additional information autophosphorylation Mus musculus
additional information autophosphorylation Oryctolagus cuniculus
additional information autophosphorylation Calliphoridae
additional information autophosphorylation Squalus acanthias
additional information phosphorylation by protein kinases Mus musculus
additional information phosphorylation by protein kinases Oryctolagus cuniculus
additional information phosphorylation by protein kinases Calliphoridae
additional information phosphorylation by protein kinases Squalus acanthias
additional information the nonactivated enzyme is activated either by limited proteolysis Mus musculus
additional information the nonactivated enzyme is activated either by limited proteolysis Oryctolagus cuniculus
additional information the nonactivated enzyme is activated either by limited proteolysis Calliphoridae
additional information the nonactivated enzyme is activated either by limited proteolysis Squalus acanthias
Proteases
-
Mus musculus
Proteases
-
Oryctolagus cuniculus
Proteases
-
Calliphoridae
Proteases
-
Squalus acanthias
Trypsin proteolytic activation of nonactivated enzyme Mus musculus
Trypsin proteolytic activation of nonactivated enzyme Oryctolagus cuniculus
Trypsin proteolytic activation of nonactivated enzyme Calliphoridae
Trypsin proteolytic activation of nonactivated enzyme Squalus acanthias
Trypsin strong, by limited proteolysis of alpha and beta subunits (not gamma) Mus musculus
Trypsin strong, by limited proteolysis of alpha and beta subunits (not gamma) Oryctolagus cuniculus
Trypsin strong, by limited proteolysis of alpha and beta subunits (not gamma) Calliphoridae
Trypsin strong, by limited proteolysis of alpha and beta subunits (not gamma) Squalus acanthias
Trypsin strong, by limited proteolysis of alpha and beta subunits Mus musculus
Trypsin strong, by limited proteolysis of alpha and beta subunits Oryctolagus cuniculus
Trypsin strong, by limited proteolysis of alpha and beta subunits Calliphoridae
Trypsin strong, by limited proteolysis of alpha and beta subunits Squalus acanthias

General Stability

General Stability Organism
Rabbit muscle enzyme is subject to pressure denaturation leading to the formation of polydisperse aggregates Oryctolagus cuniculus

Inhibitors

Inhibitors Comment Organism Structure
DTNB
-
Calliphoridae
DTNB
-
Mus musculus
DTNB
-
Oryctolagus cuniculus
DTNB
-
Squalus acanthias
glucose 6-phosphate
-
Calliphoridae
glucose 6-phosphate
-
Mus musculus
glucose 6-phosphate
-
Oryctolagus cuniculus
glucose 6-phosphate
-
Squalus acanthias
KCl
-
Calliphoridae
KCl
-
Mus musculus
KCl
-
Squalus acanthias
additional information no inhibition by glucose 1-phosphate (gammadelta subunit complex); no inhibition by UDPglucose Calliphoridae
additional information no inhibition by glucose 1-phosphate (gammadelta subunit complex); no inhibition by UDPglucose Mus musculus
additional information no inhibition by glucose 1-phosphate (gammadelta subunit complex); no inhibition by UDPglucose Oryctolagus cuniculus
additional information no inhibition by glucose 1-phosphate (gammadelta subunit complex); no inhibition by UDPglucose Squalus acanthias
Polyaspartic acid pH 8.2 Calliphoridae
Polyaspartic acid pH 8.2 Mus musculus
Polyaspartic acid pH 8.2 Oryctolagus cuniculus
Polyaspartic acid pH 8.2 Squalus acanthias
protamine pH 8.2 Calliphoridae
protamine pH 8.2 Mus musculus
protamine pH 8.2 Oryctolagus cuniculus
protamine pH 8.2 Squalus acanthias

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information pH-dependence of kinetic parameters Mus musculus
additional information
-
additional information pH-dependence of kinetic parameters Oryctolagus cuniculus
additional information
-
additional information pH-dependence of kinetic parameters Calliphoridae
additional information
-
additional information pH-dependence of kinetic parameters Squalus acanthias
additional information
-
additional information kinetic properties, overview Mus musculus
additional information
-
additional information kinetic properties, overview Oryctolagus cuniculus
additional information
-
additional information kinetic properties, overview Calliphoridae
additional information
-
additional information kinetic properties, overview Squalus acanthias
additional information
-
additional information kinetic data for phosphorylase b Mus musculus
additional information
-
additional information kinetic data for phosphorylase b Oryctolagus cuniculus
additional information
-
additional information kinetic data for phosphorylase b Calliphoridae
additional information
-
additional information kinetic data for phosphorylase b Squalus acanthias

Localization

Localization Comment Organism GeneOntology No. Textmining
sarcoplasmic reticulum
-
Mus musculus 16529
-
sarcoplasmic reticulum
-
Oryctolagus cuniculus 16529
-
sarcoplasmic reticulum
-
Calliphoridae 16529
-
sarcoplasmic reticulum
-
Squalus acanthias 16529
-

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+
-
Oryctolagus cuniculus
Ca2+ requirement Mus musculus
Ca2+ requirement Calliphoridae
Ca2+ requirement Squalus acanthias
Li+ activation Mus musculus
Li+ activation Oryctolagus cuniculus
Li+ activation Calliphoridae
Li+ activation Squalus acanthias
Li+ LiBr Mus musculus
Li+ LiBr Oryctolagus cuniculus
Li+ LiBr Calliphoridae
Li+ LiBr Squalus acanthias
Mg2+ requirement Mus musculus
Mg2+ requirement Oryctolagus cuniculus
Mg2+ requirement Calliphoridae
Mg2+ requirement Squalus acanthias
Mg2+ major role of Mg2+: cosubstrate in Mg2+-ATP complex Mus musculus
Mg2+ major role of Mg2+: cosubstrate in Mg2+-ATP complex Oryctolagus cuniculus
Mg2+ major role of Mg2+: cosubstrate in Mg2+-ATP complex Calliphoridae
Mg2+ major role of Mg2+: cosubstrate in Mg2+-ATP complex Squalus acanthias
phosphate requirement, phosphate containing enzyme Mus musculus
phosphate requirement, phosphate containing enzyme Oryctolagus cuniculus
phosphate requirement, phosphate containing enzyme Calliphoridae
phosphate requirement, phosphate containing enzyme Squalus acanthias

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
additional information
-
amino acid composition Mus musculus
additional information
-
amino acid composition Oryctolagus cuniculus
additional information
-
amino acid composition Calliphoridae
additional information
-
amino acid composition Squalus acanthias
1330000
-
analytical ultracentrifugation Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Calliphoridae
-
blowfly
-
Mus musculus
-
-
-
Oryctolagus cuniculus
-
-
-
Squalus acanthias
-
-
-

Purification (Commentary)

Purification (Comment) Organism
overview Oryctolagus cuniculus

Source Tissue

Source Tissue Comment Organism Textmining
cardiac muscle
-
Oryctolagus cuniculus
-
cardiac muscle
-
Squalus acanthias
-
flight muscle
-
Calliphoridae
-
liver
-
Oryctolagus cuniculus
-
liver
-
Squalus acanthias
-
additional information isozyme distribution in different tissues Mus musculus
-
additional information isozyme distribution in different tissues Oryctolagus cuniculus
-
additional information isozyme distribution in different tissues Calliphoridae
-
additional information isozyme distribution in different tissues Squalus acanthias
-
skeletal muscle
-
Mus musculus
-
skeletal muscle
-
Oryctolagus cuniculus
-
skeletal muscle
-
Squalus acanthias
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + myosin light chain kinase rabbit Oryctolagus cuniculus ?
-
?
ATP + phosphorylase b cosubstrate: Mg-ATP complex Mus musculus ADP + phosphorylase a
-
?
ATP + phosphorylase b cosubstrate: Mg-ATP complex Oryctolagus cuniculus ADP + phosphorylase a
-
?
ATP + phosphorylase b cosubstrate: Mg-ATP complex Calliphoridae ADP + phosphorylase a
-
?
ATP + phosphorylase b cosubstrate: Mg-ATP complex Squalus acanthias ADP + phosphorylase a
-
?
ATP + synthetic peptides derived from phosphorylase b overview Mus musculus ?
-
?
ATP + synthetic peptides derived from phosphorylase b overview Oryctolagus cuniculus ?
-
?
ATP + synthetic peptides derived from phosphorylase b overview Calliphoridae ?
-
?
ATP + synthetic peptides derived from phosphorylase b overview Squalus acanthias ?
-
?

Subunits

Subunits Comment Organism
More spatial arrangement of subunits Mus musculus
More spatial arrangement of subunits Oryctolagus cuniculus
More spatial arrangement of subunits Squalus acanthias

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
-
Mus musculus
additional information
-
-
Calliphoridae
additional information
-
-
Squalus acanthias
additional information
-
pI: 5.77 (nonactivated rabbit enzyme) Oryctolagus cuniculus