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

BRENDA support

Literature summary for 2.7.11.19 extracted from

  • Chan, K.F.J.; Graves, D.J.
    Rabbit skeletal muscle phosphorylase kinase. Catalytic and regulatory properties of the active alpha gamma delta and gamma delta complexes (1982), J. Biol. Chem., 257, 5948-5955.
    View publication on PubMed
Search for more literature for 2.7.11.19

Activating Compound

Activating Compound Comment Organism Structure
1,2-dimethoxyethane activation, 10% v/v, stimulates phosphorylase kinase and alphagammadelta (not gammadelta) subunit complex Oryctolagus cuniculus
Catalytic subunit of cAMP-dependent protein kinase activation of nonactivated enzyme Oryctolagus cuniculus
Catalytic subunit of cAMP-dependent protein kinase or alphagammadelta subunit complex Oryctolagus cuniculus
glycogen activation Oryctolagus cuniculus
glycogen stimulates phosphorylase kinase and alphagammadelta (not gammadelta) subunit complex Oryctolagus cuniculus
heparin activation Oryctolagus cuniculus
heparin stimulates only holoenzyme, not subunit complexes Oryctolagus cuniculus

Inhibitors

Inhibitors Comment Organism Structure
1,2-dimethoxyethane above 10% v/v, stimulates below Oryctolagus cuniculus
ADP gammadelta subunit complex Oryctolagus cuniculus
EGTA alphagammadelta and gammadelta subunit complexes less sensitive than holoenzyme; Ca2+ restores; effect on kinetic parameters Oryctolagus cuniculus
glucose 6-phosphate not (gammadelta subunit complex) Oryctolagus cuniculus
GTP gammadelta subunit complex Oryctolagus cuniculus
Histone VIIS gammadelta subunit complex Oryctolagus cuniculus
ITP not (gammadelta subunit complex) Oryctolagus cuniculus
Mn2+ free Mn2+ Oryctolagus cuniculus
additional information no inhibition by CTP, caffeine, cAMP, cGMP, IMP, glucose 6-phosphate (gammadelta subunit complex); no inhibition by glucose 1-phosphate (gammadelta subunit complex) Oryctolagus cuniculus
UTP weak, gammadelta subunit complex Oryctolagus cuniculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information kinetic properties of subunit complexes at pH 6.8 and 8.5 Oryctolagus cuniculus
0.08
-
 MgATP2- phosphorylase b, activated enzyme Oryctolagus cuniculus
0.094
-
 phosphorylase b pH 8.2, gammadelta subunit complex Oryctolagus cuniculus
0.11
-
 phosphorylase b pH 8.2, alphagammadelta subunit complex Oryctolagus cuniculus
0.22
-
 ATP pH 8.2, nonactivated enzyme Oryctolagus cuniculus
0.25
-
 phosphorylase b pH 8.2, nonactivated enzyme Oryctolagus cuniculus
0.5
-
 ATP pH 8.2, alphagammadelta subunit complex Oryctolagus cuniculus
0.95
-
 ATP pH 8.2, gammadelta subunit complex Oryctolagus cuniculus

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ requirement Oryctolagus cuniculus
Mg2+ 10 mM Oryctolagus cuniculus
Mg2+ major role of Mg2+: cosubstrate in Mg2+-ATP complex Oryctolagus cuniculus
Mn2+ requirement Oryctolagus cuniculus
Mn2+ can substitute for Mg2+ Oryctolagus cuniculus
Mn2+ free Mn2+ inhibits Oryctolagus cuniculus
Mn2+ at equimolar concentration of metal ion and ATP Mn2+ more effective than Mg2+ Oryctolagus cuniculus
Mn2+ optimal at ATP:Mg ratio of 1:1 Oryctolagus cuniculus
phosphate alphagammadelta complex undergoes autophosphorylation: up to 4.2 mol phosphate/mol complex incorporated into alpha subunit Oryctolagus cuniculus
phosphate requirement, phosphate containing enzyme Oryctolagus cuniculus
phosphate gammadelta subunit complex cannot phosphorylate itself but phosphorylates and activates native enzyme, even in the presence of EGTA or protein kinase inhibitor Oryctolagus cuniculus

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Reaction

Reaction Comment Organism Reaction ID
2 ATP + phosphorylase b = 2 ADP + phosphorylase a mechanism Oryctolagus cuniculus
a

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 + alphagammadelta subunit complex autophosphorylation, by incorporation of phosphate into alpha subunit Oryctolagus cuniculus ADP + activated alphagammadelta subunit complex
-
 ?
ATP + phosphorylase b cosubstrate: Mg-ATP complex Oryctolagus cuniculus ADP + phosphorylase a
-
 ?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
91.4
-
 phosphorylase b nonactivated enzyme Oryctolagus cuniculus
99
-
 phosphorylase b alphagammadelta subunit complex Oryctolagus cuniculus
104
-
 phosphorylase b gammadelta subunit complex Oryctolagus cuniculus