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

BRENDA support

Literature summary for 2.7.11.19 extracted from

  • Cheng, A.; Fitzgerald, T.J.; Carlson, G.M.
    Adenosine 5-diphosphate as an allosteric effector of phosphorylase kinase from rabbit skeletal muscle (1985), J. Biol. Chem., 260, 2535-2542.
    View publication on PubMed
Search for more literature for 2.7.11.19

Activating Compound

Activating Compound Comment Organism Structure
adenosine 3'-phosphate 5'-phosphosulfate activation, can replace ADP to some extent Oryctolagus cuniculus
adenosine 5'-phosphosulfate activation, can replace ADP to some extent Oryctolagus cuniculus
additional information no activation by g adenine, adenosine, 5'-AMP, 2',5'-ADP, 3',5'-ADP, adenosine 2':3'cyclicphosphate 5'-monophosphate, alpha,beta-methylene-ADP, adenosine 2'-phosphate 5'-phosphosulfate, adenosine 5'-diphosphoglucose, adenosine 5'-diphosphoribose, ADP-3'-diphosphate, adenylylimidodiphosphate, diadenosine diphosphate Oryctolagus cuniculus

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
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 + phosphorylase b cosubstrate: Mg-ATP complex Oryctolagus cuniculus ADP + phosphorylase a
-
 ?

Cofactor

Cofactor Comment Organism Structure
2'-deoxy-ADP activation, can replace ADP Oryctolagus cuniculus
ADP kinetics, 8 binding sites per hexadecamer Oryctolagus cuniculus
ADP allosteric effector Oryctolagus cuniculus