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Literature summary for 2.7.11.19 extracted from

  • Makeeva, V.F.; Chebotareva, N.A.; Andreeva, I.E.; Livanova, N.B.; Kurganov, B.I.
    Interaction of phosphorylase kinase from rabbit skeletal muscle with flavin adenine dinucleotide (2006), Biochemistry (Moscow), 71, 652-657.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
additional information FAD prevents the formation of the enzyme-glycogen complex in a cooperative manner, but exerts practically no effect on the phosphorylase kinase activity, in the presence of 1 M trimethylamine-N-oxide, FAD has an inhibitory effect on self-association of phosphorylase kinase Oryctolagus cuniculus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information kinetics of phosphorylase kinase-glycogen complex formation Oryctolagus cuniculus

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ required for complex formation Oryctolagus cuniculus
Mg2+ required for complex formation and activity 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 + phosphorylated glycogen phosphorylase b
-
?
additional information Oryctolagus cuniculus interaction of flavin adenine dinucleotide, FAD, with rabbit skeletal muscle phosphorylase kinase, FAD prevents the formation of the enzyme-glycogen complex in a cooperative manner, but exerts practically no effect on the phosphorylase kinase activity, the complex of glycogen metabolism enzymes in protein-glycogen particles may function as a flavin depot in skeletal muscle ?
-
?

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme from skeletal muscle by anion exchange chromatography to homogeneity 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 + phosphorylated glycogen phosphorylase b
-
?
additional information interaction of flavin adenine dinucleotide, FAD, with rabbit skeletal muscle phosphorylase kinase, FAD prevents the formation of the enzyme-glycogen complex in a cooperative manner, but exerts practically no effect on the phosphorylase kinase activity, the complex of glycogen metabolism enzymes in protein-glycogen particles may function as a flavin depot in skeletal muscle Oryctolagus cuniculus ?
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
26
-
assay at Oryctolagus cuniculus

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6.8
-
assay at Oryctolagus cuniculus

Cofactor

Cofactor Comment Organism Structure
ATP
-
Oryctolagus cuniculus