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Literature summary for 2.4.1.1 extracted from

  • Chebotareva, N.A.; Meremyanin, A.V.; Makeeva, V.F.; Eronina, T.B.; Kurganov, B.I.
    Glycogen phosphorylase b and phosphorylase kinase binding to glycogen under molecular crowding conditions. Inhibitory effect of FAD (2009), Biochemistry, 74, 562-568.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
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glycogen phosphorylase b
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Source Tissue

Source Tissue Comment Organism Textmining
skeletal muscle
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Oryctolagus cuniculus
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General Information

General Information Comment Organism
physiological function molecular crowding by 1 M trimethylamine N-oxide stimulates phosphorylase b and phosphorylase kinase combined binding on glycogen particles. Phosphorylase kinase binding to glycogen particles containing adsorbed phosphorylase shows a two-stage character. At the initial stage, limited size particles with hydrodynamic radius of about 220 nm are formed, whereas the second stage is accompanied by linear growth of hydrodynamic radius. Flavin adenine dinucleotide selectively inhibits phosphorylase kinase binding at the second stage, while its binding in the second stage does not involve phosphorylase b Oryctolagus cuniculus