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Literature summary for 3.5.3.15 extracted from

  • Eronina, T.B.; Livanova, N.B.; Chebotareva, N.A.; Kurganov, B.I.; Luo, S.; Graves, D.J.
    Deimination of glycogen phosphorylase b by peptidylarginine deiminase. Influence on the kinetical characteristics and dimer-tetramer transition (1996), Biochimie, 78, 253-258.
    View publication on PubMed
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
glycogen phosphorylase b + H2O Oryctolagus cuniculus specific deimination by peptidylarginine deiminase has a pronounced effect on the binding of some allosteric effectors with the enzyme and hampers the association of phosphorylase b dimers into tetramers in the presence of AMP ?
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 ?

Organism

Organism UniProt Comment Textmining
Oryctolagus cuniculus
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Source Tissue

Source Tissue Comment Organism Textmining
muscle skeletal muscle Oryctolagus cuniculus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glycogen phosphorylase b + H2O specific deimination by peptidylarginine deiminase has a pronounced effect on the binding of some allosteric effectors with the enzyme and hampers the association of phosphorylase b dimers into tetramers in the presence of AMP Oryctolagus cuniculus ? + NH3
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 ?
glycogen phosphorylase b + H2O specific deimination by peptidylarginine deiminase has a pronounced effect on the binding of some allosteric effectors with the enzyme and hampers the association of phosphorylase b dimers into tetramers in the presence of AMP Oryctolagus cuniculus ?
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 ?