Isolation and structural analysis of a peptide containing the novel tyrosyl-glucose linkage in glycogenin.

Carl Smythe, F. Barry Caudwell, Michael A. J. Ferguson, Philip Cohen

    Research output: Contribution to journalArticle

    85 Citations (Scopus)

    Abstract

    The glucosylation site on glycogenin, the protein primer required for de novo glycogen synthesis, has been identified. The glucose is attached at position C1 in a glycosidic linkage with a unique tyrosine, and the sequence surrounding this residue was found to be: His-Leu-Pro-Phe-Ile-Tyr-Asn-Leu-Ser-Ser-Ile-Ser-Ile-Tyr(Glc)-Ser-Tyr-Leu -Pro- Ala-Phe-Lys. The same tyrosine residue is glycosylated whether glycogenin is isolated as a complex with the catalytic subunit of glycogen synthase, or covalently attached to glycogen. The possibility that insulin and growth factors may enhance glycogen synthesis via stimulation of the priming reaction is discussed.

    Original languageEnglish
    Pages (from-to)2681-2686
    Number of pages6
    JournalEMBO Journal
    Volume7
    Issue number9
    Publication statusPublished - 7 Sep 1988

    Cite this

    @article{db770db12809424e9437aa1d1e3e925c,
    title = "Isolation and structural analysis of a peptide containing the novel tyrosyl-glucose linkage in glycogenin.",
    abstract = "The glucosylation site on glycogenin, the protein primer required for de novo glycogen synthesis, has been identified. The glucose is attached at position C1 in a glycosidic linkage with a unique tyrosine, and the sequence surrounding this residue was found to be: His-Leu-Pro-Phe-Ile-Tyr-Asn-Leu-Ser-Ser-Ile-Ser-Ile-Tyr(Glc)-Ser-Tyr-Leu -Pro- Ala-Phe-Lys. The same tyrosine residue is glycosylated whether glycogenin is isolated as a complex with the catalytic subunit of glycogen synthase, or covalently attached to glycogen. The possibility that insulin and growth factors may enhance glycogen synthesis via stimulation of the priming reaction is discussed.",
    author = "Carl Smythe and Caudwell, {F. Barry} and Ferguson, {Michael A. J.} and Philip Cohen",
    year = "1988",
    month = "9",
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    language = "English",
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    pages = "2681--2686",
    journal = "EMBO Journal",
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    }

    Isolation and structural analysis of a peptide containing the novel tyrosyl-glucose linkage in glycogenin. / Smythe, Carl; Caudwell, F. Barry; Ferguson, Michael A. J.; Cohen, Philip.

    In: EMBO Journal, Vol. 7, No. 9, 07.09.1988, p. 2681-2686.

    Research output: Contribution to journalArticle

    TY - JOUR

    T1 - Isolation and structural analysis of a peptide containing the novel tyrosyl-glucose linkage in glycogenin.

    AU - Smythe, Carl

    AU - Caudwell, F. Barry

    AU - Ferguson, Michael A. J.

    AU - Cohen, Philip

    PY - 1988/9/7

    Y1 - 1988/9/7

    N2 - The glucosylation site on glycogenin, the protein primer required for de novo glycogen synthesis, has been identified. The glucose is attached at position C1 in a glycosidic linkage with a unique tyrosine, and the sequence surrounding this residue was found to be: His-Leu-Pro-Phe-Ile-Tyr-Asn-Leu-Ser-Ser-Ile-Ser-Ile-Tyr(Glc)-Ser-Tyr-Leu -Pro- Ala-Phe-Lys. The same tyrosine residue is glycosylated whether glycogenin is isolated as a complex with the catalytic subunit of glycogen synthase, or covalently attached to glycogen. The possibility that insulin and growth factors may enhance glycogen synthesis via stimulation of the priming reaction is discussed.

    AB - The glucosylation site on glycogenin, the protein primer required for de novo glycogen synthesis, has been identified. The glucose is attached at position C1 in a glycosidic linkage with a unique tyrosine, and the sequence surrounding this residue was found to be: His-Leu-Pro-Phe-Ile-Tyr-Asn-Leu-Ser-Ser-Ile-Ser-Ile-Tyr(Glc)-Ser-Tyr-Leu -Pro- Ala-Phe-Lys. The same tyrosine residue is glycosylated whether glycogenin is isolated as a complex with the catalytic subunit of glycogen synthase, or covalently attached to glycogen. The possibility that insulin and growth factors may enhance glycogen synthesis via stimulation of the priming reaction is discussed.

    M3 - Article

    VL - 7

    SP - 2681

    EP - 2686

    JO - EMBO Journal

    JF - EMBO Journal

    SN - 0261-4189

    IS - 9

    ER -