The discovery of glycogenin and the priming mechanism for glycogen biogenesis

Carl SMYTHE, Philip COHEN

    Research output: Contribution to journalArticle

    134 Citations (Scopus)

    Abstract

    The biogenesis of glycogen in skeletal muscle requires a priming mechanism that has recently been elucidated. The first step is catalysed by a protein tyrosine glucosyltransferase and involves the formation of a novel glycosidic linkage, namely the covalent attachment of glucose to a single tyrosine residue (Tyr194) on a priming protein, termed glycogenin. The next stage is the extension of the glucan chain from Tyr194 and involves the sequential addition of up to seven further glucosyl residues. This reaction is brought about autocatalytically by glycogenin itself, which is a Mn2+/Mg2+‐dependent UDP‐Glc‐requiring glucosyltransferase. The glucan primer is elongated by glycogen synthase, but only when glycogenin and glycogen synthase are complexed together. Glycogen synthase dissociates from glycogenin during the synthesis of a glycogen molecule, enabling glycogen molecules to reach their maximum theoretical size. Each mature glycogen β particle in muscle contains one molecule of glycogenin attached covalently, and an average one glycogen synthase catalytic subunit bound non‐covalently. As evidence accumulates that a priming protein may be a fundamental property of polysaccharide synthesis in general, the molecular details of mammalian glycogen biogenesis may serve as a useful model for other systems.

    Original languageEnglish
    Pages (from-to)625-631
    Number of pages7
    JournalEuropean Journal of Biochemistry
    Volume200
    Issue number3
    DOIs
    Publication statusPublished - Sep 1991

    Fingerprint

    Glycogen Synthase
    Glycogen
    Glucosyltransferases
    Glucans
    Molecules
    Tyrosine
    Muscle
    Proteins
    Polysaccharides
    Catalytic Domain
    Skeletal Muscle
    glycogenin
    Glucose
    Muscles

    Cite this

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    abstract = "The biogenesis of glycogen in skeletal muscle requires a priming mechanism that has recently been elucidated. The first step is catalysed by a protein tyrosine glucosyltransferase and involves the formation of a novel glycosidic linkage, namely the covalent attachment of glucose to a single tyrosine residue (Tyr194) on a priming protein, termed glycogenin. The next stage is the extension of the glucan chain from Tyr194 and involves the sequential addition of up to seven further glucosyl residues. This reaction is brought about autocatalytically by glycogenin itself, which is a Mn2+/Mg2+‐dependent UDP‐Glc‐requiring glucosyltransferase. The glucan primer is elongated by glycogen synthase, but only when glycogenin and glycogen synthase are complexed together. Glycogen synthase dissociates from glycogenin during the synthesis of a glycogen molecule, enabling glycogen molecules to reach their maximum theoretical size. Each mature glycogen β particle in muscle contains one molecule of glycogenin attached covalently, and an average one glycogen synthase catalytic subunit bound non‐covalently. As evidence accumulates that a priming protein may be a fundamental property of polysaccharide synthesis in general, the molecular details of mammalian glycogen biogenesis may serve as a useful model for other systems.",
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    The discovery of glycogenin and the priming mechanism for glycogen biogenesis. / SMYTHE, Carl; COHEN, Philip.

    In: European Journal of Biochemistry, Vol. 200, No. 3, 09.1991, p. 625-631.

    Research output: Contribution to journalArticle

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