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

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

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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 language	English
Pages (from-to)	2681-2686
Number of pages	6
Journal	EMBO Journal
Volume	7
Issue number	9
Publication status	Published - 7 Sept 1988

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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 = sep,

day = "7",

language = "English",

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pages = "2681--2686",

journal = "EMBO Journal",

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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

SN - 0261-4189

VL - 7

SP - 2681

EP - 2686

JO - EMBO Journal

JF - EMBO Journal

IS - 9

ER -

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

Abstract

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