Tyrosine-194 of glycogenin undergoes autocatalytic glucosylation but is not essential for catalytic function and activity

Miriam D. Alonso, Joseph Lomako, Wieslawa M. Lomako, William J. Whelan

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

Glycogenin is the protein primer for glycogen synthesis. By autocatalytic transglucosylation from UDPglucose, it creates a malto-octaose chain attached to its Tyr-194. It has been uncertain whether the autocatalysis includes the addition of the first glucose residue to Tyr-194. We now show this to be the case. However, we also demonstrate, contrary to a claim by others, that Tyr-194 is not necessary for the catalytic function and activity of glycogenin.

Original languageEnglish
Pages (from-to)38-42
Number of pages5
JournalFEBS Letters
Volume342
Issue number1
DOIs
StatePublished - Mar 28 1994

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Tyrosine
Glycogen
Glucose
Proteins
glycogenin

Keywords

  • Glycogenin
  • n-Dodecyl β-maltoside
  • Transglucosylation

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Tyrosine-194 of glycogenin undergoes autocatalytic glucosylation but is not essential for catalytic function and activity. / Alonso, Miriam D.; Lomako, Joseph; Lomako, Wieslawa M.; Whelan, William J.

In: FEBS Letters, Vol. 342, No. 1, 28.03.1994, p. 38-42.

Research output: Contribution to journalArticle

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