Substrate specificity of the autocatalytic protein that primes glycogen synthesis

Joseph Lomako, Wieslawa M. Lomako, William J. Whelan

Research output: Contribution to journalArticlepeer-review

29 Scopus citations


The autocatalytic protein that primes muscle-glycogen synthesis, and which glucosylates itself from UDPglucose, is inhibited by maltose. Investigation of the reason for the inhibition led to the finding that the protein will glucosylate substrates other than itself. p-Nitrophenyl αglucoside, αmaltoside, αmaltotrioside and αmaltotetraoside each inhibit self-glucosylation of the protein by acting as alternative acceptor substrates. The αmaltoside is the best acceptor. The αmaltohexaoside did not act as an acceptor but was an effective inhibitor. These findings help to explain the self-limiting nature of the autocatalytic extension of the maltosaccharide chain of the protein and suggest that protein self-glucosylation may be an intennolecular event. They may also point to the mechanism by which the autocatalytic protein is initially glycosylated.

Original languageEnglish (US)
Pages (from-to)13-16
Number of pages4
JournalFEBS letters
Issue number1
StatePublished - May 7 1990


  • Glycogen biogenesis
  • Glycogenin
  • Self-glucosylating protein

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology


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