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Tyrosine‐194 of glycogenin undergoes autocatalytic glucosylation but is not essential for catalytic function and activity
Author(s) -
Alonso Miriam D.,
Lomako Joseph,
Lomako Wieslawa M.,
Whelan William J.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80580-6
Subject(s) - autocatalysis , residue (chemistry) , glycosyltransferase , chemistry , biochemistry , tyrosine , glycogen , function (biology) , glycosylation , catalysis , stereochemistry , biology , enzyme , microbiology and biotechnology
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.