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

FEBS Letters

Lomako, Wieslawa M.¹  Alonso, Miriam D.¹  Lomako, Joseph¹  Whelan, William J.¹ 

[1] Department of Biochemistry and Molecular Biology, University of Miami School of Medicine (M823), PO Box 016129, Miami, FL 33101, USA

关键词: Glycogenin;    Transglucosylation;    n-Dodecyl β-maltoside;    DBM;    n-dodecyl β-maltoside;   

DOI  :  10.1016/0014-5793(94)80580-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown