期刊论文详细信息
FEBS Letters | |
Tyrosine‐194 of glycogenin undergoes autocatalytic glucosylation but is not essential for catalytic function and activity | |
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
【 预 览 】
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RO201912020299353ZK.pdf | 633KB | download |