TYROSINE-194 OF GLYCOGENIN UNDERGOES AUTOCATALYTIC GLUCOSYLATION BUT IS NOT ESSENTIAL FOR CATALYTIC FUNCTION AND ACTIVITY

被引：26

作者：

ALONSO, MD ^{[1
]}

LOMAKO, J ^{[1
]}

LOMAKO, WM ^{[1
]}

WHELAN, WJ ^{[1
]}

机构：

[1] UNIV MIAMI,SCH MED M823,DEPT BIOCHEM & MOLEC BIOL,MIAMI,FL 33101

来源：

FEBS LETTERS | 1994年 / 342卷 / 01期

关键词：

GLYCOGENIN; TRANSGLUCOSYLATION; N-DODECYL BETA-MALTOSIDE;

D O I：

10.1016/0014-5793(94)80580-6

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

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.

引用

页码：38 / 42

页数：5

共 13 条

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