Identification and characterization of the Nudix hydrolase from the Archaeon, Methanococcus jannaschii, as a highly specific ADP-ribose pyrophosphatase

被引:54
作者
Sheikh, S
O'Handley, SF
Dunn, CA
Bessman, MJ [1 ]
机构
[1] Johns Hopkins Univ, Dept Biol, Baltimore, MD 21218 USA
[2] Johns Hopkins Univ, McCollum Pratt Inst, Baltimore, MD 21218 USA
关键词
D O I
10.1074/jbc.273.33.20924
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
The MJ1149 gene from the Archaeon, Methanococcus jannaschii, has been cloned and expressed in Escherichia coli, The 19-kDa protein containing the Nudix box, GX(5)EX(7)REUXEEXGU, has been purified and identified as a highly specific enzyme catalyzing the Mg2+-dependent hydrolysis of ADP-ribose according to the equation: ADP-ribose + H2O --> AMP + ribose-5-phosphate. The enzyme retains full activity when heated to 80 degrees C, and the rate of hydrolysis is 15-fold higher at 75 degrees C than at 37 degrees C in keeping with the thermophilicity of the organism. This is the first Nudix hydrolase identified from the Archaea, indicating that the family of enzymes containing the Nudix signature sequence is represented in all three kingdoms.
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页码:20924 / 20928
页数:5
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