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J Biol Chem, Vol. 273, Issue 33, 20924-20928, August 14, 1998

Identification and Characterization of the Nudix Hydrolase from the Archaeon, Methanococcus jannaschii, as a Highly Specific ADP-ribose Pyrophosphatase

Saifuddin Sheikh, Suzanne F. O'Handley, Christopher A. Dunn, and Maurice J. Bessman

From the Department of Biology and the McCollum-Pratt Institute, The Johns Hopkins University, Baltimore, Maryland 21218

The MJ1149 gene from the Archaeon, Methanococcus jannaschii, has been cloned and expressed in Escherichia coli. The 19-kDa protein containing the Nudix box, GX5EX7REUXEEXGU, 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 right-arrow AMP + ribose-5-phosphate. The enzyme retains full activity when heated to 80 °C, and the rate of hydrolysis is 15-fold higher at 75 °C than at 37 °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.

Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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