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M205207200v1
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Papers In Press, published online ahead of print October 23, 2002
J. Biol. Chem, 10.1074/jbc.M205207200
Submitted on May 28, 2002
Revised on October 23, 2002
Accepted on October 23, 2002

Cloning and characterization of the first member of the Nudix family from Arabidopsis thaliana

Marta Dobrzanska, Blanka Szurmak, Aleksandra Wyslouch-Cieszynska, and Elzbieta Kraszewska

Department of Plant Biochemistry, Polish Academy of Sciences, Warsaw 02-106

Corresponding Author: martad{at}ibb.waw.pl

Summary The sequence motif commonly called a Nudix box, represented by (GX5EX7REVXEEXGU) is the marker of a widely distributed family of enzymes that catalyze the hydrolysis of a variety of nucleoside diphosphate derivatives. Here we describe the cloning and characterization of an Arabidopsis thaliana cDNA encoding a Nudix hydrolase that degrades NADH. The deduced amino acid sequence of AtNUDT1 contains 147 amino acids. The recombinant AtNUDT1 was expressed in E. coli and purified. In the presence of Mn2+ and the optimal pH of 7. 0, the recombinant AtNUDT1 catalyzed the hydrolysis of NADH with a Km value of 0. 36 mM. A Vmax of 12. 7 units mg –1 for NADH was determined. The recombinant AtNUDT1 migrated as a dimer on a gel filtration column. Biochemical analysis of recombinant AtNUDT1 indicated that the first characterized member of the Nudix family from Arabidopsis thaliana is a NADH pyrophosphatase.


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