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Papers In Press, published online ahead of print August 23, 2004
Department of Biochemistry and Molecular Biology, Saitama University, Saitama, Saitama 338-8570
Corresponding Author: kotake{at}molbiol.saitama-u.ac.jp
UDP-sugars, activated forms of monosaccharides, are synthesized through de novo and salvage pathways and serve as substrates for the synthesis of polysaccharides, glycolipids, and glycoproteins in higher plants. A UDP-sugar pyrophosphorylase, designated PsUSP, was purified about 1,200-fold from pea (Pisum sativum L.) sprouts by conventional chromatography. The apparent molecular mass of the purified PsUSP was 67,000 Da. The enzyme catalyzed the formation of UDP-Glc, UDP-Gal, UDP-glucuronic acid, UDP-L-arabinose, and UDP-xylose from respective monosaccharide 1-phosphates in the presence of UTP as a co-substrate, indicating that the enzyme has broad substrate specificity towards monosaccharide 1-phosphates. Maximum activity of the enzyme occurred at pH 6.5 to 7.5, and at 45°C in the presence of 2 mM Mg2+. The apparent Km values for Glc 1-phosphate and L-arabinose 1-phosphate were 0.34 and 0.96 mM, respectively. PsUSP cDNA was cloned by reverse transcriptase-PCR. PsUSP appears to encode a protein with a molecular mass of 66,040 Da (600 amino acids) and possesses a uridine-binding site which has also been found in a human UDP-N-acetylhexosamine pyrophosphorylase. Phylogenetic analysis revealed that PsUSP can be categorized in a group together with homologues from Arabidopsis and rice, which is distinct from the UDP-Glc and UDP-N-acetylhexosamine pyrophosphorylase groups. Recombinant PsUSP expressed in Escherichia coli catalyzed the formation of UDP-sugars from monosaccharide 1-phosphates and UTP with efficiency similar to that of the native enzyme. These results indicate that the enzyme is a novel type of UDP-sugar pyrophosphorylase, which catalyzes the formation of various UDP-sugars at the end of salvage pathways in higher plants.
J. Biol. Chem, 10.1074/jbc.M408716200
Submitted on July 30, 2004
Revised on August 23, 2004
Accepted on August 23, 2004
UDP-sugar pyrophosphorylase with broad substrate specificity towards various monosaccharide 1-phosphates from pea sprouts
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