| http://purl.uniprot.org/citations/15326166 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15326166 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/15326166 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/15326166 | http://www.w3.org/2000/01/rdf-schema#comment | "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 toward monosaccharide 1-phosphates. Maximum activity of the enzyme occurred at pH 6.5-7.5, and at 45 degrees C in the presence of 2 mm Mg(2+). The apparent K(m) 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."xsd:string |
| http://purl.uniprot.org/citations/15326166 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m408716200"xsd:string |
| http://purl.uniprot.org/citations/15326166 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m408716200"xsd:string |
| http://purl.uniprot.org/citations/15326166 | http://purl.uniprot.org/core/author | "Ishida H."xsd:string |
| http://purl.uniprot.org/citations/15326166 | http://purl.uniprot.org/core/author | "Ishida H."xsd:string |
| http://purl.uniprot.org/citations/15326166 | http://purl.uniprot.org/core/author | "Kaneko S."xsd:string |
| http://purl.uniprot.org/citations/15326166 | http://purl.uniprot.org/core/author | "Kaneko S."xsd:string |
| http://purl.uniprot.org/citations/15326166 | http://purl.uniprot.org/core/author | "Kotake T."xsd:string |
| http://purl.uniprot.org/citations/15326166 | http://purl.uniprot.org/core/author | "Kotake T."xsd:string |
| http://purl.uniprot.org/citations/15326166 | http://purl.uniprot.org/core/author | "Tsumuraya Y."xsd:string |
| http://purl.uniprot.org/citations/15326166 | http://purl.uniprot.org/core/author | "Tsumuraya Y."xsd:string |
| http://purl.uniprot.org/citations/15326166 | http://purl.uniprot.org/core/author | "Hojo S."xsd:string |
| http://purl.uniprot.org/citations/15326166 | http://purl.uniprot.org/core/author | "Hojo S."xsd:string |
| http://purl.uniprot.org/citations/15326166 | http://purl.uniprot.org/core/author | "Yamaguchi D."xsd:string |
| http://purl.uniprot.org/citations/15326166 | http://purl.uniprot.org/core/author | "Yamaguchi D."xsd:string |
| http://purl.uniprot.org/citations/15326166 | http://purl.uniprot.org/core/author | "Ohzono H."xsd:string |
| http://purl.uniprot.org/citations/15326166 | http://purl.uniprot.org/core/author | "Ohzono H."xsd:string |
| http://purl.uniprot.org/citations/15326166 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15326166 | http://purl.uniprot.org/core/date | "2004"xsd:gYear |
| http://purl.uniprot.org/citations/15326166 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/15326166 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
| http://purl.uniprot.org/citations/15326166 | http://purl.uniprot.org/core/pages | "45728-45736"xsd:string |