Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: EC:2.4.1.112 (EC 2.4.1.112)
 4 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

UDP-glucose: protein transglucosylase (UPTG, EC 2.4.1.112) catalyzes the first step of protein-bound alpha-glucan synthesis in potato tuber and developing maize endosperm. The presence of a non-dialyzable, heat labile protein responsible for low levels of UPTG activity in developing maize endosperm was investigated. UPTG activity in 5-day old maize seedlings and potato tuber solubilized preparations was also reduced by the endosperm preparation. FPLC-Mono Q column chromatography of developing maize endosperm was effective in separating the inhibitor protein (IP) from UPTG. After gel filtration on Superose 12, IP yielded a major polypeptide of about 80 kDa on SDS-PAGE. IP was purified by gel filtration on Superose 12 and preparative SDS-PAGE, and specific antibodies were prepared. Polyclonal antibodies reacted specifically with an 80 kDa polypeptide of developing maize endosperm on Western blot. They also recognized a similar band in 5-day old maize seedlings, but not in potato tubers. The identification of a factor that regulates the level of UPTG activity in developing maize endosperm may help to elucidate the functional role of the enzyme in the initiation of starch synthesis during seed development.
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PMID:Inhibition of UDP-glucose: protein transglucosylase by a maize endosperm protein factor. 883 94

UDP-Glc:protein transglucosylase (UPTG) (EC 2.4.1.112) is an autocatalytic glycosyl-transferase previously postulated as a protein that primes starch biosynthesis. Polyclonal antibodies raised against UPTG purified from potato (Solanum tuberosum L.) tubers were used to screen a potato swelling stolon tip cDNA expression library. The isolation, cloning and sequencing of two cDNAs corresponding to UPTG are described. Recombinant UPTG was labelled after incubation with UDP-[(14)C]-Glc and Mn(2+), indicating that it was enzymatically active. It was determined that purified as well as recombinant UPTG can be reversibly glycosylated by UDP-Glc, UDP-Xyl or UDP-Gal. RNA hybridization studies and western blot analysis indicate that UPTG mRNA and protein are expressed in all potato tissues. Databank searches revealed a high degree of identity between UPTG and several plant sequences that encode for proteins with apparent localization at the cytoplasmic face of the Golgi apparatus and at plasmodesmata. The biochemical properties of UPTG and the apparent lack of a signal peptide that could allow its entrance into plastids argue against the postulated role of UPTG in starch synthesis and point towards a possible role of the protein in the synthesis of cell wall polysaccharides.
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PMID:Molecular cloning and characterization of the enzyme UDP-glucose: protein transglucosylase from potatodaggerdaggerThis paper is specially dedicated to the memory of Dr Juana S. Tandecarz, deceased on December 10, 1996. 1058 Feb 81

Many plant autocatalytic glycosyltransferases are implicated in plant polysaccharide biosynthesis. Cloning of cDNAs encoding potato (Solanum tuberosum L.) UDP-Glc:protein transglucosylase (UPTG, EC 2.4.1.112) and expression of the cDNA clone E11 in Escherichia coli have been previously reported. Here, we studied the functional expression of a second cDNA of the enzyme (E2 clone). Northern blots analysis, with specific cDNA probes for the two UPTG isoforms, showed a differential expression pattern of mRNA levels in different potato tissues. Moreover, both UPTG recombinant enzymes showed different kinetic parameters. The recombinant protein encoded by E2 clone has an apparent Imax for UDP-Xyl and UDP-Gal, significantly higher than for UDP-Glc. The Km values for UDP-Glc were 0.45-0.71 microM and the values for UDP-Xyl and UDP-Gal were slightly higher than that of the UDP-Glc (1.2-2.71 microM) for both UPTG recombinant enzymes. The present study revealed further evidence for the proposed role of UPTG in the synthesis of cell wall polysaccharide. It was found a correlation between UPTG transcript levels and the growing state of the tissues in which there was an active synthesis of cell wall components. Southern blot analysis indicates that at least three genes encoding UPTG are present in potato genome. Phylogenetic analysis of both UPTG recombinant proteins showed that they are members of the RGP subfamilies from dicots.
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PMID:Characterization of UDP-glucose:protein transglucosylase genes from potato. 1367 61

Potato (Solanum tuberosum L.) tuber UDP-glucose:protein transglucosylase (UPTG) (EC 2.4.1.112) is involved in the first of a two-step mechanism proposed for protein-bound alpha-glucan synthesis by catalyzing the covalent attachment of a single glucose residue to an acceptor protein. The resulting glucosylated 38-kilodalton polypeptide would then serve as a primer for enzymic glucan chain elongation during the second step. In the present report, we describe the fast protein liquid chromatography purification of UPTG from a membrane pellet of potato tuber. An apparently close association of UPTG, phosphorylase, and starch synthase was observed under native conditions during different purification steps. Enrichment of a 38-kilodalton polypeptide was found throughout enzyme purification. It is now shown that the purified UPTG, with an apparent molecular mass of 38 kilodaltons, undergoes self-glucosylation in a UDP-glucose- and Mn(2+)-dependent reaction. Therefore, it is concluded that UPTG is the enzyme and at the same time the priming protein required for the biogenesis of protein-bound alpha-glucan in potato tuber.
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PMID:Potato Tuber UDP-Glucose:Protein Transglucosylase Catalyzes Its Own Glucosylation. 1666 42