The biosynthesis of trehalose phosphate. J Biol Chem 231: 259-275

Journal of Biological Chemistry (Impact Factor: 4.57). 04/1958; 231(1):259-75.
Source: PubMed
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    • "TPS (EC is encoded by the otsA gene (locus XAC3211) and catalyses the transfer of glucose from UDP-glucose to glucose-6-phosphate, forming T6P, which is then dephosphorylated to release free trehalose by TPP, encoded by the otsB gene (Xcc locus XAC3209) (Cabib and Leloir, 1958). In the treY–treZ pathway, (1→4)-α-d- glucan 1-α-d-glucosylmutase (EC changes the glycosidic bond in terminal maltosyl moieties of maltodextrins from an α-(1–4) to an α,α-(1-1) configuration, and then the resulting trehalosyl moiety is released as free trehalose by 4-α-d-[(1→4)-α-d-glucano]trehalose trehalohydrolase (EC "
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    ABSTRACT: Xanthomonas citri subsp. citri (Xcc) is a bacterial pathogen that causes citrus canker in susceptible Citrus spp. The Xcc genome contains genes encoding enzymes from three separate pathways of trehalose biosynthesis. Expression of genes encoding trehalose-6-phosphate synthase (otsA) and trehalose phosphatase (otsB) was highly induced during canker development, suggesting that the two-step pathway of trehalose biosynthesis via trehalose-6-phosphate has a function in pathogenesis. This pathway was eliminated from the bacterium by deletion of the otsA gene. The resulting XccΔotsA mutant produced less trehalose than the wild-type strain, was less resistant to salt and oxidative stresses, and was less able to colonize plant tissues. Gene expression and proteomic analyses of infected leaves showed that infection with XccΔotsA triggered only weak defence responses in the plant compared with infection with Xcc, and had less impact on the host plant's metabolism than the wild-type strain. These results suggested that trehalose of bacterial origin, synthesized via the otsA-otsB pathway, in Xcc, plays a role in modifying the host plant's metabolism to its own advantage but is also perceived by the plant as a sign of pathogen attack. Thus, trehalose biosynthesis has both positive and negative consequences for Xcc. On the one hand, it enables this bacterial pathogen to survive in the inhospitable environment of the leaf surface before infection and exploit the host plant's resources after infection, but on the other hand, it is a tell-tale sign of the pathogen's presence that triggers the plant to defend itself against infection. © The Author 2015. Published by Oxford University Press on behalf of the Society for Experimental Biology.
    Journal of Experimental Botany 03/2015; 66(9). DOI:10.1093/jxb/erv095 · 5.53 Impact Factor
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    • "The most common pathway to produce trehalose involves two enzymes : trehalose - 6 - phosphate synthase ( TPS ) , which catalyzes the synthesis of trehalose - 6 - phos - phate ( T6P ) from glucose - 6 - phosphate ( G6P ) and UDP - glucose ( UDPG ) , and trehalose - 6 - phosphate phosphatase ( TPP ) , which dephosphorylates T6P to trehalose ( Cabib and Leloir 1958 ; Kaasen et al . 1992 ; Lunn et al . "
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    ABSTRACT: Establishing the function of trehalose in yeast cells has led us, over the years, through a long path-from simple energy storage carbohydrate, then a stabilizer and protector of membranes and proteins, through a safety valve against damage caused by oxygen radicals, up to regulator of the glycolytic path. In addition, trehalose biosynthesis has been proposed as a target for novel drugs against several pathogens. Since this pathway is entirely absent in mammalian cells and makes use of highly specific enzymes, trehalose metabolism might be an interesting target for the development of novel therapies. In this review, we want to address some recent points investigated about trehalose metabolism in Saccharomyces cerevisiae, focusing mainly on the mechanism by which this simple disaccharide protects against stress and on the enzymes involved in its synthesis and breakdown. We believe that these concepts are of great importance for medical and biotechnological applications.
    Current Genetics 09/2014; 61(3). DOI:10.1007/s00294-014-0450-1 · 2.68 Impact Factor
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    • "In insects, the blood sugar is trehalose instead of glucose; therefore, the synthesis and utilization of trehalose is unique to insect energy metabolism compared with other animals [50]. Trehalose-6-phosphate synthase (TPS) is the crucial enzyme for the biosynthesis of trehalose, and catalyzes the formation of trehalose-6-phosphate from uridine diphosphate glucose and glucose-6-phosphate [51]. Apart from the synthesizing trehalose in insects, TPS was also reported to be an important enzyme for insect development. "
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    ABSTRACT: The oriental fruit fly, Bactrocera dorsalis, is a destructive pest in tropical and subtropical areas. In this study, we performed transcriptome-wide analysis of the fat body of B. dorsalis and obtained more than 59 million sequencing reads, which were assembled into 27,787 unigenes with an average length of 591 bp. Among them, 17,442 (62.8%) unigenes matched known proteins in the NCBI database. The assembled sequences were further annotated with gene ontology, cluster of orthologous group terms, and Kyoto encyclopedia of genes and genomes. In depth analysis was performed to identify genes putatively involved in immunity, detoxification, and energy metabolism. Many new genes were identified including serpins, peptidoglycan recognition proteins and defensins, which were potentially linked to immune defense. Many detoxification genes were identified, including cytochrome P450s, glutathione S-transferases and ATP-binding cassette (ABC) transporters. Many new transcripts possibly involved in energy metabolism, including fatty acid desaturases, lipases, alpha amylases, and trehalose-6-phosphate synthases, were identified. Moreover, we randomly selected some genes to examine their expression patterns in different tissues by quantitative real-time PCR, which indicated that some genes exhibited fat body-specific expression in B. dorsalis. The identification of a numerous transcripts in the fat body of B. dorsalis laid the foundation for future studies on the functions of these genes.
    PLoS ONE 04/2014; 9(4):e94470. DOI:10.1371/journal.pone.0094470 · 3.23 Impact Factor
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