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evolution
Arthrobacter strain A3 has only two trehalose synthesis pathways (OtsA/B and TreS), while other Arthrobacter spp. have three
evolution
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Adineta vaga likely has acquired its trehalose biosynthesis and hydrolysis genes by horizontal gene transfers. The four trehalose-6-phosphate synthase TPS copies of Adineta vaga appear more closely related to plant and fungi proteins, as well as to some protists, whereas the seven TRE copies of the gene encoding trehalase fall in bacterial clades
evolution
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Arabidopsis thaliana has 11 TPS or TPS-like proteins, which belong to two distinct clades: class I (AtTPS1-AtTPS4) and class II (AtTPS5-AtTPS11)
evolution
the enzyme belongs to the glucosyltransferase-GTB-type superfamily
evolution
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Arthrobacter strain A3 has only two trehalose synthesis pathways (OtsA/B and TreS), while other Arthrobacter spp. have three
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malfunction
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DELTAtps1 strains have reduced NADPH levels during growth on nitrate-containing media due to decreased G6PDH activity
malfunction
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expression of TPS1 driven by the ABI3 promoter rescues the severe embryo phenotype but not the vegetative phenotype of tps1. tps1 exhibits a severe phenotype in vegetative tissue, consistent with the role played in embryo development
malfunction
stress hypersensitivity of mutants deleted for gene TPS1. At 42°C, the viability of the tps1DELTA mutant sharply drops by several decades, whereas the viability of the wild-type TPS1 strain remains almost unchanged. The the mal- BY4741 strain is unable to import trehalose. Overview of the impact of the different stresses on the drop of viability in wild-type and mdeletion mutants. The tps1DELTA mutant rapidly loses its ATP content in response to heat shock at 42°C
malfunction
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tps1DELTA mutants fail to complete embryogenesis and rescued lines have stunted growth and delayed flowering. Loss of trehalose 6-phosphate production might not be the only reason for the growth defects of Arabidopsis thaliana tps1 mutants
malfunction
an otsA deletion mutant has significantly reduced intracellular trehalose levels compared to the wild-type strain and exhibits an apparent markedly slower growth rate in low osmolarity medium
malfunction
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enzyme knockdown decreases hemolymph trehalose content and causes larval and pupal lethality. Enzyme knockdown survivors have a smaller amount of chitin and show elevated feeding on foliage
malfunction
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enzyme knockdown results in optimal interference at 24 h and 36 h postinjection and causes a sharp decline in the survival rate during the 5th instar larval-pupal stage and obviously abnormal or lethal phenotypes. Silencing of the enzyme inhibits chitin biosynthesis. Furthermore, the expression levels of two genes associated with lipid biosynthesis are upregulated
malfunction
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expression inhibition of isoform TPS3 leads to molting and wing deformity
malfunction
increased mortality can be observed in enzyme-depleted larvae under bacterial infection
malfunction
silencing the enzyme gene leads to molting deformities and high mortality rates via regulation of gene expression in the chitin biosynthetic pathway
metabolism
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the first step in trehalose biosynthesis involves trehalose 6-phosphate synthase, Tps1
metabolism
gene TPS1 encodes the first enzyme in trehalose biosynthetic pathway, trehalose is a stress protectant
metabolism
in the OtsAB pathway, a trehalose-6-phosphate synthase (TPS, OtsA) catalyzes the formation of trehalose-6-phosphate from a glucosyl nucleotide and glucose-6-phosphate
metabolism
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in the OtsAB pathway, a trehalose-6-phosphate synthase (TPS, OtsA) catalyzes the formation of trehalose-6-phosphate from a glucosyl nucleotide and glucose-6-phosphate
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physiological function
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disruption of the TPS2 gene encoding the only trehalose 6-phosphate phosphatase activity in Candida albicans causes a pleiotropic defective phenotype, maintaining the cell wall integrity and the ability to form chlamydospores. A homozygous tps2Delta/tps2Delta shows reduced growth at high temperatures and a marked sensitivity to heatshock and severe oxidative exposure. Exponential tps2Delta null cells display an adaptive response to oxidative stress as well as cross-tolerance between temperature and oxidative stress. Differential measurement of trehalose and trehalose 6-phosphate, revealed a significant accumulation of trehalose 6-phosphate in tps2Delta cells, which is enhanced after oxidative exposure. The level of trehalose 6-phosphate in parental cells is virtually undetectable, and oxidative treatment only induces the synthesis of free trehalose
physiological function
DvTPS increases the salt tolerance of the organism, overview
physiological function
regulation of OtsA expression during cold shock, both low temperature and accumulation of trehalose can inhibit OtsA expression, overview
physiological function
the multifunctional protein, OtsA, is indispensable for bacterial survival in various environments. The catalytic efficiency of OtsA is affected by its N-loop at low temperatures. The flexibility of the OtsA N-loop is related to the growth temperature of the respective bacterial species
physiological function
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the non-reducing disaccharide, trehalose, is present in conidia of the fungus and is mobilized during appressorium formation. Trehalose 6-phosphate synthase protein ia a regulator during infection by the rice blast fungus Magnaporthe oryzae. Tps1 functions as a sugar sensor to integrate carbon and nitrogen metabolism and regulate a subset of primary and secondary metabolic pathways, such as the oxidative pentose phosphate pathway and pigment formation, respectively, during plant colonization, allowing the fungus to adapt to the nutritional and redox conditions encountered in the plant cell and establish disease. Tps1 regulates gene expression via the modulation of NADPH. Tps1 also regulates Nmr activity, involved in nitrogen metabolism, mechanism, overview
physiological function
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the TPS1 protein is a key regulator of trehalose metabolism throughout the Arabidopsis life cycle and not just in embryo development, it plays a key role in modulating trehalose 6-phosphate levels in vegetative tissues of Arabidopsis thaliana
physiological function
trehalose phosphate synthase is the crucial enzyme for the biosynthesis of trehalose, the main haemolymph sugar of insects
physiological function
trehalose phosphate synthase is the crucial enzyme for the biosynthesis of trehalose, the main haemolymph sugar of insects
physiological function
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enzyme TPS1 is important throughout the life cycle with At least three catalytically active TPS isoforms
physiological function
in fungi, trehalose-6-phosphate synthase 1 plays a key role in the biosynthesis of trehalose
physiological function
isozyme OstA2 mainly contributes to the trehalose pool of strain 1CP
physiological function
isozyme OtsA1 seems to be involved in the overproduction of trehalose lipids
physiological function
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possible signaling role of trehalose-6-phosphate or trehalose in the dessication process, sugars are proposed to play a role in osmotic adjustment, to stabilize biomolecules and membranes, and to act as a replacement for water
physiological function
the fused trehalose-6-phosphate synthase/phosphatase TPSP consists of an N-terminal trehalose-6-phosphate synthase (TPS) and a C-terminal trehalose-6-phosphate phosphatase (TPP) domain. The gene is organized in an operon with a putative glycosyltransferase GT and a putative mechanosensitive channel MSC. The enzyme exhibits high phosphatase activity, but requires activation by the co-expressed GT for bifunctional synthase-phosphatase activity. The GT mediated activation of trehalose-6-phosphate synthase activity relies on the fusion of both, trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase domain, in the enzyme. Activation is mediated by complex-formation
physiological function
the Tps1 protein is essential to maintain ATP levels during heat shock. Tps1 is endowed with a regulatory function in energy homeostasis, which is essential to withstand adverse conditions and maintain cellular integrity. Tps1, not trehalose, is important for yeast viability in response to various kinds of stresses. Contribution of the Tps1 protein to thermotolerance and acquired thermotolerance, enzyme deletion mutants show highly reduced growth at 42°C in contrast to the wild-type enzyme
physiological function
the enzyme functions as a cytoskeletal element regulating cell morphology
physiological function
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the enzyme is essential for the normal growth and development of Heortia vitessoides
physiological function
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the enzyme regulates trehalose metabolism and also mediates trehalase regulation of chitin synthesis and degradation pathways, and control insect molting process
physiological function
the enzyme takes part in immune defense in Musca domestica via synthesizing its product trehalose
physiological function
trehalose phosphate synthase 5-dependent trehalose metabolism regulates Arabidopsis thaliana defenses against pathogens (necrotrophic Botrytis cinerea and biotrophic Pseudomonas syringae).The enzyme is necessary for trehalose synthesis after pathogen infection
physiological function
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the multifunctional protein, OtsA, is indispensable for bacterial survival in various environments. The catalytic efficiency of OtsA is affected by its N-loop at low temperatures. The flexibility of the OtsA N-loop is related to the growth temperature of the respective bacterial species
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physiological function
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the fused trehalose-6-phosphate synthase/phosphatase TPSP consists of an N-terminal trehalose-6-phosphate synthase (TPS) and a C-terminal trehalose-6-phosphate phosphatase (TPP) domain. The gene is organized in an operon with a putative glycosyltransferase GT and a putative mechanosensitive channel MSC. The enzyme exhibits high phosphatase activity, but requires activation by the co-expressed GT for bifunctional synthase-phosphatase activity. The GT mediated activation of trehalose-6-phosphate synthase activity relies on the fusion of both, trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase domain, in the enzyme. Activation is mediated by complex-formation
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physiological function
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isozyme OtsA1 seems to be involved in the overproduction of trehalose lipids
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physiological function
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isozyme OstA2 mainly contributes to the trehalose pool of strain 1CP
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physiological function
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regulation of OtsA expression during cold shock, both low temperature and accumulation of trehalose can inhibit OtsA expression, overview
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physiological function
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the fused trehalose-6-phosphate synthase/phosphatase TPSP consists of an N-terminal trehalose-6-phosphate synthase (TPS) and a C-terminal trehalose-6-phosphate phosphatase (TPP) domain. The gene is organized in an operon with a putative glycosyltransferase GT and a putative mechanosensitive channel MSC. The enzyme exhibits high phosphatase activity, but requires activation by the co-expressed GT for bifunctional synthase-phosphatase activity. The GT mediated activation of trehalose-6-phosphate synthase activity relies on the fusion of both, trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase domain, in the enzyme. Activation is mediated by complex-formation
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additional information
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trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase form a complex
additional information
differences in muscle trehalose content in female and male animals due to polymorphisms
additional information
differences in muscle trehalose content in female and male animals due to polymorphisms
additional information
differences in muscle trehalose content in female and male animals due to polymorphisms
additional information
differences in muscle trehalose content in female and male animals due to polymorphisms
additional information
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differences in muscle trehalose content in female and male animals due to polymorphisms
additional information
the conserved residues Arg9, Trp45, Tyr81, Trp90, Asp135 and Arg284 are involved in glycosyl acceptor binding, and residues Gly29, His159, Arg246, Lys251, Asp345 and Glu353 are involved in glycosyl donor binding. Homology modeling of the enzyme using the enzyme structure from Escherichia coli, OtsA, PDB ID 1GZ5, chain A, as the template
additional information
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the conserved residues Arg9, Trp45, Tyr81, Trp90, Asp135 and Arg284 are involved in glycosyl acceptor binding, and residues Gly29, His159, Arg246, Lys251, Asp345 and Glu353 are involved in glycosyl donor binding. Homology modeling of the enzyme using the enzyme structure from Escherichia coli, OtsA, PDB ID 1GZ5, chain A, as the template
additional information
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trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase form a complex
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