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2-Deoxy-D-glucose 6-phosphate + H2O
2-Deoxy-D-glucose + phosphate
-
-
-
-
?
alpha,alpha-1,1-trehalose 6-phosphate
alpha,alpha-1,1-trehalose + phosphate
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
D-fructose 6-phosphate + H2O
D-fructose + phosphate
D-glucose 6-phosphate + H2O
D-glucose + phosphate
D-mannose 6-phosphate + H2O
D-mannose + phosphate
-
16% of the activity with trehalose 6-phosphate
-
-
?
glucose 6-phosphate + H2O
?
trehalose 6-phosphate + H2O
trehalose + phosphate
trehalose-6-phosphate + H2O
trehalose + phosphate
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
additional information
?
-
alpha,alpha-1,1-trehalose 6-phosphate
alpha,alpha-1,1-trehalose + phosphate
-
-
-
?
alpha,alpha-1,1-trehalose 6-phosphate
alpha,alpha-1,1-trehalose + phosphate
-
-
-
?
alpha,alpha-1,1-trehalose 6-phosphate
alpha,alpha-1,1-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
16% of the activity with trehalose 6-phosphate
-
-
?
D-fructose 6-phosphate + H2O
D-fructose + phosphate
-
-
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
3.1% of activity with trehalose 6-phosphate
-
-
?
D-glucose 6-phosphate + H2O
D-glucose + phosphate
3.1% of activity with trehalose 6-phosphate
-
-
?
glucose 6-phosphate + H2O
?
-
7% of the activity with trehalose 6-phosphate
-
-
?
glucose 6-phosphate + H2O
?
-
activated by trehalose
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
bioinformatical approach, coexpression networks analyzed
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
high substrate specificity, overview
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
pleiotropic defective phenotype of disrupted TPS2, cell wall integrity and ability to form chlamydospores maintained, reduced growth and temperature sensitivity (42°C) of homozygous mutant, severe oxidative exposure (50 mM H2O2), null mutants reveal adaptive antioxidant response and cross-tolerance between temperature and oxidative stress, expression of TPS2 and TPS1 genes promoted in wild-type cells in response to acute (50 mM) but not gentle (5 mM) oxidative exposure
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
protective role of the trehalose biosynthetic pathway in the cellular response to oxidative stress and subsequently in the resistance to phagocytosis
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
the product trehalose acts as a global against abiotic stress
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
the enzyme is absolutely specific for trehalose 6-phosphate
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
glucose disaccharide with alpha,alpha-1,1 linkage
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
the enzyme is involved in trehalose biosynthesis, trehalose serves as a stress protectant and/or reserve carbohydrate
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
the trehalose pathway involving trehalose-6-phosphate phosphatase plays a role in osmoadaptation, enzyme deficiency leads to reduced osmotolerance
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
high substrate specificity of recombinant enzyme
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
the trehalose pathway involving trehalose-6-phosphate phosphatase plays a role in osmoadaptation, enzyme deficiency leads to reduced osmotolerance
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
high substrate specificity of recombinant enzyme
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
step in trehalose synthesis
-
-
?
trehalose-6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose-6-phosphate + H2O
trehalose + phosphate
-
the enzyme is required for trehalose synthesis
-
-
?
trehalose-6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose-6-phosphate + H2O
trehalose + phosphate
-
-
?
trehalose-6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose-6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose-6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose-6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose-6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose-6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose-6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose-6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose-6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose-6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose-6-phosphate + H2O
trehalose + phosphate
-
in temperature-sensitive mutant that is defect in trehalose 6-phosphate phosphohydrolase the accumulation of high levels of trehalose 6-phosphate probably is inhibitory to growth
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
?
additional information
?
-
phosphomolybdate/malachite green phosphate detection method
-
-
?
additional information
?
-
the enzyme is specific for trehalose 6-phosphate
-
-
?
additional information
?
-
-
the enzyme is specific for trehalose 6-phosphate
-
-
?
additional information
?
-
phosphomolybdate/malachite green phosphate detection method
-
-
?
additional information
?
-
-
the gene gob-1, encoding the enzyme, loss of function causes the lethal gut-obstructed phenotype in the worms, analysis of phenotype including larval lethality, overview
-
-
?
additional information
?
-
wide tissue distribution suggests multiple biosynthetic sites, functional role of trehalose in energy metabolism and physiological adaptation
-
-
?
additional information
?
-
-
wide tissue distribution suggests multiple biosynthetic sites, functional role of trehalose in energy metabolism and physiological adaptation
-
-
?
additional information
?
-
analysis of mechanisms of substrate recognition and catalysis, substrate binding structure, overview
-
-
?
additional information
?
-
-
analysis of mechanisms of substrate recognition and catalysis, substrate binding structure, overview
-
-
?
additional information
?
-
analysis of mechanisms of substrate recognition and catalysis. Tps2 C-terminal trehalose-6-phosphate phosphatase domain (Tps2PD) undergoes a large conformational change upon substrate binding, substrate specificity of Tps2PD, oerview
-
-
?
additional information
?
-
-
no activity with sucrose-6-phosphate, fructose-6-phosphate, glucose-6-phosphate, fructose-6-phosphate, mannose-6-phosphate, 4-nitrophenylphosphate, ATP, and ADP
-
-
?
additional information
?
-
phosphomolybdate/malachite green phosphate detection method
-
-
?
additional information
?
-
substrate binding structure analysis, overview. The substrate binding site of MtbTPP is located within a highly positively charged cavity formed by the 3 conserved motifs. In the complex structure, the sugar group of trehalose 6-phosphate is likely to localize to the opening of the cleft between the hydrolase domain and the cap domain. In contrast, the phosphate group is buried inside the MtbTPP active site and close to the Mg2+. Four MtbTPP residues directly participate in the stabilization of the substrate: Asp149, Ser185, and Gly186, forming hydrogen bonds with the 3 phosphoryl oxygen atoms of trehalose 6-phosphate, and Val156, interacting with the sugar group via its main chain amide
-
-
?
additional information
?
-
-
substrate binding structure analysis, overview. The substrate binding site of MtbTPP is located within a highly positively charged cavity formed by the 3 conserved motifs. In the complex structure, the sugar group of trehalose 6-phosphate is likely to localize to the opening of the cleft between the hydrolase domain and the cap domain. In contrast, the phosphate group is buried inside the MtbTPP active site and close to the Mg2+. Four MtbTPP residues directly participate in the stabilization of the substrate: Asp149, Ser185, and Gly186, forming hydrogen bonds with the 3 phosphoryl oxygen atoms of trehalose 6-phosphate, and Val156, interacting with the sugar group via its main chain amide
-
-
?
additional information
?
-
substrate binding structure analysis, overview. The substrate binding site of MtbTPP is located within a highly positively charged cavity formed by the 3 conserved motifs. In the complex structure, the sugar group of trehalose 6-phosphate is likely to localize to the opening of the cleft between the hydrolase domain and the cap domain. In contrast, the phosphate group is buried inside the MtbTPP active site and close to the Mg2+. Four MtbTPP residues directly participate in the stabilization of the substrate: Asp149, Ser185, and Gly186, forming hydrogen bonds with the 3 phosphoryl oxygen atoms of trehalose 6-phosphate, and Val156, interacting with the sugar group via its main chain amide
-
-
?
additional information
?
-
phosphomolybdate/malachite green phosphate detection method
-
-
?
additional information
?
-
-
the enzyme has essentially no activity with any other sugar phosphates
-
?
additional information
?
-
almost no activity with glucose 1-phosphate, glucose 6-phosphate, galactose 6-phosphate, mannose 1-phosphate, mannose 6-phosphate, fructose 1-phosphate, fructose 6-phosphate, sucrose 6-phosphate, lactose 1-phosphate, and ribose 5-phosphate
-
-
?
additional information
?
-
-
almost no activity with glucose 1-phosphate, glucose 6-phosphate, galactose 6-phosphate, mannose 1-phosphate, mannose 6-phosphate, fructose 1-phosphate, fructose 6-phosphate, sucrose 6-phosphate, lactose 1-phosphate, and ribose 5-phosphate
-
-
?
additional information
?
-
involvement in stress tolerance
-
-
?
additional information
?
-
-
involvement in stress tolerance
-
-
?
additional information
?
-
almost no activity with glucose 1-phosphate, glucose 6-phosphate, galactose 6-phosphate, mannose 1-phosphate, mannose 6-phosphate, fructose 1-phosphate, fructose 6-phosphate, sucrose 6-phosphate, lactose 1-phosphate, and ribose 5-phosphate
-
-
?
additional information
?
-
phosphomolybdate/malachite green phosphate detection method
-
-
?
additional information
?
-
enzyme addtionally acts as tzrehalose 6-phosphate synthase, reaction of EC 2.4.1.15
-
-
?
additional information
?
-
-
enzyme addtionally acts as tzrehalose 6-phosphate synthase, reaction of EC 2.4.1.15
-
-
?
additional information
?
-
enzyme addtionally acts as tzrehalose 6-phosphate synthase, reaction of EC 2.4.1.15
-
-
?
additional information
?
-
enzyme addtionally acts as tzrehalose 6-phosphate synthase, reaction of EC 2.4.1.15
-
-
?
additional information
?
-
glucose diphosphate nucleosides are no substrates
-
-
?
additional information
?
-
glucose diphosphate nucleosides are no substrates
-
-
?
additional information
?
-
-
glucose diphosphate nucleosides are no substrates
-
-
?
additional information
?
-
phosphomolybdate/malachite green phosphate detection method
-
-
?
additional information
?
-
-
the enzyme is complexed with the trehalose 6-phosphate synthase in vivo, both are responsible for trehalose synthesis
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
trehalose 6-phosphate + H2O
trehalose + phosphate
trehalose-6-phosphate + H2O
trehalose + phosphate
additional information
?
-
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
pleiotropic defective phenotype of disrupted TPS2, cell wall integrity and ability to form chlamydospores maintained, reduced growth and temperature sensitivity (42°C) of homozygous mutant, severe oxidative exposure (50 mM H2O2), null mutants reveal adaptive antioxidant response and cross-tolerance between temperature and oxidative stress, expression of TPS2 and TPS1 genes promoted in wild-type cells in response to acute (50 mM) but not gentle (5 mM) oxidative exposure
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
the product trehalose acts as a global against abiotic stress
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
the enzyme is involved in trehalose biosynthesis, trehalose serves as a stress protectant and/or reserve carbohydrate
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
the trehalose pathway involving trehalose-6-phosphate phosphatase plays a role in osmoadaptation, enzyme deficiency leads to reduced osmotolerance
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
the trehalose pathway involving trehalose-6-phosphate phosphatase plays a role in osmoadaptation, enzyme deficiency leads to reduced osmotolerance
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
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step in trehalose synthesis
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trehalose-6-phosphate + H2O
trehalose + phosphate
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the enzyme is required for trehalose synthesis
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trehalose-6-phosphate + H2O
trehalose + phosphate
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trehalose-6-phosphate + H2O
trehalose + phosphate
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trehalose-6-phosphate + H2O
trehalose + phosphate
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trehalose-6-phosphate + H2O
trehalose + phosphate
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in temperature-sensitive mutant that is defect in trehalose 6-phosphate phosphohydrolase the accumulation of high levels of trehalose 6-phosphate probably is inhibitory to growth
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additional information
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the gene gob-1, encoding the enzyme, loss of function causes the lethal gut-obstructed phenotype in the worms, analysis of phenotype including larval lethality, overview
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additional information
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wide tissue distribution suggests multiple biosynthetic sites, functional role of trehalose in energy metabolism and physiological adaptation
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additional information
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wide tissue distribution suggests multiple biosynthetic sites, functional role of trehalose in energy metabolism and physiological adaptation
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additional information
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the enzyme has essentially no activity with any other sugar phosphates
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additional information
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involvement in stress tolerance
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additional information
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involvement in stress tolerance
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additional information
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the enzyme is complexed with the trehalose 6-phosphate synthase in vivo, both are responsible for trehalose synthesis
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evolution
Pseudomonas aeruginosa possesses two trehalose 6-phosphate phosphatase proteins, one with chromosomal and one with extrachromosomal location. The occurrence of both proteins is mutually exclusive, all Pseudomonas aeruginosa strains for which information is available to date possess either the chromosomal (Paer-chTPP) or the plasmid-encoded (Paer-ecTPP) trehalose 6-phosphate phosphatase
evolution
Pseudomonas aeruginosa possesses two trehalose 6-phosphate phosphatase proteins, one with chromosomal and one with extrachromosomal location. The occurrence of both proteins is mutually exclusive, all Pseudomonas aeruginosa strains for which information is available to date possess either the chromosomal (Paer-chTPP) or the plasmid-encoded (Paer-ecTPP) trehalose 6-phosphate phosphatase. The enzyme Paer-chTPP belogs to the HAD superfamily of enzymes, HAD C2 subfamily
evolution
the enzyme belongs to the haloacid dehalogenase (HAD) family of phosphatases. HAD phosphatases are magnesium-dependent and share a common mechanism that involves a nucleophilic attack by an aspartate, resulting in the formation of a phospho-aspartyl intermediate that is then hydrolysed by a water molecule in a second step, releasing phosphate and regenerating the catalytic nucleophile. The HAD enzymes can be classified into three groups based on their structural topology, thus distinguishing among enzymes from nematodes, mycobacteria, other eubacteria, and archaea
evolution
the enzyme belongs to the haloacid dehalogenase (HAD) family of phosphatases. HAD phosphatases are magnesium-dependent and share a common mechanism that involves a nucleophilic attack by an aspartate, resulting in the formation of a phospho-aspartyl intermediate that is then hydrolysed by a water molecule in a second step, releasing phosphate and regenerating the catalytic nucleophile. The HAD enzymes can be classified into three groups based on their structural topology, thus distinguishing among enzymes from nematodes, mycobacteria, other eubacteria, and archaea
evolution
the enzyme belongs to the haloacid dehalogenase (HAD) family of phosphatases. HAD phosphatases are magnesium-dependent and share a common mechanism that involves a nucleophilic attack by an aspartate, resulting in the formation of a phospho-aspartyl intermediate that is then hydrolysed by a water molecule in a second step, releasing phosphate and regenerating the catalytic nucleophile. The HAD enzymes can be classified into three groups based on their structural topology, thus distinguishing among enzymes from nematodes, mycobacteria, other eubacteria, and archaea
evolution
the enzyme belongs to the haloacid dehalogenase (HAD) family of phosphatases. HAD phosphatases are magnesium-dependent and share a common mechanism that involves a nucleophilic attack by an aspartate, resulting in the formation of a phospho-aspartyl intermediate that is then hydrolysed by a water molecule in a second step, releasing phosphate and regenerating the catalytic nucleophile. The HAD enzymes can be classified into three groups based on their structural topology, thus distinguishing among enzymes from nematodes, mycobacteria, other eubacteria, and archaea
evolution
the enzyme belongs to the haloacid dehalogenase (HAD) family of phosphatases. HAD phosphatases are magnesium-dependent and share a common mechanism that involves a nucleophilic attack by an aspartate, resulting in the formation of a phospho-aspartyl intermediate that is then hydrolysed by a water molecule in a second step, releasing phosphate and regenerating the catalytic nucleophile. The HAD enzymes can be classified into three groups based on their structural topology, thus distinguishing among enzymes from nematodes, mycobacteria, other eubacteria, and archaea
evolution
the enzyme belongs to the haloacid dehalogenase (HAD) superfamily, which includes various phosphatases, epoxide hydrolases, P-type ATPases, and L-2-haloacid dehalogenases. The ubiquitous HAD superfamily features 2 domains: the core domain and the cap domain. Both domains are notably conserved across HAD superfamily, while the cap domain typically varies in size
evolution
TPP belongs to the superfamily of haloacid dehalogenase (HAD) phosphatases that share a catalytic domain with the topology of a Rossmann fold
evolution
Tps2PD is a member of the haloacid dehydrogenase superfamily (HADSF) phosphatases, enzymes that recognize a broad spectrum of substrates
evolution
-
Pseudomonas aeruginosa possesses two trehalose 6-phosphate phosphatase proteins, one with chromosomal and one with extrachromosomal location. The occurrence of both proteins is mutually exclusive, all Pseudomonas aeruginosa strains for which information is available to date possess either the chromosomal (Paer-chTPP) or the plasmid-encoded (Paer-ecTPP) trehalose 6-phosphate phosphatase
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evolution
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the enzyme belongs to the haloacid dehalogenase (HAD) superfamily, which includes various phosphatases, epoxide hydrolases, P-type ATPases, and L-2-haloacid dehalogenases. The ubiquitous HAD superfamily features 2 domains: the core domain and the cap domain. Both domains are notably conserved across HAD superfamily, while the cap domain typically varies in size
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evolution
-
the enzyme belongs to the haloacid dehalogenase (HAD) family of phosphatases. HAD phosphatases are magnesium-dependent and share a common mechanism that involves a nucleophilic attack by an aspartate, resulting in the formation of a phospho-aspartyl intermediate that is then hydrolysed by a water molecule in a second step, releasing phosphate and regenerating the catalytic nucleophile. The HAD enzymes can be classified into three groups based on their structural topology, thus distinguishing among enzymes from nematodes, mycobacteria, other eubacteria, and archaea
-
evolution
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Pseudomonas aeruginosa possesses two trehalose 6-phosphate phosphatase proteins, one with chromosomal and one with extrachromosomal location. The occurrence of both proteins is mutually exclusive, all Pseudomonas aeruginosa strains for which information is available to date possess either the chromosomal (Paer-chTPP) or the plasmid-encoded (Paer-ecTPP) trehalose 6-phosphate phosphatase. The enzyme Paer-chTPP belogs to the HAD superfamily of enzymes, HAD C2 subfamily
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malfunction
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complementation assays using different yeast mutants show that ChTPSP possesses trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase activities
malfunction
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overexpression of the gene results in plants with increased size and number of rosette leaves, as well as an increased number of trichome branches
malfunction
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study of ra mutants reveal that RA3 acts upstream of transcriptional regulator RA1 to regulate maize inflorescence meristem identity and determinacy
malfunction
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transgenic plants overexpressing AtTPS1 do not show any phenotypic alterations, other than delayed flowering. The AtPS1 overexpression exhibit drought stress tolerance as well as glucose and ABA insensitive phenotypes
malfunction
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T6PP mutant OrlA displays severe morphological defects related to asexual reproduction when grown on glucose minimal medium. The production of conidia is highly reduced in the temperature-sensitive mutant. The defects can be rescued partially by growth at below 30°C and fully by addition of osmotic stabilizers, e.g. 1.2 M sorbitol or 1% glycerol, reduction in incubation temperature or increase in glucose levels. The orlA mutant is virtually avirulent in two distinct murine models of invasive pulmonary aspergillosis, mutant hyphae are clearly dysmorphic with shorter length compartments between septa and truncated hyphal tips with knobby, abnormal branching, phenotype, overview
malfunction
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disruption of the TPPB gene leads to Arabidopsis plants with larger leaves, which is the result of an increased cell number in the leaves
malfunction
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plants deficient in trehalose-6-phosphate phosphatase D isoform are hypersensitive to high salinity stress
malfunction
a Tps2-specific inhibitor is predicted to eliminate Cryptococcus neoformans infections. Despite the lack of a trehalose biosynthesis function of the Tps2 N-terminal domain (Tps2NTD), deletion of this domain in Cryptococcus neoformans results in a temperature-sensitive phenotype at 39°C, suggesting Tps2NTD is functionally essential for cell survival at elevated temperature. Disruption of any of the direct substrate-protein residue interactions leads to significant or complete loss of phosphatase activity. The Tps2NTD closely resembles the structure of Tps1 but lacks any catalytic activity
malfunction
bacteria may be vulnerable to the detrimental effects of intracellular trehalose 6-phosphate accumulation
malfunction
disruption of any of the direct substrate-protein residue interactions leads to significant or complete loss of phosphatase activity. Mutants tps2DELTA, tps2NTDDELTA, and tps2D705N strains are unable to grow at elevated temperatures
malfunction
two independent OX and Dongjin have significantly greater coleoptile lengths (1.5-2.6fold) and amylase activity (1.5-2.9fold) than their respective null segregants (transgene-lacking siblings) and the OsTPP7 knockout line
malfunction
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bacteria may be vulnerable to the detrimental effects of intracellular trehalose 6-phosphate accumulation
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malfunction
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bacteria may be vulnerable to the detrimental effects of intracellular trehalose 6-phosphate accumulation
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malfunction
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T6PP mutant OrlA displays severe morphological defects related to asexual reproduction when grown on glucose minimal medium. The production of conidia is highly reduced in the temperature-sensitive mutant. The defects can be rescued partially by growth at below 30°C and fully by addition of osmotic stabilizers, e.g. 1.2 M sorbitol or 1% glycerol, reduction in incubation temperature or increase in glucose levels. The orlA mutant is virtually avirulent in two distinct murine models of invasive pulmonary aspergillosis, mutant hyphae are clearly dysmorphic with shorter length compartments between septa and truncated hyphal tips with knobby, abnormal branching, phenotype, overview
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metabolism
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Aspergillus fumigatus contains two trehalose phosphorylases that may be responsible for trehalose production in the absence of OrlA, potential activation of trehalose phosphorylase enzymes by depleted free Pi levels in the orlA mutant, overview
metabolism
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the enzyme catalyzes the final step of trehalose metabolism
metabolism
OsTPP7 is involved in trehalose-6-phosphate (T6P) metabolism, central to an energy sensor that determines anabolism or catabolism depending on local sucrose availability. OsTPP7 activity may increase sink strength in proliferating heterotrophic tissues by indicating low sugar availability through increased alpha,alpha-trehalose 6-phosphate turnover, thus enhancing starch mobilization to drive growth kinetics of the germinating embryo and elongating coleoptile, which consequently enhances anaerobic germination tolerance
metabolism
the enzyme participates in the trehalose biosynthesis. Trehalose is synthesized by the conversion of glucose-6-phosphate and UDP-glucose to trehalose-6-phosphate (T6P) by Tps1 followed by dephosphorylation of T6P by Tps2
metabolism
the enzyme participates in the trehalose biosynthesis. Trehalose is synthesized by the conversion of glucose-6-phosphate and UDP-glucose to trehalose-6-phosphate (T6P) by Tps1 followed by dephosphorylation of T6P by Tps2
metabolism
trehalose-6-phosphate phosphatase (TPP) is a pivotal enzyme in the most prominent biosynthesis pathway (OtsAB)
metabolism
trehalose-6-phosphate phosphatase (TPP) is a pivotal enzyme in the most prominent biosynthesis pathway (OtsAB)
metabolism
trehalose-6-phosphate phosphatase (TPP) is a pivotal enzyme in the most prominent biosynthesis pathway (OtsAB)
metabolism
trehalose-6-phosphate phosphatase (TPP) is a pivotal enzyme in the most prominent biosynthesis pathway (OtsAB)
metabolism
trehalose-6-phosphate phosphatase (TPP) is a pivotal enzyme in the most prominent biosynthesis pathway (OtsAB)
metabolism
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trehalose-6-phosphate phosphatase (TPP) is a pivotal enzyme in the most prominent biosynthesis pathway (OtsAB)
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metabolism
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Aspergillus fumigatus contains two trehalose phosphorylases that may be responsible for trehalose production in the absence of OrlA, potential activation of trehalose phosphorylase enzymes by depleted free Pi levels in the orlA mutant, overview
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physiological function
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enzyme is a functional synthase and phosphatase as proved by yeast complementation assays
physiological function
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functional protein as revealed by yeast complementation assay
physiological function
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in a yeast complementation assay using a yeast strain lacking trehalose 6-phosphate phosphatase no significant enzymatic activity is detected, suggesting a regulatory rather than a metabolic function for the protein
physiological function
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OtTPPA is approximately 100fold more active than the protein of Arabidopsis thaliana
physiological function
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RfTPP is approximately 100fold more active than the protein of Arabidopsis thaliana
physiological function
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trehalose 6-phosphate phosphatase is functional as revealed by yeast complementation assay
physiological function
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trehalose 6-phosphate phosphatase is required for cell wall integrity and fungal virulence but not trehalose biosynthesis. The trehalose biosynthesis pathway is critical for virulence in human and plant fungal pathogens. Cell wall biosynthesis and trehalose 6-phosphate levels are linked
physiological function
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an essential enzyme for growth
physiological function
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isoforms TPPA and TPPG fulfill redundant roles during the differentiation process of root epidermal cells
physiological function
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the enzyme is involved in nitrogen fixation efficiency and plays a role in nodule respiration and adaptation to phosphorus deficiency
physiological function
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the enzyme regulates salt stress tolerance
physiological function
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trehalose 6-phosphate phosphatase is required for development, virulence and mycotoxin biosynthesis apart from trehalose biosynthesis in Fusarium graminearum
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
expression of the OsTPP7 allele enhances anaerobic germination tolerance in all lines investigated, as monitored by coleoptile length and alpha-amylase activity after 4 days of growth in the dark under submergence. OsTPP7 activity results in higher sucrose availability. Although trehalose 6-phosphate contents are not statistically distinguishable between genotypes, the relative amount of trehalose 6-phosphate to sucrose decreases in OsTPP7-containing lines, indicating a change in trehalose 6-phosphate/sucrose homeostasis. Anaerobic germination is tolerated through the presence of a functional OsTPP7 gene
physiological function
trehalose-6-phosphate phosphatase (MtbTPP), an essential enzyme in the trehalose biosynthesis OtsAB pathway, catalyzes the dephosphorylation of trehalose-6-phosphate to generate trehalose, and plays a critical role in Mycobacterium tuberculosis survival-associated cell wall formation and permeability
physiological function
trehalose-6-phosphate phosphatase (OtsB2) is involved in the OtsAB trehalose synthesis pathway to produce free trehalose and is strictly essential for mycobacterial growth
physiological function
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trehalose 6-phosphate phosphatase is required for development, virulence and mycotoxin biosynthesis apart from trehalose biosynthesis in Fusarium graminearum
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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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trehalose-6-phosphate phosphatase (MtbTPP), an essential enzyme in the trehalose biosynthesis OtsAB pathway, catalyzes the dephosphorylation of trehalose-6-phosphate to generate trehalose, and plays a critical role in Mycobacterium tuberculosis survival-associated cell wall formation and permeability
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physiological function
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trehalose-6-phosphate phosphatase (OtsB2) is involved in the OtsAB trehalose synthesis pathway to produce free trehalose and is strictly essential for mycobacterial growth
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physiological function
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an essential enzyme for growth
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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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trehalose 6-phosphate phosphatase is required for cell wall integrity and fungal virulence but not trehalose biosynthesis. The trehalose biosynthesis pathway is critical for virulence in human and plant fungal pathogens. Cell wall biosynthesis and trehalose 6-phosphate levels are linked
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additional information
Candida albicans trehalose-6-phosphate phosphatase (Tps2) is one component of the trehalose biosynthetic complex, which also consists of trehalose synthase (Tps1) and the trehalose synthase regulatory protein (Tps3). Analysis of structures of the N-terminal domain of Tps2 (Tps2NTD) from Candida albicans, and a transition-state complex of the Tps2 C-terminal trehalose-6-phosphate phosphatase domain (Tps2PD) bound to BeF3 and trehalose. The Tps2PD-BeF3-trehalose complex structure reveals a closed conformation that is effected by extensive interactions between each trehalose hydroxyl group and residues of the cap and core domains of the protein, thereby providing exquisite substrate specificity. The Tps2PD-BeF3-trehalose complex structure captures an aspartyl-BeF3 covalent adduct, which closely mimics the proposed aspartyl-phosphate intermediate of the phosphatase catalytic cycle. Structures of substrate-free Tps2PD reveal an open conformation whereby the cap and core domains separate and visualize the striking conformational changes effected by substrate binding and product release and the role of two hinge regions centered at approximately residues 102-103 and 184-188. Substrate binding pocket structure and mechanism analysis, detailed overview
additional information
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Candida albicans trehalose-6-phosphate phosphatase (Tps2) is one component of the trehalose biosynthetic complex, which also consists of trehalose synthase (Tps1) and the trehalose synthase regulatory protein (Tps3). Analysis of structures of the N-terminal domain of Tps2 (Tps2NTD) from Candida albicans, and a transition-state complex of the Tps2 C-terminal trehalose-6-phosphate phosphatase domain (Tps2PD) bound to BeF3 and trehalose. The Tps2PD-BeF3-trehalose complex structure reveals a closed conformation that is effected by extensive interactions between each trehalose hydroxyl group and residues of the cap and core domains of the protein, thereby providing exquisite substrate specificity. The Tps2PD-BeF3-trehalose complex structure captures an aspartyl-BeF3 covalent adduct, which closely mimics the proposed aspartyl-phosphate intermediate of the phosphatase catalytic cycle. Structures of substrate-free Tps2PD reveal an open conformation whereby the cap and core domains separate and visualize the striking conformational changes effected by substrate binding and product release and the role of two hinge regions centered at approximately residues 102-103 and 184-188. Substrate binding pocket structure and mechanism analysis, detailed overview
additional information
comparisons of phenotypes of OsTPP7 present and absent Oryza sativa lines
additional information
in contrast to Asp213, the residue inferred to carry out the nucleophilic attack on the substrate, Asp215 and Asp428 of enzyme BmTPP are involved in the chemistry steps of enzymatic hydrolysis of the substrate, molecular mechanism, overview. BmTPP structural topology, structure comparisons
additional information
residues interacting with the substrate in catalysis are Asp147, Asp149, Asp330, and Asp331, they are pivotal for the enzymatic activity of enzyme MtbTPP. Enzyme structure comparisons, overview
additional information
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residues interacting with the substrate in catalysis are Asp147, Asp149, Asp330, and Asp331, they are pivotal for the enzymatic activity of enzyme MtbTPP. Enzyme structure comparisons, overview
additional information
structure analysis of catalytically dead Tps2PD(D24N) from Cryptococcus neoformans bound to trehalose-6-phosphate. The Tps2PD(D24N)-T6P complex structures reveals a closed conformation that is effected by extensive interactions between each trehalose hydroxyl group and residues of the cap and core domains of the protein, thereby providing exquisite substrate specificity
additional information
three-dimensional enzyme structure analysis and comparisons, overview. Molecular dynamics simulation highlights substantial flexibility of the beta2/beta3 hairpin with respect to the core domain
additional information
three-dimensional enzyme structure analysis and comparisons, overview. Molecular dynamics simulation highlights substantial flexibility of the beta2/beta3 hairpin with respect to the core domain
additional information
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three-dimensional enzyme structure analysis and comparisons, overview. Molecular dynamics simulation highlights substantial flexibility of the beta2/beta3 hairpin with respect to the core domain
additional information
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residues interacting with the substrate in catalysis are Asp147, Asp149, Asp330, and Asp331, they are pivotal for the enzymatic activity of enzyme MtbTPP. Enzyme structure comparisons, overview
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additional information
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three-dimensional enzyme structure analysis and comparisons, overview. Molecular dynamics simulation highlights substantial flexibility of the beta2/beta3 hairpin with respect to the core domain
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D213N
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
D215N
site-directed mutagenesis, the mutant shows about 80% reduced activity compared to the wild-type enzyme
D336A
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
D378A
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
D424N
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
D428N
site-directed mutagenesis, the mutant shows about 85-90% reduced activity compared to the wild-type enzyme
DELTA59
the mutant shows increased catalytic efficiency compared to the wild type enzyme
E384A
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
E386A
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
K334A
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
N228A
the mutant shows increased catalytic efficiency compared to the wild type enzyme
Q332A
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
R337A
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
S329A
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
T339A
the mutant shows increased catalytic efficiency compared to the wild type enzyme
W280A
the mutant shows increased catalytic efficiency compared to the wild type enzyme
Y221A
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
Y225A
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
D705N
site-directed mutagenesis, inactive mutant, the mutant fails to restore growth at elevated temperatures
D147A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D149A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D330A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
D331A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
L29M/L133M
site-directed mutagenesis, mutant MtbTPP-M1
S68A
site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
D147A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
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D149A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
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D330A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
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S68A
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site-directed mutagenesis, the mutant shows activity similar to the wild-type enzyme
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D24N
site-directed mutagenesis, inactive mutant
D24N
site-directed mutagenesis, inactive mutant
additional information
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generation of a null mutant of orlA by disruption of the coding sequence in the uracil/uridine auxotrophic Aspergillus fumigatus strain CEA17 with the selectable marker pyrG from Aspergillus parasiticus, phenotype and quantitative real-time PCR analysis of cell wall biosynthesis genes in the orlA mutant and wild type, overview
additional information
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generation of a null mutant of orlA by disruption of the coding sequence in the uracil/uridine auxotrophic Aspergillus fumigatus strain CEA17 with the selectable marker pyrG from Aspergillus parasiticus, phenotype and quantitative real-time PCR analysis of cell wall biosynthesis genes in the orlA mutant and wild type, overview
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additional information
construction of deletion mutants deleting either the N-terminal domain or the other part of the enzyme, structure and phenotypes, overview
additional information
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construction of deletion mutants deleting either the N-terminal domain or the other part of the enzyme, structure and phenotypes, overview
additional information
deletion of the N-terminal domain of Tps2, mutant Tps2NTD, resulting in a temperature-sensitive phenotype at 39°C, structure analysis of mutant Tps2NTD
additional information
trehalose has been implicated in tolerance to abiotic stress in plants, so the response to heat stress of seeds from the transgenic lines of Solanum lycopersicum cv. Joyful and seeds from wild-type plants are compared. Wild-type heat-treated seeds have a germination rate of 17%, while four transgenic lines have germination rates over 50% following heat stress at 55°C. In one heat-treated transgenic line, 100% of the seeds germinated, and therefore had a germination rate six times that of seeds from wild-type plants. Quantitative PCR reveals that the expression of diverse genes that respond to heat stress is enhanced in TPSP transgenic seeds compared to wild-type seeds 150 min after the onset of heat stress. The enhanced germination rate and expression of these genes in the transgenic seeds are essentially mimicked in wild-type seeds treated with 1 mM exogenous trehalose. Accumulated trehalose and associated metabolites may act as signaling molecules that enhance the expression of heat stress-responsive genes and confer heat-stress tolerance to seeds. Changed of transcript levels of imbibed seeds in TPSP transgenic and wild type with exogenous trehalose under no heat-treated condition, overview
additional information
deletion of the N-terminal domain results in mutant DELTAN-terminal domaincomprising residues 121-391, which shows 70% reduced activity compared to wild-type, deletion of residues 121-391 resulting in the isolated N-terminal domain and comprising residues 1-120 leads to complete loss of activity
additional information
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deletion of the N-terminal domain results in mutant DELTAN-terminal domaincomprising residues 121-391, which shows 70% reduced activity compared to wild-type, deletion of residues 121-391 resulting in the isolated N-terminal domain and comprising residues 1-120 leads to complete loss of activity
additional information
effects of OtsB2 expression in Mycobacterium tuberculosis variant bovis BCG on mycobacterial phenotypes such as growth, phagocytosis and survival in macrophages. Mycobacterium bovis-bacillus calmette-guerin (BCG) overexpressing enzyme OtsB2 is able to better survive in stationary phase. Overexpression of enzyme OtsB2 leads to a decrease in phagocytosis but not survival in human monocyte cell-line THP-1, macrophage-like cells, and this is not due to a decrease in general macrophage phagocytic activity. Strain BCG overexpressing enzyme OtsB2 have stronger binding to THP-1 cells than wild-type BCG. Altering OtsB2 expression has implications for mycobacterial host-pathogen interactions, overview
additional information
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deletion of the N-terminal domain results in mutant DELTAN-terminal domaincomprising residues 121-391, which shows 70% reduced activity compared to wild-type, deletion of residues 121-391 resulting in the isolated N-terminal domain and comprising residues 1-120 leads to complete loss of activity
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additional information
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effects of OtsB2 expression in Mycobacterium tuberculosis variant bovis BCG on mycobacterial phenotypes such as growth, phagocytosis and survival in macrophages. Mycobacterium bovis-bacillus calmette-guerin (BCG) overexpressing enzyme OtsB2 is able to better survive in stationary phase. Overexpression of enzyme OtsB2 leads to a decrease in phagocytosis but not survival in human monocyte cell-line THP-1, macrophage-like cells, and this is not due to a decrease in general macrophage phagocytic activity. Strain BCG overexpressing enzyme OtsB2 have stronger binding to THP-1 cells than wild-type BCG. Altering OtsB2 expression has implications for mycobacterial host-pathogen interactions, overview
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additional information
overexpression of Oryza sativa TPP in Zea mays increases both kernel set and harvest index. Field data at several sites and over multiple seasons show that the engineered trait improves yields from 9% to 49% under non-drought or mild drought conditions, and from 31% to 123% under more severe drought conditions, relative to yields from nontransgenic controls. Yield increases are consistent over time. Phenotype, overview
additional information
yeast gene encoding trehalose-6-phosphate synthase (TPS1) fused to yeast gene encoding trehalose-6-phosphate phosphatase (TPS2) gene expression under the 35S promoter in Medicago sativa plants leads to plants with stunted growth and less biomass, whereas TPS1-TPS2 expression driven by the rd29A promoter improves growth and provokes a significant increase in plant biomass at the foliage level in the different transgenic lines. Trehalose accumulates in all the different lines at similar levels under stress conditions (drought by watering withheld for 5, 10, 20, and 30 d, freezing by preadapted 5 d at 4°C before subjected to freezing stress at -5, -10, and -15°C for 6, 12, 24, 48, and 72 h, and heat-shock by treatment at 40, 45, 50, and 55°C during 1 h). Transgenic plants display a significant increase in drought, freezing, salt, and heat tolerance, phenotypes, detailed overview
additional information
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yeast gene encoding trehalose-6-phosphate synthase (TPS1) fused to yeast gene encoding trehalose-6-phosphate phosphatase (TPS2) gene expression under the 35S promoter in Medicago sativa plants leads to plants with stunted growth and less biomass, whereas TPS1-TPS2 expression driven by the rd29A promoter improves growth and provokes a significant increase in plant biomass at the foliage level in the different transgenic lines. Trehalose accumulates in all the different lines at similar levels under stress conditions (drought by watering withheld for 5, 10, 20, and 30 d, freezing by preadapted 5 d at 4°C before subjected to freezing stress at -5, -10, and -15°C for 6, 12, 24, 48, and 72 h, and heat-shock by treatment at 40, 45, 50, and 55°C during 1 h). Transgenic plants display a significant increase in drought, freezing, salt, and heat tolerance, phenotypes, detailed overview
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