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Enzyme Nomenclature
Information on EC 2.4.1.15 - alpha,alpha-trehalose-phosphate synthase (UDP-forming)
Word Map on EC 2.4.1.15
- 2.4.1.15
- trehalase
- disaccharide
- tpp
-
desiccation
- maltotriose
-
resurrection
- isomaltose
-
anhydrobiosis
- selaginella
-
snf1-related
- agriculture
- drug development
- medicine
- analysis
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
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EC NUMBER 
COMMENTARY 
2.4.1.15
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RECOMMENDED NAME
GeneOntology No.
alpha,alpha-trehalose-phosphate synthase (UDP-forming)
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate
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UDP-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate
ordered bi-bi mechanism
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UDP-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate
complex bimodal kinetics
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UDP-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate
reaction mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
hexosyl group transfer
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
UDP-glucose:D-glucose-6-phosphate 1-alpha-D-glucosyltransferase
See also EC 2.4.1.36 [alpha,alpha-trehalose-phosphate synthase (GDP-forming)].
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CAS REGISTRY NUMBER
COMMENTARY
9030-07-3
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from the alpine permafrost, CGMCC 1.8987, gene otsA
UniProt
bifunctional trehalose 6-phospate synthase and trehalose 6-phospate phosphatase enzyme
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; bifunctional trehalose-6-phosphate synthase/phosphatase, EC 2.4.1.15 and EC 3.1.3.12
SwissProt
bifunctional trehalose-6-phosphate synthase/phosphatase, EC 2.4.1.15 and EC 3.1.3.12
SwissProt
isozyme 1a; collected from the upper Chesapeake Bay, China
UniProt
isozyme 1b; collected from the upper Chesapeake Bay, China
UniProt
isozyme 1c; collected from the upper Chesapeake Bay, China
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
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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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; the enzyme belongs to the glucosyltransferase-GTB-type superfamily
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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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
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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
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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
metabolism
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the first step in trehalose biosynthesis involves trehalose 6-phosphate synthase, Tps1
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; 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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gene TPS1 encodes the first enzyme in trehalose biosynthetic pathway, trehalose is a stress protectant
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; 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
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
regulation of OtsA expression during cold shock, both low temperature and accumulation of trehalose can inhibit OtsA expression, overview
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
DvTPS increases the salt tolerance of the organism, overview
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
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
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enzyme TPS1 is important throughout the life cycle with At least three catalytically active TPS isoforms
physiological function
isozyme OstA2 mainly contributes to the trehalose pool of strain 1CP; isozyme OtsA1 seems to be involved in the overproduction of trehalose lipids
physiological function
in fungi, trehalose-6-phosphate synthase 1 plays a key role in the biosynthesis of trehalose
physiological function
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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
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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
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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 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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isozyme OstA2 mainly contributes to the trehalose pool of strain 1CP; isozyme OtsA1 seems to be involved in the overproduction of trehalose lipids
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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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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
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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differences in muscle trehalose content in female and male animals due to polymorphisms; differences in muscle trehalose content in female and male animals due to polymorphisms; differences in muscle trehalose content in female and male animals due to polymorphisms; 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; differences in muscle trehalose content in female and male animals due to polymorphisms; differences in muscle trehalose content in female and male animals due to polymorphisms; 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; differences in muscle trehalose content in female and male animals due to polymorphisms; differences in muscle trehalose content in female and male animals due to polymorphisms; 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; differences in muscle trehalose content in female and male animals due to polymorphisms; differences in muscle trehalose content in female and male animals due to polymorphisms; 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; differences in muscle trehalose content in female and male animals due to polymorphisms; differences in muscle trehalose content in female and male animals due to polymorphisms; differences in muscle trehalose content in female and male animals due to polymorphisms
additional information
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trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase form a complex
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
dTDP-glucose + glucose 6-phosphate
trehalose 6-phosphate + dTDP
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?
GDP-glucose + glucose 6-phosphate
GDP + alpha,alpha-trehalose 6-phosphate
cf. EC 2.4.1.36
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?
TDP-alpha-D-glucose + D-glucose 6-phosphate
TDP + alpha,alpha-1,1-trehalose 6-phosphate
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-
-
-
?
UDP-alpha-D-glucose + D-fructose 6-phosphate
UDP + ?
activity with D-fructose 6-phosphate is about 10% compared to the activity with D-glucose 6-phosphate
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-
?
UDP-alpha-D-glucose + D-galactose 6-phosphate
UDP + ?
activity with D-galactose 6-phosphate is about 10% compared to the activity with D-glucose 6-phosphate
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?
UDP-alpha-D-glucose + D-mannose 6-phosphate
UDP + ?
activity with D-mannose 6-phosphate is about 40% compared to the activity with D-glucose 6-phosphate
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?
UDP-alpha-D-glucose + D-mannose 6-phosphate
UDP + alpha,alpha-1,1-trehalose 6-phosphate
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maximum activity with glucose 6-phosphate, followed by mannose 6-phosphate and fructose 6-phosphate
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?
UDP-glucose + D-fructose 6-phosphate
UDP + ?
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16% of the activity with D-glucose 6-phosphate
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?
UDP-glucose + D-galactose
UDP + ?
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17% of the activity with D-glucose 6-phosphate
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?
UDP-glucose + D-glucose
UDP + ?
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28% of the activity with D-glucose 6-phosphate
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?
UDP-glucose + lactose
UDP + ?
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10% of the activity with D-glucose 6-phosphate
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?
UDP-glucose + sucrose
UDP + ?
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19% of the activity with D-glucose 6-phosphate
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?
ADP-alpha-D-glucose + D-glucose 6-phosphate
ADP + alpha,alpha-1,1-trehalose 6-phosphate
4% of the activity with UDP-glucose
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?
ADP-alpha-D-glucose + D-glucose 6-phosphate
ADP + alpha,alpha-1,1-trehalose 6-phosphate
4% of the activity with UDP-glucose
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?
ADP-alpha-D-glucose + D-glucose 6-phosphate
ADP + alpha,alpha-trehalose 6-phosphate
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ADP-glucose is the best donor substrate
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?
ADP-alpha-D-glucose + D-glucose 6-phosphate
ADP + alpha,alpha-trehalose 6-phosphate
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ADP-glucose is the best donor substrate
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?
ADP-alpha-D-glucose + D-glucose 6-phosphate
ADP + alpha,alpha-trehalose 6-phosphate
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13.4% of the activity with GDPglucose
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?
ADP-alpha-D-glucose + D-glucose 6-phosphate
ADP + alpha,alpha-trehalose 6-phosphate
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-
-
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?
ADP-alpha-D-glucose + D-glucose 6-phosphate
ADP + alpha,alpha-trehalose 6-phosphate
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-
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?
ADP-alpha-D-glucose + D-glucose 6-phosphate
ADP + alpha,alpha-trehalose 6-phosphate
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in crude extracts of Propionibacterium freudenreichii, OtsA is specific for ADP-glucose, in contrast to the pure recombinant OtsA, which uses UDP-glucose, GDP-glucose and TDP-glucose, in addition to ADP-glucose. The substrate specificity of OtsA in cell extracts is lost during purification, and the recombinant OtsA becomes specific to ADP-glucose upon incubation with a dialysed cell extract
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?
ADP-alpha-D-glucose + D-glucose 6-phosphate
ADP + alpha,alpha-trehalose 6-phosphate
activity with ADP-glucose is about 50% compared to the activity with UDP-glucose
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-
?
ADP-alpha-D-glucose + D-glucose 6-phosphate
ADP + alpha,alpha-trehalose 6-phosphate
less effective than UDP-glucose
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-
?
ADP-alpha-D-glucose + D-glucose 6-phosphate
ADP + alpha,alpha-trehalose 6-phosphate
less effective than UDP-glucose
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?
ADP-glucose + D-glucose 6-phosphate
ADP + alpha,alpha-trehalose 6-phosphate
recombinant His10-tagged OtsA1 shows highest activity with ADP-glucose and UDP-glucose, whereas recombinant His10-tagged OtsA2 prefers UDP-glucose
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-
?
ADP-glucose + D-glucose 6-phosphate
ADP + alpha,alpha-trehalose 6-phosphate
recombinant His10-tagged OtsA1 shows highest activity with ADP-glucose and UDP-glucose, whereas recombinant His10-tagged OtsA2 prefers UDP-glucose
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?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
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-
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?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
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-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
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-
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?
CDP-glucose + D-glucose 6-phosphate
trehalose 6-phosphate + CDP
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-
-
-
?
CDP-glucose + D-glucose 6-phosphate
trehalose 6-phosphate + CDP
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-
-
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?
GDP-alpha-D-glucose + D-glucose 6-phosphate
GDP + alpha,alpha-1,1-trehalose 6-phosphate
23% of the activity with UDP-glucose
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-
?
GDP-alpha-D-glucose + D-glucose 6-phosphate
GDP + alpha,alpha-1,1-trehalose 6-phosphate
23% of the activity with UDP-glucose
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-
?
GDP-alpha-D-glucose + D-glucose 6-phosphate
GDP + alpha,alpha-1,1-trehalose 6-phosphate
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-
-
-
?
GDP-alpha-D-glucose + D-glucose 6-phosphate
GDP + alpha,alpha-trehalose 6-phosphate
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cf. EC 2.4.1.36
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-
?
GDP-alpha-D-glucose + D-glucose 6-phosphate
GDP + alpha,alpha-trehalose 6-phosphate
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cf. EC 2.4.1.36
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-
?
GDP-alpha-D-glucose + D-glucose 6-phosphate
GDP + alpha,alpha-trehalose 6-phosphate
-
in crude extracts of Propionibacterium freudenreichii, OtsA is specific for ADP-glucose, in contrast to the pure recombinant OtsA, which uses UDP-glucose, GDP-glucose and TDP-glucose, in addition to ADP-glucose. The substrate specificity of OtsA in cell extracts is lost during purification, and the recombinant OtsA becomes specific to ADP-glucose upon incubation with a dialysed cell extract
-
-
?
GDP-alpha-D-glucose + D-glucose 6-phosphate
GDP + alpha,alpha-trehalose 6-phosphate
activity with GDP-glucose is about 20% compared to the activity with UDP-glucose
-
-
?
GDP-alpha-D-glucose + D-glucose 6-phosphate
GDP + alpha,alpha-trehalose 6-phosphate
much less effective than UDP-glucose
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-
?
GDP-alpha-D-glucose + D-glucose 6-phosphate
GDP + alpha,alpha-trehalose 6-phosphate
much less effective than UDP-glucose
-
-
?
GDP-glucose + D-glucose 6-phosphate
trehalose 6-phosphate + GDP
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18.4% of the activity with UDP-glucose
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-
?
GDP-glucose + D-glucose 6-phosphate
trehalose 6-phosphate + GDP
-
-
-
-
?
GDP-glucose + D-glucose 6-phosphate
trehalose 6-phosphate + GDP
-
-
-
-
?
GDP-glucose + D-glucose 6-phosphate
trehalose 6-phosphate + GDP
-
13% of the activity with UDPglucose
-
-
?
TDP-alpha-D-glucose + D-glucose 6-phosphate
TDP + alpha,alpha-trehalose 6-phosphate
-
-
-
-
?
TDP-alpha-D-glucose + D-glucose 6-phosphate
TDP + alpha,alpha-trehalose 6-phosphate
-
-
-
-
?
TDP-alpha-D-glucose + D-glucose 6-phosphate
TDP + alpha,alpha-trehalose 6-phosphate
-
in crude extracts of Propionibacterium freudenreichii, OtsA is specific for ADP-glucose, in contrast to the pure recombinant OtsA, which uses UDP-glucose, GDP-glucose and TDP-glucose, in addition to ADP-glucose. The substrate specificity of OtsA in cell extracts is lost during purification, and the recombinant OtsA becomes specific to ADP-glucose upon incubation with a dialysed cell extract
-
-
?
TDP-alpha-D-glucose + D-glucose 6-phosphate
TDP + alpha,alpha-trehalose 6-phosphate
less effective than UDP-glucose
-
-
?
TDP-glucose + glucose 6-phosphate
trehalose 6-phosphate + TDP
-
15.9% of the activity with UDPglucose
-
-
?
TDP-glucose + glucose 6-phosphate
trehalose 6-phosphate + TDP
-
-
-
-
?
UDP-alpha-D-glucose + D-fructose 6-phosphate
UDP + alpha,alpha-1,1-trehalose 6-phosphate
-
maximum activity with glucose 6-phosphate, followed by mannose 6-phosphate and fructose 6-phosphate
-
-
?
UDP-alpha-D-glucose + D-fructose 6-phosphate
UDP + alpha,alpha-1,1-trehalose 6-phosphate
-
presence of glycosyltransferase protein is required
-
?
UDP-alpha-D-glucose + D-fructose 6-phosphate
UDP + alpha,alpha-1,1-trehalose 6-phosphate
-
presence of glycosyltransferase protein is required
-
?
UDP-alpha-D-glucose + D-fructose 6-phosphate
UDP + alpha,alpha-1,1-trehalose 6-phosphate
-
presence of glycosyltransferase protein is required
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-1,1-trehalose 6-phosphate
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-1,1-trehalose 6-phosphate
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-1,1-trehalose 6-phosphate
-
step in trehalose biosynthesis
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-1,1-trehalose 6-phosphate
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-1,1-trehalose 6-phosphate
-
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-1,1-trehalose 6-phosphate
-
maximum activity with glucose 6-phosphate, followed by mannose 6-phosphate and fructose 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
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
first step in trehalose biosynthesis, enzyme is essential for embryo maturation
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
step in trehalose biosynthesis
-
-
?
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
-
-
-
?
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
-
step in trehalose biosynthesis
-
-
?
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
both TPS1 and TPS2 are required for high-temperature (37°C) growth and glycolysis but that the block at TPS2 results in the apparent toxic accumulation of trehalose-6-phosphate, which makes this enzyme a fungicidal target
-
-
?
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
both TPS1 and TPS2 are required for high-temperature (37°C) growth and glycolysis but that the block at TPS2 results in the apparent toxic accumulation of trehalose-6-phosphate, which makes this enzyme a fungicidal target
-
-
?
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
the enzyme is substrate-specific
-
-
?
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
-
-
-
-
?
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
the enzyme is substrate-specific
-
-
?
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
-
step in trehalose biosynthesis
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
with retention of the anomeric configuration of the UDP-sugar donor, reaction stereochemistry
-
-
?
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
-
in crude extracts of Propionibacterium freudenreichii, OtsA is specific for ADP-glucose, in contrast to the pure recombinant OtsA, which uses UDP-glucose, GDP-glucose and TDP-glucose, in addition to ADP-glucose. The substrate specificity of OtsA in cell extracts is lost during purification, and the recombinant OtsA becomes specific to ADP-glucose upon incubation with a dialysed cell extract
-
-
?
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
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
step in trehalose biosynthesis
-
-
?
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
-
step in trehalose biosynthesis
-
-
?
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
-
step in trehalose biosynthesis
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
the enzyme is highly specific for UDP-glucose and D-glucose 6-phosphate
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
the enzyme can utilize various nucleoside diphosphate monosaccharides. Maximal activity with UDP-glucose. Various phosphorylated monosaccharides D-glucose 6-phosphate, glucosamine-6-phosphate, fructose-6-phosphate and mannose-6-phosphate can be used as catalytic acceptors, with maximal activity towards D-glucose 6-phosphate
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
first step in one of 2 existing trehalose biosynthesis pathways, plays a role in osmoadaptation
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
best substrates, absolutely specific for D-glucose 6-phosphate
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
first step in one of 2 existing trehalose biosynthesis pathways, plays a role in osmoadaptation
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
best substrates, absolutely specific for D-glucose 6-phosphate
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
recombinant His10-tagged OtsA1 shows highest activity with ADP-glucose and UDP-glucose, whereas recombinant His10-tagged OtsA2 prefers UDP-glucose
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
recombinant His10-tagged OtsA1 shows highest activity with ADP-glucose and UDP-glucose, whereas recombinant His10-tagged OtsA2 prefers UDP-glucose
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
the enzyme is essential for Arabidopsis embryo development, TPS1 appears to play a vital role in responding to the increase in sucrose supply, which accompanies the onset of embryo maturation
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
AtTPS1 is a single-copy gene and is expressed constitutively at very low levels
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
trehalose-6-phosphate synthase A affects citrate accumulation by Aspergillus niger under conditions of high glycolytic flux
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
absolute specificity for glucose 6-phosphate
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
enzyme is osmotically inducible, mutants which are defective in the synthesis of the synthase have an impaired osmotic tolerance in glucose-mineral medium
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
specific for UDPglucose, no reaction with ADPglucose or GDPglucose
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
absolute specificity for glucose 6-phosphate
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
absolute specificity for glucose 6-phosphate
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
TPS1-encoded trehalose-6-phosphate synthase exerts an essential control on the influx into glycolysis. Tps1-mediated protein-protein interactions are important for control of glucose influx into yeast glycolysis
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
key enzyme for biosynthesis of trehalose, the major soluble carbohydrate in resting cells
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
the enzyme plays a role in the control of glycolysis
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
key enzyme for biosynthesis of trehalose, the major soluble carbohydrate in resting cells
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
alpha,alpha-trehalose 6-phosphate synthase is dispensable for growth on glucose but not for spore germination
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
the enzyme does not play a role in the control of glycolysis
-
?
additional information
?
-
no substrate: CDP-glucose, fructose 6-phosphate
-
-
-
additional information
?
-
no substrate: CDP-glucose, fructose 6-phosphate
-
-
-
additional information
?
-
-
the enzyme, encoded by gen tps1, is a regulator of glucose, abscisic acid, and stress signaling, trehalose is an osmoprotectant, trehalose content in wild-type and transgenic plants, overview
-
-
-
additional information
?
-
-
TPS1 may play a major role in coordinating cell wall biosynthesis and cell division with cellular metabolism during embryo development
-
-
-
additional information
?
-
-
the purified native enzyme is not absolutely substrate-specific, besides glucose 6-phosphate, the enzyme is able to use fructose 6-phosphate as an acceptor of glucose. The enzyme is inactive in the presence of glucose and fructose
-
-
-
additional information
?
-
the purified native enzyme is not absolutely substrate-specific, besides glucose 6-phosphate, the enzyme is able to use fructose 6-phosphate as an acceptor of glucose. The enzyme is inactive in the presence of glucose and fructose
-
-
-
additional information
?
-
the purified native enzyme is not absolutely substrate-specific, besides glucose 6-phosphate, the enzyme is able to use fructose 6-phosphate as an acceptor of glucose. The enzyme is inactive in the presence of glucose and fructose
-
-
-
additional information
?
-
-
trehalose is able to protect the integrity of the cells against a variety of environmental stresses such as desiccation, dehydration, heat, cold, and oxidation, probably via reduction of protein denaturation through protein-trehalose interactions, the enzyme might be a radical scavenger
-
-
-
additional information
?
-
-
ADP-gucose is the best donor substrate, and displays highest activity of 4.23 U/mg, followed by UDPG with 2.016 U/mg and GDPG with 1.609 U/mg. TDPG displays activity of 0.95 U/mg
-
-
-
additional information
?
-
-
ADP-gucose is the best donor substrate, and displays highest activity of 4.23 U/mg, followed by UDPG with 2.016 U/mg and GDPG with 1.609 U/mg. TDPG displays activity of 0.95 U/mg
-
-
-
additional information
?
-
-
trehalose is able to protect the integrity of the cells against a variety of environmental stresses such as desiccation, dehydration, heat, cold, and oxidation, probably via reduction of protein denaturation through protein-trehalose interactions, in flying insects trehalose content is especially high in hemolymph and thorax muscles and is consumed during flight
-
-
-
additional information
?
-
-
trehalose acts as a global protectant against abiotic stress, accumulation of trehalose leads to increased salt, drought, and cold resistance in plants
-
-
-
additional information
?
-
-
trehalose is able to protect the integrity of the cells against a variety of environmental stresses such as desiccation, dehydration, heat, cold, and oxidation, probably via reduction of protein denaturation through protein-trehalose interactions
-
-
-
additional information
?
-
-
donor subsite interactions, enzyme-substrate binding conformation, the N-terminal loop, residues 9-22, is responsible for the more relaxed coformation of the binary enzyme-UDP-sugar complex, overview
-
-
-
additional information
?
-
-
yeast functional complementation analysis shows that DvTPS has neither trehalose-6-phosphate synthase nor trehalose-6-phosphate phospatase activity
-
-
-
additional information
?
-
yeast functional complementation analysis shows that DvTPS has neither trehalose-6-phosphate synthase nor trehalose-6-phosphate phospatase activity
-
-
-
additional information
?
-
-
no substrates: fructose, fructose 6-phosphate, glucose, sucrose, and trehalose
-
-
-
additional information
?
-
-
the trehalose-6-phosphate synthase/phosphatase (OtsA–OtsB) pathway plays an important role in the synthesis of trehalose in response to stress
-
-
-
additional information
?
-
-
trehalose is able to protect the integrity of the cells against a variety of environmental stresses such as desiccation, dehydration, heat, cold, and oxidation, probably via reduction of protein denaturation through protein-trehalose interactions, the enzyme might be a radical scavenger
-
-
-
additional information
?
-
-
trehalose is able to protect the integrity of the cells against a variety of environmental stresses such as desiccation, dehydration, heat, cold, and oxidation, probably via reduction of protein denaturation through protein-trehalose interactions
-
-
-
additional information
?
-
-
substrate specificity, no activity with trehalose, maltose, or fructose as acceptor substrates
-
-
-
additional information
?
-
the enzyme utilizes UDP-glucose, ADP-glucose (ADPG) and GDP-glucose (GDPG) as glycosyl donors and various phosphorylated monosaccharides as glycosyl acceptors. Maximal activity is found towards UDP-glucose and D-glucose 6-phosphate. The N-loop region is important for the catalytic efficiency of the enzyme, different roles of N-loop sequences in different trehalose-6-phosphate synthases
-
-
-
additional information
?
-
-
the enzyme utilizes UDP-glucose, ADP-glucose (ADPG) and GDP-glucose (GDPG) as glycosyl donors and various phosphorylated monosaccharides as glycosyl acceptors. Maximal activity is found towards UDP-glucose and D-glucose 6-phosphate. The N-loop region is important for the catalytic efficiency of the enzyme, different roles of N-loop sequences in different trehalose-6-phosphate synthases
-
-
-
additional information
?
-
donor substrate specificity in descending order: UDP-glucose, TDP-glucose, ADP-glucose, GDP-glucose, no activity with mannose-6-phosphate, fructose 6-phosphate, or glucose 1,6-diphosphate as acceptors
-
-
-
additional information
?
-
donor substrate specificity in descending order: UDP-glucose, TDP-glucose, ADP-glucose, GDP-glucose, no activity with mannose-6-phosphate, fructose 6-phosphate, or glucose 1,6-diphosphate as acceptors
-
-
-
additional information
?
-
-
donor substrate specificity in descending order: UDP-glucose, TDP-glucose, ADP-glucose, GDP-glucose, no activity with mannose-6-phosphate, fructose 6-phosphate, or glucose 1,6-diphosphate as acceptors
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-1,1-trehalose 6-phosphate
-
step in trehalose biosynthesis
-
-
?
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
Q94AH8
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
first step in trehalose biosynthesis, enzyme is essential for embryo maturation
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
step in trehalose biosynthesis
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
Q1KLW0
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
C7EZF1
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
C7EZF1
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
Q1KLW0
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
step in trehalose biosynthesis
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
Q6IVK9
both TPS1 and TPS2 are required for high-temperature (37°C) growth and glycolysis but that the block at TPS2 results in the apparent toxic accumulation of trehalose-6-phosphate, which makes this enzyme a fungicidal target
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
Q6IVK9
both TPS1 and TPS2 are required for high-temperature (37°C) growth and glycolysis but that the block at TPS2 results in the apparent toxic accumulation of trehalose-6-phosphate, which makes this enzyme a fungicidal target
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
J7G8S5
-
-
-
?
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
Q9Y119
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
step in trehalose biosynthesis
-
-
?
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
Q66Q98
-
-
-
?
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
P31688, Q00764
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
step in trehalose biosynthesis
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
step in trehalose biosynthesis
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
step in trehalose biosynthesis
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
Q7WUI7
first step in one of 2 existing trehalose biosynthesis pathways, plays a role in osmoadaptation
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
Q7WUI7
first step in one of 2 existing trehalose biosynthesis pathways, plays a role in osmoadaptation
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
E1U2Z7, E1U2Z8, E1U2Z9, E1U300
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
A0A0B5WYD4
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
A4K8Z1, A4K8Z2
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
A4K8Z1, A4K8Z2
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
Q9HIW6
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
Q9SYM4
the enzyme is essential for Arabidopsis embryo development, TPS1 appears to play a vital role in responding to the increase in sucrose supply, which accompanies the onset of embryo maturation
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
AtTPS1 is a single-copy gene and is expressed constitutively at very low levels
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
trehalose-6-phosphate synthase A affects citrate accumulation by Aspergillus niger under conditions of high glycolytic flux
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
enzyme is osmotically inducible, mutants which are defective in the synthesis of the synthase have an impaired osmotic tolerance in glucose-mineral medium
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
TPS1-encoded trehalose-6-phosphate synthase exerts an essential control on the influx into glycolysis. Tps1-mediated protein-protein interactions are important for control of glucose influx into yeast glycolysis
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
key enzyme for biosynthesis of trehalose, the major soluble carbohydrate in resting cells
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
the enzyme plays a role in the control of glycolysis
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
key enzyme for biosynthesis of trehalose, the major soluble carbohydrate in resting cells
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
alpha,alpha-trehalose 6-phosphate synthase is dispensable for growth on glucose but not for spore germination
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
the enzyme does not play a role in the control of glycolysis
-
?
additional information
?
-
-
the enzyme, encoded by gen tps1, is a regulator of glucose, abscisic acid, and stress signaling, trehalose is an osmoprotectant, trehalose content in wild-type and transgenic plants, overview
-
-
-
additional information
?
-
-
TPS1 may play a major role in coordinating cell wall biosynthesis and cell division with cellular metabolism during embryo development
-
-
-
additional information
?
-
-
trehalose is able to protect the integrity of the cells against a variety of environmental stresses such as desiccation, dehydration, heat, cold, and oxidation, probably via reduction of protein denaturation through protein-trehalose interactions, the enzyme might be a radical scavenger
-
-
-
additional information
?
-
-
trehalose is able to protect the integrity of the cells against a variety of environmental stresses such as desiccation, dehydration, heat, cold, and oxidation, probably via reduction of protein denaturation through protein-trehalose interactions, in flying insects trehalose content is especially high in hemolymph and thorax muscles and is consumed during flight
-
-
-
additional information
?
-
-
trehalose acts as a global protectant against abiotic stress, accumulation of trehalose leads to increased salt, drought, and cold resistance in plants
-
-
-
additional information
?
-
-
trehalose is able to protect the integrity of the cells against a variety of environmental stresses such as desiccation, dehydration, heat, cold, and oxidation, probably via reduction of protein denaturation through protein-trehalose interactions
-
-
-
additional information
?
-
-
the trehalose-6-phosphate synthase/phosphatase (OtsA–OtsB) pathway plays an important role in the synthesis of trehalose in response to stress
-
-
-
additional information
?
-
-
trehalose is able to protect the integrity of the cells against a variety of environmental stresses such as desiccation, dehydration, heat, cold, and oxidation, probably via reduction of protein denaturation through protein-trehalose interactions, the enzyme might be a radical scavenger
-
-
-
additional information
?
-
-
trehalose is able to protect the integrity of the cells against a variety of environmental stresses such as desiccation, dehydration, heat, cold, and oxidation, probably via reduction of protein denaturation through protein-trehalose interactions
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
K+
KCl
-
upon an increase in the KCl concentration from 0 to 100 mM, the OtsA activity decreases by more than 40%, whereas it is not significantly affected when UDP or GDP-glucose is used as the substrate
Mg2+
Mn2+
NaCl
Zn2+
additional information
Co2+
1.91fold activation at 10 mM; the enzyme does not require divalent metal ions for catalysis, but Mg2+, Zn2+, Co2+ and Mn2+ can stimulate enzyme activity and maximal activation is found in the presence of Mg2+. 1.91fold activation by 10 mM Co2+
Mg2+
2.33fold activation at 10 mM; the enzyme does not require divalent metal ions for catalysis, but Mg2+, Zn2+, Co2+ and Mn2+ can stimulate enzyme activity and maximal activation is found in the presence of Mg2+. 2.33fold activation ba 10 mM Mg2+
Mn2+
1.16fold activation at 10 mM; the enzyme does not require divalent metal ions for catalysis, but Mg2+, Zn2+, Co2+ and Mn2+ can stimulate enzyme activity and maximal activation is found in the presence of Mg2+. 1.16fold activation by 10 mM Mn2+
NaCl
-
an increase in the concentration of NaCl from 0 to 100 mM leads to a decrease in the OtsA activity by more than 35% when ADP-glucose or TDP-glucose is the substrate. When UDP-glucose or GDP-glucose is used as substrate, the OtsA activity is increased by 10–30%
Zn2+
2.26fold activation at 10 mM; the enzyme does not require divalent metal ions for catalysis, but Mg2+, Zn2+, Co2+ and Mn2+ can stimulate enzyme activity and maximal activation is found in the presence of Mg2+. 2.26fold activation by 10 mM Zn2+
additional information
-
no or poor effects by CoCl2, CaCl2, BaCl2, and FeSO4
additional information
heparin in assays has no effect on the activity of recombinant OtsA1-His10
additional information
heparin in assays has no effect on the activity of recombinant OtsA1-His10
additional information
no effect by Li+ at 10 mM; the addition of monovalent metal ions Na+, K+ and Li+ has no effect on the enzyme activity
additional information
-
no effect by Li+ at 10 mM; the addition of monovalent metal ions Na+, K+ and Li+ has no effect on the enzyme activity
additional information
no requirement for divalent cations for activity
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
3-amino-4-formyl-2-[2-oxo-2-(tricyclo[3.3.1.13,7]dec-1-yl)ethyl]cyclopent-3-ene-1,1,2-tricarbonitrile
cathomycin
-
competitive inhibition, inhibits reaction with either UDPglucose or GDPglucose as glucosyl donor. Preincubation with heparin prevents inhibition. 0.05 mg/ml-0.2 mg/ml: 50% inhibition
circulin
-
noncompetitive inhibition, inhibits reaction with either UDPglucose or GDPglucose as glucosyl donor. Preincubation with heparin prevents inhibition. 0.05 mg/ml-0.2 mg/ml: 50% inhibition
Diumycin
-
competitive inhibition, inhibits reaction with either UDPglucose or GDPglucose as glucosyl donor. Preincubation with heparin prevents inhibition. 0.05 mg/ml: 50% inhibition
-
guanidine hydrochloride
10 mM, 63% inhibition; 37% inhibition
methyl 2-chloro-5-(5-[(Z)-[3-(2,4-dimethylphenyl)-4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene]methyl]furan-2-yl)benzoate
Moenomycin
-
competitive inhibition, inhibits reaction with either UDPglucose or GDPglucose as glucosyl donor. Preincubation with heparin prevents inhibition. Preincubation with heparin prevents inhibition. 0.05 mg/ml: 50% inhibition
O,O-diphenyl [(2E)-2-[2-(2-chlorophenyl)hydrazinylidene]-2-cyanoethanethioyl]phosphoramidothioate
Polyribonucleotide inhibitor from Mycobacterium tuberculosis
-
-
-
2,6-diamino-4-(2,4-dichlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(2,4-dichlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(2-methylphenyl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(2-methylphenyl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(3,4-dichlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(3,4-dichlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(3-bromophenyl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(3-chlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(3-chlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(3-fluorophenyl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(3-fluorophenyl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(3-iodophenyl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(4,5-dihydrofuran-3-yl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(4,5-dihydrofuran-3-yl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(4,5-dihydrothiophen-3-yl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(4,5-dihydrothiophen-3-yl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(4-bromo-5-ethylthiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(4-bromo-5-ethylthiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(4-bromo-5-methylthiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(4-bromo-5-methylthiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(4-bromothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(4-bromothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(4-chlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(4-chlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(4-methylphenyl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(4-methylphenyl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(4-nitrophenyl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(5-bromothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(5-bromothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(5-chlorothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(5-chlorothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(5-ethylthiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(5-ethylthiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(5-nitrothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(5-nitrothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(cyclohex-2-en-1-yl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(cyclohex-2-en-1-yl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(cyclohex-3-en-1-yl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-(cyclohex-3-en-1-yl)-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-[3-(trifluoromethyl)phenyl]-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-[3-(trifluoromethyl)phenyl]-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-[4-(trifluoromethyl)phenyl]-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-[4-(trifluoromethyl)phenyl]-4H-thiopyran-3,5-dicarbonitrile
-
3-amino-4-formyl-2-[2-oxo-2-(tricyclo[3.3.1.13,7]dec-1-yl)ethyl]cyclopent-3-ene-1,1,2-tricarbonitrile
-
3-amino-4-formyl-2-[2-oxo-2-(tricyclo[3.3.1.13,7]dec-1-yl)ethyl]cyclopent-3-ene-1,1,2-tricarbonitrile
-
6-amino-4-(3,4-dichlorophenyl)-2-thioxo-1,2,3,4-tetrahydropyridine-3,5-dicarbonitrile
-
6-amino-4-(3,4-dichlorophenyl)-2-thioxo-1,2,3,4-tetrahydropyridine-3,5-dicarbonitrile
-
8-chloro-11-(piperazin-1-yl)-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridine
-
8-chloro-11-(piperazin-1-yl)-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridine
-
methyl 2-chloro-5-(5-[(Z)-[3-(2,4-dimethylphenyl)-4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene]methyl]furan-2-yl)benzoate
-
methyl 2-chloro-5-(5-[(Z)-[3-(2,4-dimethylphenyl)-4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene]methyl]furan-2-yl)benzoate
-
NaCl
-
an increase in the concentration of NaCl from 0 to 100 mM leads to a decrease in the OtsA activity by more than 35% when ADP-glucose or TDP-glucose is the substrate. When UDP-glucose or GDP-glucose is used as substrate, the OtsA activity is increased by 10–30%
O,O-diphenyl [(2E)-2-[2-(2-chlorophenyl)hydrazinylidene]-2-cyanoethanethioyl]phosphoramidothioate
-
O,O-diphenyl [(2E)-2-[2-(2-chlorophenyl)hydrazinylidene]-2-cyanoethanethioyl]phosphoramidothioate
-
phosphate
-
enzyme is less sensitive to in vitro inhibition at 50°C than at 30°C. Fructose-6-phosphate partially relieves the inhibitory effect of phosphate at 30°C but not at 50°C
phosphate
-
noncompetitive with respect to noth UDPglucose or glucose 6-phosphate; potent noncompetitive inhibitor
additional information
-
inhibitor screening amongst over 115000 synthetic compounds, structure-function relationship analysis of 4-substituted 2,6-diamino-3,5-dicyano-4H-thiopyrans, overview
-
additional information
inhibitor screening amongst over 115000 synthetic compounds, structure-function relationship analysis of 4-substituted 2,6-diamino-3,5-dicyano-4H-thiopyrans, overview
-
additional information
inhibitor screening amongst over 115000 synthetic compounds, structure-function relationship analysis of 4-substituted 2,6-diamino-3,5-dicyano-4H-thiopyrans, overview
-
additional information
-
transglycosylase inhibitor is an oligonucleotide containing between 6 and 9 purine bases and no pyrimidine bases, noncompetitively inhibits the transglucosylase
-
additional information
-
no effect by sucrose and trehalose up to 0.4 M, no substrate and product inhibition
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Chondroitin
-
stimulation, particularly when a pyrimidine glucose nucleotide is used, rather than a purine glucose nucleotide
glycosyltransferase
the Thermoproteus tenax trehalose-6-phosphate synthase/phosphatase (TPSP) exhibits high phosphatase activity, but requires activation by the co-expressed glycosyltransferase for bifunctional synthase/phosphatase activity. The glycosyltransferase 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 TPSP enzyme. Activation is mediated by complex-formation in vivo
-
chondroitin sulfate
-
polyanions heparin and chondroitin sulfate stimulate TPS activity with different glucosyl donors
chondroitin sulfate
-
activation; chondroitin 4-sulfate, chondroitin 6-sulfate
chondroitin sulfate
maximal activation at 0.0005 mg; maximal stimulation at 400 ng
heparin
-
polyanions heparin and chondroitin sulfate stimulate TPS activity with different glucosyl donors
heparin
the activity of OtsA2-His10 is significantly increased, most of all when UDP-glucose is used as substrate
heparin
-
stimulation, particularly when a pyrimidine glucose nucleotide is used, rather than a purine glucose nucleotide. Heparin helps to retain both stability and activity of the final purified enzyme
heparin
0.006 mg, stimulates; heparin can stimulate the activity of the enzyme, although the activity decreases while the concentration of heparin is above 600 ng
RNA
-
various RNA, particularly that isolated from Mycobacterium smegmatis chondroitin sulfate, activate
additional information
increase of trehalose in the first 2-3 h of cold shock
-
additional information
-
dependence on polyanion concentrations for optimum TPS activity, overview
-
additional information
-
when pyrimidine sugar nucleotides are used as substrates, there is an almost absolute requirement for a high molecular weight polyanion for activity. When the purine sugar nucleotides are used as substrates fairly good enzymatic activity is observed in absence of a polyanion, this activity increases 2 to 4fold in the presence of optimum concentrations of polyanion. Activation by the polyanion is inhibited by high salt concentrations as well as by high concentrations of mononucleoside phosphates
-
additional information
-
the trehalose-6-phosphate synthase of Saccharomyces cerevisiae shows 1.76fold enhanced activity after specific methylation at a cysteine residue through 14 kDa cysteine methyltransferase from Saccharomyces cerevisiae
-
additional information
-
no effect by sucrose and trehalose up tp 0.4 M
-
additional information
the enzymatic activity can be stimulated by divalent metal ions and polyanions heparin and chondroitin sulfate
-
additional information
-
the enzymatic activity can be stimulated by divalent metal ions and polyanions heparin and chondroitin sulfate
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.34
D-glucose 6-phosphate
pH 6.0, 60°C, N-loop truncation mutant enzyme
0.8
D-glucose 6-phosphate
recombinant enzyme, pH 7.0, 80°C, in presence of Mg2+
3
D-glucose 6-phosphate
-
37°C, pH 5.5, cosubstrate: UDP-glucose
4.2
D-glucose 6-phosphate
-
37°C, pH 5.5, cosubstrate: ADP-glucose
5.3
D-glucose 6-phosphate
-
37°C, pH 5.5, cosubstrate: TDP-glucose
7.1
D-glucose 6-phosphate
-
37°C, pH 5.5, cosubstrate: GDP-glucose
7.5
glucose 6-phosphate
-
bifunctional fusion enzyme of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase
0.74
UDP-alpha-D-glucose
pH 6.0, 60°C, N-loop truncation mutant enzyme
0.5
UDP-glucose
recombinant enzyme, pH 7.0, 80°C, in presence of Mg2+
0.04
UDPglucose
-
in presence of optimal concentration of a polyanion
5.1
UDPglucose
-
bifunctional fusion enzyme of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase
additional information
additional information
-
complex bimodal kinetics
-
additional information
additional information
-
bifunctional fusion enzyme of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase
-
additional information
additional information
-
the high catalytic efficiency of OtsA results from the high affinity of the enzyme for uridine 5'-diphosphoglucose at low temperatures
-
additional information
additional information
the high catalytic efficiency of OtsA results from the high affinity of the enzyme for uridine 5'-diphosphoglucose at low temperatures
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Escherichia coli
-
bifunctional fusion enzyme of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase
-
3.2
glucose 6-phosphate
Escherichia coli
-
bifunctional fusion enzyme of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase
3.6
UDPglucose
Escherichia coli
-
bifunctional fusion enzyme of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Arthrobacter sp.
-
the high catalytic efficiency of OtsA results from the high affinity of the enzyme for uridine 5'-diphosphoglucose at low temperatures
2
additional information
additional information
Arthrobacter sp.
Q1KLW0
the high catalytic efficiency of OtsA results from the high affinity of the enzyme for uridine 5'-diphosphoglucose at low temperatures
2
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0008 - 0.1
2,6-diamino-4-(4-bromo-5-methylthiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
0.00371 - 0.00505
2,6-diamino-4-[3-(trifluoromethyl)phenyl]-4H-thiopyran-3,5-dicarbonitrile
0.0014 - 0.0046
3-amino-4-formyl-2-[2-oxo-2-(tricyclo[3.3.1.13,7]dec-1-yl)ethyl]cyclopent-3-ene-1,1,2-tricarbonitrile
0.0062 - 0.0066
8-chloro-11-(piperazin-1-yl)-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridine
0.0094 - 0.0147
methyl 2-chloro-5-(5-[(Z)-[3-(2,4-dimethylphenyl)-4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene]methyl]furan-2-yl)benzoate
0.0028 - 0.0055
O,O-diphenyl [(2E)-2-[2-(2-chlorophenyl)hydrazinylidene]-2-cyanoethanethioyl]phosphoramidothioate
0.1
2,6-diamino-4-(2,4-dichlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.1
2,6-diamino-4-(2,4-dichlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.1
2,6-diamino-4-(2-methylphenyl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.1
2,6-diamino-4-(2-methylphenyl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0002
2,6-diamino-4-(3,4-dichlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0005
2,6-diamino-4-(3,4-dichlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0012
2,6-diamino-4-(3-bromophenyl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0017
2,6-diamino-4-(3-bromophenyl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0012
2,6-diamino-4-(3-chlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0013
2,6-diamino-4-(3-chlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.005
2,6-diamino-4-(3-fluorophenyl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0061
2,6-diamino-4-(3-fluorophenyl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0026
2,6-diamino-4-(3-iodophenyl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0049
2,6-diamino-4-(3-iodophenyl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0918
2,6-diamino-4-(4,5-dihydrofuran-3-yl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.1
2,6-diamino-4-(4,5-dihydrofuran-3-yl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0631
2,6-diamino-4-(4,5-dihydrothiophen-3-yl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.1
2,6-diamino-4-(4,5-dihydrothiophen-3-yl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.1
2,6-diamino-4-(4-bromo-5-ethylthiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.1
2,6-diamino-4-(4-bromo-5-ethylthiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0008
2,6-diamino-4-(4-bromo-5-methylthiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.1
2,6-diamino-4-(4-bromo-5-methylthiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.004
2,6-diamino-4-(4-bromothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.011
2,6-diamino-4-(4-bromothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0045
2,6-diamino-4-(4-chlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0149
2,6-diamino-4-(4-chlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0129
2,6-diamino-4-(4-methylphenyl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0758
2,6-diamino-4-(4-methylphenyl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0287
2,6-diamino-4-(4-nitrophenyl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0419
2,6-diamino-4-(4-nitrophenyl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0045
2,6-diamino-4-(5-bromothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.023
2,6-diamino-4-(5-bromothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0059
2,6-diamino-4-(5-chlorothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0173
2,6-diamino-4-(5-chlorothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0665
2,6-diamino-4-(5-ethylthiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.1
2,6-diamino-4-(5-ethylthiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0054
2,6-diamino-4-(5-nitrothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0061
2,6-diamino-4-(5-nitrothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0026
2,6-diamino-4-(cyclohex-2-en-1-yl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0029
2,6-diamino-4-(cyclohex-2-en-1-yl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0031
2,6-diamino-4-(cyclohex-3-en-1-yl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0046
2,6-diamino-4-(cyclohex-3-en-1-yl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0014
2,6-diamino-4-cyclohexyl-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0019
2,6-diamino-4-cyclohexyl-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.1
2,6-diamino-4-phenyl-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
789
2,6-diamino-4-phenyl-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.00371
2,6-diamino-4-[3-(trifluoromethyl)phenyl]-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.00505
2,6-diamino-4-[3-(trifluoromethyl)phenyl]-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.1
2,6-diamino-4-[4-(trifluoromethyl)phenyl]-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.1
2,6-diamino-4-[4-(trifluoromethyl)phenyl]-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0014
3-amino-4-formyl-2-[2-oxo-2-(tricyclo[3.3.1.13,7]dec-1-yl)ethyl]cyclopent-3-ene-1,1,2-tricarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0046
3-amino-4-formyl-2-[2-oxo-2-(tricyclo[3.3.1.13,7]dec-1-yl)ethyl]cyclopent-3-ene-1,1,2-tricarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.1
6-amino-4-(3,4-dichlorophenyl)-2-thioxo-1,2,3,4-tetrahydropyridine-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.1
6-amino-4-(3,4-dichlorophenyl)-2-thioxo-1,2,3,4-tetrahydropyridine-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0062
8-chloro-11-(piperazin-1-yl)-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridine
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0066
8-chloro-11-(piperazin-1-yl)-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridine
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0086
8-hydroxy-2,4-dimethyl-7H-chromen-7-one
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0314
8-hydroxy-2,4-dimethyl-7H-chromen-7-one
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0094
methyl 2-chloro-5-(5-[(Z)-[3-(2,4-dimethylphenyl)-4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene]methyl]furan-2-yl)benzoate
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0147
methyl 2-chloro-5-(5-[(Z)-[3-(2,4-dimethylphenyl)-4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene]methyl]furan-2-yl)benzoate
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0028
O,O-diphenyl [(2E)-2-[2-(2-chlorophenyl)hydrazinylidene]-2-cyanoethanethioyl]phosphoramidothioate
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0055
O,O-diphenyl [(2E)-2-[2-(2-chlorophenyl)hydrazinylidene]-2-cyanoethanethioyl]phosphoramidothioate
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.01
-
preparation of trehalose-6-phosphate synthase from Saccharomyces cerevisiae, preparation step soluble supernatant
0.011
-
TPS specific activity in glucose, yeast mutant strain tps2delta + pSAL4
0.013
-
TPS specific activity in galactose, yeast mutant strain tps1delta_tps2delta + pSAL4::TPS1
0.02
-
TPS specific activity in glucose, yeast mutant strain tps1delta_tps2delta + pSAL4::TPS1
0.063
-
TPS specific activity in galactose, yeast mutant strain tps2delta + pSAL4::TPS2
0.067
-
TPS specific activity in glucose, yeast mutant strain tps2delta + pSAL4::TPS2
0.073
-
TPS specific activity in glucose, yeast mutant strain tps2delta + pSAL4::TPS1-TPS2
0.078
-
TPS specific activity in galactose, yeast mutant strain tps2delta + pSAL4::TPS1-TPS2
0.081
-
TPS specific activity in galactose, yeast mutant strain tps1delta + pSAL4::TPS1-TPS2
0.086
-
TPS specific activity in glucose, yeast mutant strain tps1delta + pSAL4::TPS1-TPS2
0.088
-
TPS specific activity in galactose, yeast mutant strain tps1delta_tps2delta + pSAL4::TPS1-TPS2
0.093
-
TPS specific activity in glucose, yeast mutant strain tps1delta_tps2delta + pSAL4::TPS1-TPS2
0.144
-
TPS specific activity in glucose, yeast mutant strain tps1delta + pSAL4::TPS1
0.163
-
TPS specific activity in galactose, yeast mutant strain tps1delta + pSAL4::TPS1
0.49
-
preparation of trehalose-6-phosphate synthase from Saccharomyces cerevisiae, preparation step ammonimum sulfate fractionation
0.74
-
preparation of trehalose-6-phosphate synthase from Saccharomyces cerevisiae, preparation step HPGPLC on TSK G2000SW
1.58
7.33
purified recombinant enzyme, pH 6.0, 60°C, substrate UDP-glucose
20.6
purified recombinant enzyme, substrates GDP-glucose and D-glucose 6-phosphate
95
purified recombinant enzyme, substrates ADP-glucose and D-glucose 6-phosphate
106.7
purified recombinant enzyme, substrates TDP-glucose and D-glucose 6-phosphate
149.6
purified recombinant enzyme, substrates UDP-glucose and D-glucose 6-phosphate
150.5
purified native enzyme, pH 4.0, 37°C; purified native enzyme, pH 4.0, 37°C
additional information
1.58
-
preparation of trehalose-6-phosphate synthase from Saccharomyces cerevisiae, preparation step HPGPLC on HiLoad 16/60 Superdex 200
additional information
-
TPS activity is maximally at pH 8.5 with 2.11 U/mg, followed by 2.01 U/mg at pH 9.0, 1.93 U/mg at pH 9.5, and 1.21 U/mg at pH 10.5, but only 0.31 U/mg at pH 4.5
additional information
-
the activity of trehalose-6-phosphate synthase is concentration dependent
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.3
-
activity with ADP-glucose, UDP-glucose and TDP-glucose
6.5
7.5
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 10.5
-
TPS activity is maximally at pH 8.5 with 2.11 U/mg, followed by 2.01 U/mg at pH 9.0, 1.93 U/mg at pH 9.5, and 1.21 U/mg at pH 10.5, but only 0.31 U/mg at pH 4.5
5 - 6
-
pH 5.0: about 85% of maximal activity, pH 6.0: about 50% of maximal activity
5 - 7
pH 5.0: about 50% of maximal activity, pH 7.0: about 50% of maximal activity
5.5 - 8
-
pH 5.5: about 75% of maximal activity, pH 8.0: about 70% of maximal activity
6 - 8
drastic decrease in enzyme activity is observed at pH values below pH 6.0 and above pH 8.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
30 - 40
-
bifunctional fusion enzyme of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase
35
37
40
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 20
catalytic activity of OtsA at 4°C is 1.2fold greater than that at 20°C
20 - 60
activity range, at 40°C, the enzyme demonstrates 87.04% of its maximum activity. A rapid decrease in the enzyme activity occurs at 50°C with 35.27% of maximum activity, completely loss of activity above 60°C; activity range, at 40°C, the enzyme demonstrates 87.04% of its maximum activity. A rapid decrease in the enzyme activity occurs at 50°C with 35.27% of maximum activity, completely loss of activity above 60°C
20 - 50
drastic decrease in enzyme activity is observed at temperatures below 20°C and above 50°C
40 - 100
about half-maximal activity at 40°C, 80% of maximal activity at 100°C, inactive at 30°C
50 - 80
50°C: about 50% of maximal activity, 80°C: about 75% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
in both males and females, the darker muscles exhibit greater amounts of trehalose, trehalose 6-phosphate synthase, and trehalase activities than the light colored; in both males and females, the darker muscles exhibit greater amounts of trehalose, trehalose 6-phosphate synthase, and trehalase activities than the light colored; in both males and females, the darker muscles exhibit greater amounts of trehalose, trehalose 6-phosphate synthase, and trehalase activities than the light colored; in both males and females, the darker muscles exhibit greater amounts of trehalose, trehalose 6-phosphate synthase, and trehalase activities than the light colored
correlation between TPS activity in hemocytes and hemolymph trehalose levels is found during the molt cycle
additional information
expression of GbTPS is up-regulated by cold, NaCl, mannitol and drought treatments
expression of GbTPS is up-regulated by cold, NaCl, mannitol and drought treatments
additional information
-
bdelloids show low tps gene expression levels, but strong overexpression of the TPS genes is observed when bdelloids enter desiccation. Quantitative expression analysis
additional information
-
expression of AtTPS1 is low and not organ specific
additional information
-
gene AtTPS1 is widely expressed throughout the plant
additional information
-
gene AtTPS1 is widely expressed throughout the plant
-
additional information
-
ubiquitous expression of CasTPS in most tissues; ubiquitous expression of CasTPS in most tissues; ubiquitous expression of CasTPS in most tissues; ubiquitous expression of CasTPS in most tissues
additional information
ubiquitous expression of CasTPS in most tissues; ubiquitous expression of CasTPS in most tissues; ubiquitous expression of CasTPS in most tissues; ubiquitous expression of CasTPS in most tissues
additional information
ubiquitous expression of CasTPS in most tissues; ubiquitous expression of CasTPS in most tissues; ubiquitous expression of CasTPS in most tissues; ubiquitous expression of CasTPS in most tissues
additional information
ubiquitous expression of CasTPS in most tissues; ubiquitous expression of CasTPS in most tissues; ubiquitous expression of CasTPS in most tissues; ubiquitous expression of CasTPS in most tissues
additional information
ubiquitous expression of CasTPS in most tissues; ubiquitous expression of CasTPS in most tissues; ubiquitous expression of CasTPS in most tissues; ubiquitous expression of CasTPS in most tissues
additional information
activity of trehalose-6-phosphate synthase during larval-pupal development is significantly higher in diapause-type individuals than in nondiapause individuals and is closely correlated with the changes in the trehalose content. mRNA is detected at high levels in the late stage of sixth larval instar and the early middle stage of diapause-destined pupae
additional information
-
activity of trehalose-6-phosphate synthase during larval-pupal development is significantly higher in diapause-type individuals than in nondiapause individuals and is closely correlated with the changes in the trehalose content. mRNA is detected at high levels in the late stage of sixth larval instar and the early middle stage of diapause-destined pupae
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
the enzyme is markedly present in the vacuole and the cell wall, and to a lesser extent in the cytosol of transgenic Nicotiana tabacum
-
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PDB
SCOP
CATH
ORGANISM
UNIPROT
Burkholderia multivorans (strain ATCC 17616 / 249)
Burkholderia vietnamiensis (strain G4 / LMG 22486)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Candida albicans (strain SC5314 / ATCC MYA-2876)
Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 / CBS 10515 / FGSC 9487)
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
33000
x * 81000, TPSP holoenzyme, x * 50000, isolated trehalose-6-phosphate synthase domain, x * 33000, isolated trehalose-6-phosphate phophatase domain
50000
x * 81000, TPSP holoenzyme, x * 50000, isolated trehalose-6-phosphate synthase domain, x * 33000, isolated trehalose-6-phosphate phophatase domain
55000
-
x * 55000, isozyme TPS1, x * 100000, isozyme TPS2, x * 105000, isozyme TPS3, SDS-PAGE
57000
-
x * 115000 + x * 57000, complex of EC 2.4.1.15/EC 3.1.3.12, SDS-PAGE
58000
59000
-
estimated by HPGPLC using a Ultropak G2000SW column and by SDS-PAGE
60000
81000
x * 81000, TPSP holoenzyme, x * 50000, isolated trehalose-6-phosphate synthase domain, x * 33000, isolated trehalose-6-phosphate phophatase domain
100000
105000
-
x * 55000, isozyme TPS1, x * 100000, isozyme TPS2, x * 105000, isozyme TPS3, SDS-PAGE
115000
additional information
-
3 aggregation forms of 230, 440, and 660 kDa contain polypeptides of 50, 67, and 115 kDa polypeptides, only the 440 kDa form is catalytically active, native PAGE
100000
-
x * 55000, isozyme TPS1, x * 100000, isozyme TPS2, x * 105000, isozyme TPS3, SDS-PAGE
115000
-
x * 115000 + x * 57000, complex of EC 2.4.1.15/EC 3.1.3.12, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
oligomer
-
x * 115000 + x * 57000, complex of EC 2.4.1.15/EC 3.1.3.12, SDS-PAGE
tetramer
additional information
?
-
x * 55000, isozyme TPS1, x * 100000, isozyme TPS2, x * 105000, isozyme TPS3, SDS-PAGE; x * 56200, calculation from nucleotide sequence
?
-
x * 55000, isozyme TPS1, x * 100000, isozyme TPS2, x * 105000, isozyme TPS3, SDS-PAGE; x * 56200, calculation from nucleotide sequence
-
?
x * 81000, TPSP holoenzyme, x * 50000, isolated trehalose-6-phosphate synthase domain, x * 33000, isolated trehalose-6-phosphate phophatase domain
?
-
x * 81000, TPSP holoenzyme, x * 50000, isolated trehalose-6-phosphate synthase domain, x * 33000, isolated trehalose-6-phosphate phophatase domain
-
?
-
x * 81000, TPSP holoenzyme, x * 50000, isolated trehalose-6-phosphate synthase domain, x * 33000, isolated trehalose-6-phosphate phophatase domain
-
additional information
-
isozyme domain structure, overview; isozyme domain structure, overview; isozyme domain structure, overview. The isozyme 1b encodes both a putative TPS and a TPP domain in tandem; isozyme domain structure, overview. The isozyme 1 encodes both a putative TPS and a TPP domain in tandem
additional information
isozyme domain structure, overview; isozyme domain structure, overview; isozyme domain structure, overview. The isozyme 1b encodes both a putative TPS and a TPP domain in tandem; isozyme domain structure, overview. The isozyme 1 encodes both a putative TPS and a TPP domain in tandem
additional information
isozyme domain structure, overview; isozyme domain structure, overview; isozyme domain structure, overview. The isozyme 1b encodes both a putative TPS and a TPP domain in tandem; isozyme domain structure, overview. The isozyme 1 encodes both a putative TPS and a TPP domain in tandem
additional information
isozyme domain structure, overview; isozyme domain structure, overview; isozyme domain structure, overview. The isozyme 1b encodes both a putative TPS and a TPP domain in tandem; isozyme domain structure, overview. The isozyme 1 encodes both a putative TPS and a TPP domain in tandem
additional information
isozyme domain structure, overview; isozyme domain structure, overview; isozyme domain structure, overview. The isozyme 1b encodes both a putative TPS and a TPP domain in tandem; isozyme domain structure, overview. The isozyme 1 encodes both a putative TPS and a TPP domain in tandem
additional information
-
Tps1p subunit exhibits TPS catalytic activity in the absence of other TPS complex proteins
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
side-chain modification
side-chain modification
-
the trehalose-6-phosphate synthase of Saccharomyces cerevisiae shows 1.76fold enhanced activity after specific methylation at a cysteine residue through 14 kDa cysteine methyltransferase from Saccharomyces cerevisiae
side-chain modification
-
the trehalose-6-phosphate synthase of Saccharomyces cerevisiae shows 1.76fold enhanced activity after specific methylation at a cysteine residue through 14 kDa cysteine methyltransferase from Saccharomyces cerevisiae
-
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme complexed with either substrate UDP-glucose or the inactive substrate analogue UDP-2-deoxy-2-fluoroglucose, hanging drop vapour diffusion method, 100 nl droplets of 10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, and 200 mM NaCl, with either 25 mM UDP-glucose and 50 mM 1-deoxy-glucose 6-phosphate or 25 mM UDP-2-deoxy-2-fluoroglucose and 20 mM glucose 6-phosphate, precipitant solution: 30% w/v PEG 4000, 200 mM ammonium acetate, 100 mM Tris-HCl, pH 8.0, 36 h, 25% ethylene glycol as cryoprotectant, X-ray diffraction structure determination and analysis at 2.0 A resolution
-
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
the three fractions (aggregates of trehalose 6-phosphate synthase) elute from ion exchange chromatography are stable in a pH 5–11 range
675977
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
heparin helps to retain both stability and activity of the final purified enzyme
-
in phosphate or acetate buffers, the activity of TpS1 is decreased to 25% and 30%, respectively, of activity in Tris-HCl buffer
stabilization during purification, 10fold by addition of 20 mM MgCl2, 50 mM NaCl, 2 M glycine betaine and 5 mM mercaptoethanol
-
stable to dialysis against either water or 0.1 M Tris-maleate buffer, pH 7.0
-
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C, recombinant His10-tagged isozyme OtsA2 gel filtration pool for 7 days yields 76% of its initial activity
-20°C, recombinant His10-tagged isozyme OtsA2 gel filtration pool loses its activity after thawing
4-6°C, 2 d, enzyme retains 75% of its activity after 2 d and 25% of its activity after 3 d
-
4°C, purified recombinant His10-tagged isozyme OtsA1almost loses its entire activity overnight
4°C, purified recombinant His10-tagged isozyme OtsA2 keeps a stable activity over several days
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Arabidopsis thaliana extracts are prepared, AtTPS1 expressed in yeast is analysed in yeast extracts
-
bifunctional fusion enzyme of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase
-
crude extract is prepared, the enzyme is isolated by ammonium sulfate fractionation and high performance gel permeation liquid chromatography, using a HiLoad 16/60 Superdex 200 and a Ultropak TSK G2000SW column
-
glutathione-S-transferase-Tps1p fusion protein expressed in E. coli
-
heparin helps to retain both stability and activity of the final purified enzyme
-
native enzyme 22.1fold to homogeneity by several gel filtration steps
-
native enzyme 50fold by ammonium sulfate fractionation, gel filtration, and nickel-resin affinity chromatography
-
native enzyme from female worm muscle 265fold by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration; native enzyme from female worm muscle 265fold by ammonium sulfate fractionation, anion exchange chromatography, and gel filtration
partial
recombinant His-tagged TPS1 from Escherichia coli strain BL21 by nickel affinity chromatography
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain B21(DE3) by nickel affinity chromatography
recombinant His10-tagged isozyme from Escherichia coli strain BL21 CodonPlus(DE3)-RP by nickel affinity chromatography, ultrafiltration, tag cleavage by Factor Xa; recombinant His10-tagged isozyme from Escherichia coli strain BL21 CodonPlus(DE3)-RP by nickel affinity chromatography, ultrafiltration, tag cleavage by Factor Xa
recombinant soluble MalE-CfTPS fusion protein from Escherichia coli Rosetta (DE3) cells partially by by amylose-agarose affinity chromatography
separation of three aggregates of trehalose 6-phosphate synthase (molecular weights of 624000 Da, 224000 Da and 107000 Da) by gel filtration and ion exchange chromatography
-
trehalose-6-phosphate synthase/phosphatase complex, EC 2.4.1.15/EC 3.1.3.12
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
11 TPS genes, class I AtTPS1-AtTPS4 and class II AtTPS5-AtTPS11. Expression of genes AtTPS2 or AtTPS4 enables the yeast tps1DELTA tps2DELTA mutant to grow on glucose and accumulate trehalose 6-phosphate and trehalose. Class II TPS genes do not complement the yeast mutant
-
; gene TA1210, DNA and amino acid sequence determination and analysis, sequence comparison, recombinant expression in Escherichia coli strains DH5alpha and BL21-CodonPlus (DE3)-RIL
a translational trehalose-6-phosphate synthase - trehalose-6-phosphate phosphatase, TPS-TPP, gene-fusion is constructed and subcloned into the pBluescript SK vector, into the yeast expression vector pSal4, and into the pBin19 vector for transformation of Arabidopsis thaliana
-
Agrobacterium tumefaciens-mediated transformation of Nicotiana tabacum. The enzyme is markedly present in the vacuoles and the cell wall, and to a lesser extent in the cytosol
-
construction of a bifunctional fusion enzyme of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase and expression in Escherichia coli
-
construction of a new transformation vector containing the AtTPS1 gene as a selection marker. Overexpression of AtTPS1 in tobacco allows selecting glucose insensitive transgenic shoots
-
DNA and amino acid sequence determination and analysis, overexpression in transgenic flies, functional expression in HEK-293 cells
-
expression in Escherichia coli
expression of glutathione-S-transferase-Tps1p fusion protein in Escherichia coli
-
expression of the TPS1 gene in transgenic Solanum tuberosum, usage of potato wild-type drought-sensitive cultivar White Lady; expression of the TPS1 gene in transgenic Solanum tuberosum, usage of potato wild-type drought-sensitive cultivar White Lady
expression of TPS1 driven by the ABI3 promoter rescues the severe embryo phenotype but not the vegetative phenotype of tps1
-
functional expression of the enzyme as a fusion protein with Escherichia coli trehalose-6-phosphate phosphatase in transgenic Oryza sativa plants
-
functional expression of the enzyme as a fusion protein with Escherichia coli trehalose-6-phosphate phosphatase in transgenic Oryza sativa plants, expression in human fibroblasts
-
gene cftps, DNA and amino acid sequence determination and anaysis, phylogenetic analysis, expression of largely soluble MalE-CfTPS fusion protein in Escherichia coli Rosetta (DE3) cells
gene dmtps1, phylgenetic analysis, expression of His-tagged TPS1 in Escherichia coli strain BL21
gene otsA, cloned from genetic library, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli strain BL21
gene otsA, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain B21(DE3)
gene otsA1, DNA and amino acid sequence determination and analysis, phylogenetic analysis, cloning in Escherichia coli strain DH5alpha, recombinant expression as His10-tagged isozyme in Escherichia coli strain BL21 CodonPlus(DE3)-RP; gene otsA2, DNA and amino acid sequence determination and analysis, , phylogenetic analysis, cloning in Escherichia coli strain DH5alpha, recombinant expression as His10-tagged isozyme in Escherichia coli strain BL21 CodonPlus(DE3)-RP
gene RoTPS1, DNA and amino acid sequence determination and analysis, sequence comparisons, cloning in Escherichia coli strain DH5alpha, recombinant expression in Saccharomyces cerevisiae strain YSH 290 and secretion of the recombinant enzyme
gene tps, a single copy, genetic structure, DNA and amino acid sequence determination and analysis, wild-type realtime PCR expression and promoter region analysis, expression in Saccharomyces cerevisiae tps1DELTA mutant YSH290 strain leading to no functional complementation
gene tps, four copies, DNA and amino acid sequence determination and analysis, phylogenetic analysis and tree, quantitative reverse transcriptase PCR enzyme expression analysis and profile
-
gene tps1, DNA and amino acid sequence determination and analysis, phylogenetic analysis; gene tps2, DNA and amino acid sequence determination and analysis, phylogenetic analysis
gene TPS1, Saccharomyces cerevisiae strain 10151 is used as host strain for transformation and overexpression, strains EP-1 and 14801 are used for preparing chromosomal DNAs
-
into the pDONOR207 vector and after confirming the sequence subcloned into the pBIN-GW binary vector, into the expression vector pYES2, for transformation of yeast cells
isozyme TPS1a, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenic analysis, the full-length cDNA sequence of four structural isoforms of trehalose-6-phosphate synthase (TPS) is isolated fromchela muscles of an adult female crab. Two isoforms of Callinectes sapidus TPS encode functional domains of TPS and trehalose-6-phosphorylase, TPP, EC 2.4.1.216, in tandem as a fused gene product of Escherichia coli Ost A and Ost B. The other two isoforms contain only a single TPS domain. Quantitative RT-PCR isozyme expression analysis; isozyme TPS1b, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenic analysis, the full-length cDNA sequence of four structural isoforms of trehalose-6-phosphate synthase (TPS) is isolated fromchela muscles of an adult female crab. Two isoforms of Callinectes sapidus TPS encode functional domains of TPS and trehalose-6-phosphorylase, TPP, EC 2.4.1.216, in tandem as a fused gene product of Escherichia coli Ost A and Ost B. The other two isoforms contain only a single TPS domain. Quantitative RT-PCR isozyme expression analysis; isozyme TPS1c, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenic analysis, the full-length cDNA sequence of four structural isoforms of trehalose-6-phosphate synthase (TPS) is isolated fromchela muscles of an adult female crab. Two isoforms of Callinectes sapidus TPS encode functional domains of TPS and trehalose-6-phosphorylase, TPP, EC 2.4.1.216, in tandem as a fused gene product of Escherichia coli Ost A and Ost B. The other two isoforms contain only a single TPS domain. Quantitative RT-PCR isozyme expression analysis; isozyme TPS1, DNA and amino acid sequence determination and analysis, sequence comparison and phylogenic analysis, the full-length cDNA sequence of four structural isoforms of trehalose-6-phosphate synthase (TPS) is isolated fromchela muscles of an adult female crabl. Two isoforms of Callinectes sapidus TPS encode functional domains of TPS and trehalose-6-phosphorylase, TPP, EC 2.4.1.216, in tandem as a fused gene product of Escherichia coli Ost A and Ost B. The other two isoforms contain only a single TPS domain. Quantitative RT-PCR isozyme expression analysis
overexpression in Arabidopsis thaliana plants under control of the 35S promotor
-
overexpression of the enzyme incresases stress resistance of yeast cells
-
preparation of a recombinant strain carrying multiple copies of ggsA by cotransformation
-
the shuttle vectors pSAL4 and pSAL6, the YEplac195/KanMX plasmid, and the two-hybrid plasmids pGBT9 and pGAD242 are used, GFP-fusions are generated using pK7GWF2 and pHGWR2
-
the TPS1 gene of Saccharomyces cerevisiae is cloned into pBluescript II SK, in addition a binary vector for transformation of potato plants is constructed
-
transgenic Arabidopsis plants with T6P levels increased by expression of T6P synthase or decreased by expression of T6P phosphatase in the cytosol. Compared with wild type, leaves of T6P synthase-expressing plants have increased redox activation of ADP-glucose pyrophosphorylase and increased starch
-
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
a transitory increase in the expression of TPS2 and TPS1 genes is promoted in wild-type cells inresponse to acute, but not to gentleoxidative exposure
-
both low temperature and accumulation of trehalose can inhibit OtsA expression, increase of trehalose in the first 2.3 h of cold shock
lipopolysaccharide treatment results in increase in expression, enzyme activity, and hemolymph trehalose levels
with the increase of the salt concentration in the medium, the expression of DvTPS has a slight decrease of 17% in 5 M NaCl compared with 0.5 M condition
both low temperature and accumulation of trehalose can inhibit OtsA expression, increase of trehalose in the first 2.3 h of cold shock
both low temperature and accumulation of trehalose can inhibit OtsA expression, increase of trehalose in the first 2.3 h of cold shock
-
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D156G
-
site-directed mutagenesis of a catalytic site residue, catalytically inactive Tps1 mutant variant
additional information
additional information
-
enzyme-deficient mutant embryos develop more slowly than the wild-type, and do not progress past the torpedo stage to cotyledon stage, overview
additional information
-
transgenic plants overexpressing the intrinsic enzyme display higher dehydration resistance and a slightly increased trehalose level, but no other phenotype alterations, transgenic seedling are glucose- and abscisic-acid stress insensitive and are larger than wild-type seedlings, overview
additional information
-
hemizygous TPS1/tps1 plants are transformed with an ABI3::AtTPS1 cDNA, ABI3 promoter drives expression in developing and germinating seeds but not thereafter, the ABI3::TPS1 complemented tps1 plantlets accumulate sugars and starch, transcripts associated with carbohydrate metabolism are altered and ABA-responsive transcripts are constitutively induced in ABI3::TPS1 tps1 plantlets, phenotypes, overview
additional information
-
construction of N-loop exchange mutations of the otsA gene, the mutants show altered catalytic efficiencies at temperatures from 16 to 37°C compared to the wild-type enzyme, overview
additional information
construction of N-loop exchange mutations of the otsA gene, the mutants show altered catalytic efficiencies at temperatures from 16 to 37°C compared to the wild-type enzyme, overview
additional information
-
construction of N-loop exchange mutations of the otsA gene, the mutants show altered catalytic efficiencies at temperatures from 16 to 37°C compared to the wild-type enzyme, overview
-
additional information
-
expression of TPSP in Saccharomyces cerevisiae is able to restore the growth on glucose of both Saccharomyces tps1Delta and tps1Delta tps2Delta mutants as well as the thermotolerance of the tps2Delta mutant
additional information
-
overexpression of the enzyme in flies increases their tolerance to anoxia and shortens the recovery time
additional information
-
construction of transgenic Oryza sativa plants expressing the catalytically active enzyme as a fusion protein with trehalose-6-phosphate phosphatase of Escherichia coli under control of the ubiquitin promotor from Zea mays, the transgenic plants produce high levels of trehalose in seeds and leaves, carbohydrate profile of seeds, but not of leaves, is altered, plants show no growth inhibition or altered phenotype
additional information
-
construction of transgenic Oryza sativa plants expressing the catalytically active enzyme as a fusion protein with trehalose-6-phosphate phosphatase of Escherichia coli under control of the ubiquitin promotor from Zea mays, the transgenic plants produce high levels of trehalose in seeds and leaves, carbohydrate profile of seeds, but not of leaves, is altered, plants show no growth inhibition or altered phenotype, expression in human fibroblasts renders the cells less sensitive to drought compared to wild-type cells
additional information
-
activity of T6P synthase and the accumulation of trehalose during ethanol fermentation are significantly improved by overexpression of TPS1, and especially at 38°C cmpared to 30°C, no obvious difference occurs in the activity of T6P synthase and the trehalose concentration for wild-type strain 10151, and transformed strains 10151-URA3 and 10151-pI-RED1, indicating that the expression of URA3 and YAP1 genes, markers of the expression plasmid, does not affect the synthesis of trehalose
additional information
transgenic Solanum tunerosum plants expressing the yeast TPS1 gene show enhanced drought tolerance, 379 genes of known function in potato show at least a 2fold change in expression across genotypes, stress levels or the interaction between these factors, wild-type leaves have twice as many genes with altered expression in response to stress than TPS1 transgenic leaves, the transgenic and wildtype plants show different contents in sugar metabolites in leaves under drought conditions, four transcription factors are uniquely up-regulated in TPS1 transgenic leaves, phenotypes, overview. Microarray transcriptional and metabolic analysis of the transgenic, drought-tolerant potato line; transgenic Solanum tunerosum plants expressing the yeast TPS1 gene show enhanced drought tolerance, 379 genes of known function in potato show at least a 2fold change in expression across genotypes, stress levels or the interaction between these factors, wild-type leaves have twice as many genes with altered expression in response to stress than TPS1 transgenic leaves, the transgenic and wildtype plants show different contents in sugar metabolites in leaves under drought conditions, four transcription factors are uniquely up-regulated in TPS1 transgenic leaves, phenotypes, overview. Microarray transcriptional and metabolic analysis of the transgenic, drought-tolerant potato line
additional information
-
construction of a tps1DELTA and a tps1-156 deletion mutant
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
agriculture
analysis
-
trehalose-6-phosphate synthase is an intrinsic selection marker for plant transformation
drug development
medicine
-
the enzyme should be a valuable target for chemotherapeutic intervention in tuberculosis
agriculture
-
the results demonstrate that engineering trehalose metabolism with a yeast TPS-TPP bifunctional enzyme confers multiple stress protection in plants, comprising a potential tool to improve stress-tolerance in crops
agriculture
a new strategy to increase drought tolerance and yield in legumes by overexpressing trehalose-6-phosphate synthase in the symbiotic bacterium Rhizobium etli is shown
drug development
TPS is a potential insecticidal molecular target, 4-substituted 2,6-diamino-3,5-dicyano-4H-thiopyrans may serve as lead compounds for the development of insecticides with a distinct mode of action
drug development
TPS is a potential insecticidal molecular target, 4-substituted 2,6-diamino-3,5-dicyano-4H-thiopyrans may serve as lead compounds in for the development of insecticides with a distinct mode of action
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LINKS TO OTHER DATABASES (specific for EC-Number 2.4.1.15)
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