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ADP-alpha-D-glucose + D-glucose 6-phosphate
ADP + alpha,alpha-1,1-trehalose 6-phosphate
ADP-alpha-D-glucose + D-glucose 6-phosphate
ADP + alpha,alpha-trehalose 6-phosphate
ADP-glucose + D-glucose 6-phosphate
ADP + alpha,alpha-trehalose 6-phosphate
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
CDP-glucose + D-glucose 6-phosphate
trehalose 6-phosphate + CDP
dTDP-glucose + glucose 6-phosphate
trehalose 6-phosphate + dTDP
-
-
-
-
?
GDP-alpha-D-glucose + D-glucose 6-phosphate
GDP + alpha,alpha-1,1-trehalose 6-phosphate
GDP-alpha-D-glucose + D-glucose 6-phosphate
GDP + alpha,alpha-trehalose 6-phosphate
GDP-glucose + D-glucose 6-phosphate
trehalose 6-phosphate + GDP
GDP-glucose + glucose 6-phosphate
GDP + alpha,alpha-trehalose 6-phosphate
cf. EC 2.4.1.36
-
-
?
TDP-alpha-D-glucose + D-glucose 6-phosphate
TDP + alpha,alpha-1,1-trehalose 6-phosphate
-
-
-
-
?
TDP-alpha-D-glucose + D-glucose 6-phosphate
TDP + alpha,alpha-trehalose 6-phosphate
TDP-glucose + glucose 6-phosphate
trehalose 6-phosphate + TDP
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
-
-
?
UDP-alpha-D-glucose + D-fructose 6-phosphate
UDP + alpha,alpha-1,1-trehalose 6-phosphate
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
-
-
?
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-trehalose 6-phosphate
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
-
-
?
UDP-alpha-D-glucose + D-mannose 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-glucose + D-fructose 6-phosphate
UDP + ?
-
16% of the activity with D-glucose 6-phosphate
-
-
?
UDP-glucose + D-galactose
UDP + ?
-
17% of the activity with D-glucose 6-phosphate
-
-
?
UDP-glucose + D-glucose
UDP + ?
-
28% of the activity with D-glucose 6-phosphate
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
UDP-glucose + lactose
UDP + ?
-
10% of the activity with D-glucose 6-phosphate
-
-
?
UDP-glucose + sucrose
UDP + ?
-
19% of the activity with D-glucose 6-phosphate
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
additional information
?
-
ADP-alpha-D-glucose + D-glucose 6-phosphate
ADP + alpha,alpha-1,1-trehalose 6-phosphate
4% of the activity with UDP-glucose
-
-
?
ADP-alpha-D-glucose + D-glucose 6-phosphate
ADP + alpha,alpha-1,1-trehalose 6-phosphate
4% of the activity with UDP-glucose
-
-
?
ADP-alpha-D-glucose + D-glucose 6-phosphate
ADP + alpha,alpha-trehalose 6-phosphate
-
-
-
?
ADP-alpha-D-glucose + D-glucose 6-phosphate
ADP + alpha,alpha-trehalose 6-phosphate
-
ADP-glucose is the best donor substrate
-
-
?
ADP-alpha-D-glucose + D-glucose 6-phosphate
ADP + alpha,alpha-trehalose 6-phosphate
-
ADP-glucose is the best donor substrate
-
-
?
ADP-alpha-D-glucose + D-glucose 6-phosphate
ADP + alpha,alpha-trehalose 6-phosphate
-
13.4% of the activity with GDPglucose
-
-
?
ADP-alpha-D-glucose + D-glucose 6-phosphate
ADP + alpha,alpha-trehalose 6-phosphate
-
-
-
-
?
ADP-alpha-D-glucose + D-glucose 6-phosphate
ADP + alpha,alpha-trehalose 6-phosphate
-
-
-
-
?
ADP-alpha-D-glucose + D-glucose 6-phosphate
ADP + 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
-
-
?
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
-
-
?
ADP-alpha-D-glucose + D-glucose 6-phosphate
ADP + alpha,alpha-trehalose 6-phosphate
less effective than UDP-glucose
-
-
?
ADP-alpha-D-glucose + D-glucose 6-phosphate
ADP + alpha,alpha-trehalose 6-phosphate
less effective than UDP-glucose
-
-
?
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
-
-
?
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
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
CDP-glucose + D-glucose 6-phosphate
trehalose 6-phosphate + CDP
-
-
-
-
?
CDP-glucose + D-glucose 6-phosphate
trehalose 6-phosphate + CDP
-
-
-
-
?
GDP-alpha-D-glucose + D-glucose 6-phosphate
GDP + alpha,alpha-1,1-trehalose 6-phosphate
23% of the activity with UDP-glucose
-
-
?
GDP-alpha-D-glucose + D-glucose 6-phosphate
GDP + alpha,alpha-1,1-trehalose 6-phosphate
23% of the activity with UDP-glucose
-
-
?
GDP-alpha-D-glucose + D-glucose 6-phosphate
GDP + alpha,alpha-1,1-trehalose 6-phosphate
-
-
-
-
?
GDP-alpha-D-glucose + D-glucose 6-phosphate
GDP + alpha,alpha-trehalose 6-phosphate
-
cf. EC 2.4.1.36
-
-
?
GDP-alpha-D-glucose + D-glucose 6-phosphate
GDP + alpha,alpha-trehalose 6-phosphate
-
cf. EC 2.4.1.36
-
-
?
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
-
-
?
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
-
18.4% of the activity with UDP-glucose
-
-
?
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
-
-
-
?
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
-
-
-
?
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
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
-
-
-
?
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
-
-
-
-
?
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
-
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
-
-
-
-
?
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-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-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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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
?
-
-
no substrates: fructose, fructose 6-phosphate, glucose, sucrose, and trehalose
-
-
?
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
?
-
-
GDP-alpha-D-glucose and ADP-alpha-D-glucose give little enzyme activity. Glucosamine 6-phosphate and fructose 6-phosphate have almost no enzyme activity, while mannose 6-phosphate exhibits little activity
-
-
-
additional information
?
-
-
GDP-alpha-D-glucose and ADP-alpha-D-glucose give little enzyme activity. Glucosamine 6-phosphate and fructose 6-phosphate have almost no enzyme activity, while mannose 6-phosphate exhibits little activity
-
-
-
additional information
?
-
-
the trehalose-6-phosphate synthase/phosphatase (OtsAOtsB) 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.
ADP-alpha-D-glucose + D-glucose 6-phosphate
ADP + alpha,alpha-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-trehalose 6-phosphate
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
additional information
?
-
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
-
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
-
-
-
?
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
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
-
-
-
-
?
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
-
-
-
-
?
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
-
-
-
?
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
-
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
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
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
-
-
-
?
UDP-alpha-D-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
-
-
-
?
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
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
-
-
-
?
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 (OtsAOtsB) 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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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-(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-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-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-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-chlorophenyl)-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-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-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-3-en-1-yl)-4H-thiopyran-3,5-dicarbonitrile
2,6-diamino-4-cyclohexyl-4H-thiopyran-3,5-dicarbonitrile
2,6-diamino-4-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-mercaptoethanol
10% (v/v), 9% inhibition; 91% inhibition
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
8-chloro-11-(piperazin-1-yl)-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridine
8-hydroxy-2,4-dimethyl-7H-chromen-7-one
Ag+
-
45% inhibition at 5 mM
AMP
-
10 mM 23% inhibition
Ba2+
10 mM, 38% inhibition; 38% inhibition at 10 mM
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
CDTA
-
0.08% residual activity at 2.5 mM
Cemusol NPT-12
-
weak 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
dithiothreitol
10 mM, 27% 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
-
EGTA
-
0.22% residual activity at 2.5 mM
ethanol
10% (v/v), 28% inhibition; 72% inhibition
Fe2+
-
slightly inhibitory
GDPglucose
-
noncompetitive to UDPglucose
glucose 6-phosphate
-
high concentrations
guanidine hydrochloride
10 mM, 63% inhibition; 37% inhibition
Isopropanol
10% (v/v), 14% inhibition; 86% inhibition
Li+
-
36.45% residual activity at 12.5 mM
methanol
10% (v/v), 30% inhibition; 70% 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
Mg2+
-
inhibition in presence of 1 mM UDP or 1 mM UTP
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
n-butanol
10% (v/v), 48% inhibition; 52% inhibition
Ni2+
10 mM, 21% inhibition; 21% inhibition at 10 mM
O,O-diphenyl [(2E)-2-[2-(2-chlorophenyl)hydrazinylidene]-2-cyanoethanethioyl]phosphoramidothioate
Polyribonucleotide inhibitor from Mycobacterium tuberculosis
-
-
-
Sodium azide
-
2.5 mM, 83% residual activity
Sodium citrate
-
93.98% residual activity at 2.5 mM
Triton X-100
-
weak inhibition
UDP
-
10 mM, 65% inhibition
UDPglucose
-
competitive to GDPglucose
UMP
-
10 mM, 43% inhibition
Urea
10 mM, 15% inhibition; 85% inhibition
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-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-(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-(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-cyclohexyl-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-cyclohexyl-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-phenyl-4H-thiopyran-3,5-dicarbonitrile
-
2,6-diamino-4-phenyl-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
-
8-hydroxy-2,4-dimethyl-7H-chromen-7-one
-
8-hydroxy-2,4-dimethyl-7H-chromen-7-one
-
Ca2+
-
-
Ca2+
-
40.28% residual activity at 12.5 mM
Cd2+
-
slightly inhibitory
Cd2+
-
40.28% residual activity at 12.5 mM
Citric acid
-
3.55% residual activity at 2.5 mM
Citric acid
-
2.5 mM, 82% residual activity
Cu2+
-
-
EDTA
-
EDTA
55% inhibition at 10 mM; 55% inhibition at 10 mM
EDTA
-
0.43% residual activity at 2.5 mM
EDTA
10 mM, 15% inhibition; 85% inhibition
Fe3+
32% inhibition at 10 mM; 32% inhibition at 10 mM
Fe3+
-
34.53% residual activity at 12.5 mM
K+
50% inhibition at 10 mM; 50% inhibition at 10 mM
K+
10% inhibition at 10 mM; 10 mM, 10% 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
-
methyl 2-chloro-5-(5-[(Z)-[3-(2,4-dimethylphenyl)-4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene]methyl]furan-2-yl)benzoate
-
N-ethylmaleimide
-
68% inhibition at 1 mM
N-ethylmaleimide
-
1 mM, 83% residual activity
Na+
-
21.1% residual activity at 12.5 mM
Na+
10 mM, 8% inhibition; 8% inhibition at 10 mM
NaCl
-
25 mM or higher
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 1030%
NaCl
-
0.2 M, 35% loss of activity
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
-
10 mM, 85% inhibition
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
phosphate
-
33 mM, 50% inhibition
proline
-
-
SDS
-
-
SDS
10% (w/v), 27% inhibition; 73% inhibition
trehalose
-
non-competitive
trehalose
-
non-competitive to UDPglucose
validoxylamine A
-
Zn2+
-
additional information
not inhibitory: 2-mercaptoethanol
-
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
-
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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0.1
2,6-diamino-4-(2,4-dichlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
0.1
2,6-diamino-4-(2-methylphenyl)-4H-thiopyran-3,5-dicarbonitrile
0.0002 - 0.0005
2,6-diamino-4-(3,4-dichlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
0.0012 - 0.0017
2,6-diamino-4-(3-bromophenyl)-4H-thiopyran-3,5-dicarbonitrile
0.0012 - 0.0013
2,6-diamino-4-(3-chlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
0.005 - 0.0061
2,6-diamino-4-(3-fluorophenyl)-4H-thiopyran-3,5-dicarbonitrile
0.0026 - 0.0049
2,6-diamino-4-(3-iodophenyl)-4H-thiopyran-3,5-dicarbonitrile
0.0918 - 0.1
2,6-diamino-4-(4,5-dihydrofuran-3-yl)-4H-thiopyran-3,5-dicarbonitrile
0.0631 - 0.1
2,6-diamino-4-(4,5-dihydrothiophen-3-yl)-4H-thiopyran-3,5-dicarbonitrile
0.1
2,6-diamino-4-(4-bromo-5-ethylthiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
0.0008 - 0.1
2,6-diamino-4-(4-bromo-5-methylthiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
0.004 - 0.011
2,6-diamino-4-(4-bromothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
0.0045 - 0.0149
2,6-diamino-4-(4-chlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
0.0129 - 0.0758
2,6-diamino-4-(4-methylphenyl)-4H-thiopyran-3,5-dicarbonitrile
0.0287 - 0.0419
2,6-diamino-4-(4-nitrophenyl)-4H-thiopyran-3,5-dicarbonitrile
0.0045 - 0.023
2,6-diamino-4-(5-bromothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
0.0059 - 0.0173
2,6-diamino-4-(5-chlorothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
0.0665 - 0.1
2,6-diamino-4-(5-ethylthiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
0.0054 - 0.0061
2,6-diamino-4-(5-nitrothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
0.0026 - 0.0029
2,6-diamino-4-(cyclohex-2-en-1-yl)-4H-thiopyran-3,5-dicarbonitrile
0.0031 - 0.0046
2,6-diamino-4-(cyclohex-3-en-1-yl)-4H-thiopyran-3,5-dicarbonitrile
0.0014 - 0.0019
2,6-diamino-4-cyclohexyl-4H-thiopyran-3,5-dicarbonitrile
0.1 - 789
2,6-diamino-4-phenyl-4H-thiopyran-3,5-dicarbonitrile
0.00371 - 0.00505
2,6-diamino-4-[3-(trifluoromethyl)phenyl]-4H-thiopyran-3,5-dicarbonitrile
0.1
2,6-diamino-4-[4-(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
0.1
6-amino-4-(3,4-dichlorophenyl)-2-thioxo-1,2,3,4-tetrahydropyridine-3,5-dicarbonitrile
0.0062 - 0.0066
8-chloro-11-(piperazin-1-yl)-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridine
0.0086 - 0.0314
8-hydroxy-2,4-dimethyl-7H-chromen-7-one
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
Drosophila melanogaster
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
Ctenocephalides felis
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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
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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evolution
Arthrobacter strain A3 has only two trehalose synthesis pathways (OtsA/B and TreS), while other Arthrobacter spp. have three
evolution
-
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
-
Arabidopsis thaliana has 11 TPS or TPS-like proteins, which belong to two distinct clades: class I (AtTPS1-AtTPS4) and class II (AtTPS5-AtTPS11)
evolution
the enzyme belongs to the glucosyltransferase-GTB-type superfamily
evolution
-
Arthrobacter strain A3 has only two trehalose synthesis pathways (OtsA/B and TreS), while other Arthrobacter spp. have three
-
malfunction
-
DELTAtps1 strains have reduced NADPH levels during growth on nitrate-containing media due to decreased G6PDH activity
malfunction
-
expression of TPS1 driven by the ABI3 promoter rescues the severe embryo phenotype but not the vegetative phenotype of tps1. tps1 exhibits a severe phenotype in vegetative tissue, consistent with the role played in embryo development
malfunction
stress hypersensitivity of mutants deleted for gene TPS1. At 42°C, the viability of the tps1DELTA mutant sharply drops by several decades, whereas the viability of the wild-type TPS1 strain remains almost unchanged. The the mal- BY4741 strain is unable to import trehalose. Overview of the impact of the different stresses on the drop of viability in wild-type and mdeletion mutants. The tps1DELTA mutant rapidly loses its ATP content in response to heat shock at 42°C
malfunction
-
tps1DELTA mutants fail to complete embryogenesis and rescued lines have stunted growth and delayed flowering. Loss of trehalose 6-phosphate production might not be the only reason for the growth defects of Arabidopsis thaliana tps1 mutants
malfunction
an otsA deletion mutant has significantly reduced intracellular trehalose levels compared to the wild-type strain and exhibits an apparent markedly slower growth rate in low osmolarity medium
malfunction
-
enzyme knockdown decreases hemolymph trehalose content and causes larval and pupal lethality. Enzyme knockdown survivors have a smaller amount of chitin and show elevated feeding on foliage
malfunction
-
enzyme knockdown results in optimal interference at 24 h and 36 h postinjection and causes a sharp decline in the survival rate during the 5th instar larval-pupal stage and obviously abnormal or lethal phenotypes. Silencing of the enzyme inhibits chitin biosynthesis. Furthermore, the expression levels of two genes associated with lipid biosynthesis are upregulated
malfunction
-
expression inhibition of isoform TPS3 leads to molting and wing deformity
malfunction
increased mortality can be observed in enzyme-depleted larvae under bacterial infection
malfunction
silencing the enzyme gene leads to molting deformities and high mortality rates via regulation of gene expression in the chitin biosynthetic pathway
metabolism
-
the first step in trehalose biosynthesis involves trehalose 6-phosphate synthase, Tps1
metabolism
gene TPS1 encodes the first enzyme in trehalose biosynthetic pathway, trehalose is a stress protectant
metabolism
in the OtsAB pathway, a trehalose-6-phosphate synthase (TPS, OtsA) catalyzes the formation of trehalose-6-phosphate from a glucosyl nucleotide and glucose-6-phosphate
metabolism
-
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
-
physiological function
-
disruption of the TPS2 gene encoding the only trehalose 6-phosphate phosphatase activity in Candida albicans causes a pleiotropic defective phenotype, maintaining the cell wall integrity and the ability to form chlamydospores. A homozygous tps2Delta/tps2Delta shows reduced growth at high temperatures and a marked sensitivity to heatshock and severe oxidative exposure. Exponential tps2Delta null cells display an adaptive response to oxidative stress as well as cross-tolerance between temperature and oxidative stress. Differential measurement of trehalose and trehalose 6-phosphate, revealed a significant accumulation of trehalose 6-phosphate in tps2Delta cells, which is enhanced after oxidative exposure. The level of trehalose 6-phosphate in parental cells is virtually undetectable, and oxidative treatment only induces the synthesis of free trehalose
physiological function
DvTPS increases the salt tolerance of the organism, overview
physiological function
regulation of OtsA expression during cold shock, both low temperature and accumulation of trehalose can inhibit OtsA expression, overview
physiological function
the multifunctional protein, OtsA, is indispensable for bacterial survival in various environments. The catalytic efficiency of OtsA is affected by its N-loop at low temperatures. The flexibility of the OtsA N-loop is related to the growth temperature of the respective bacterial species
physiological function
-
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
-
the TPS1 protein is a key regulator of trehalose metabolism throughout the Arabidopsis life cycle and not just in embryo development, it plays a key role in modulating trehalose 6-phosphate levels in vegetative tissues of Arabidopsis thaliana
physiological function
trehalose phosphate synthase is the crucial enzyme for the biosynthesis of trehalose, the main haemolymph sugar of insects
physiological function
trehalose phosphate synthase is the crucial enzyme for the biosynthesis of trehalose, the main haemolymph sugar of insects
physiological function
-
enzyme TPS1 is important throughout the life cycle with At least three catalytically active TPS isoforms
physiological function
in fungi, trehalose-6-phosphate synthase 1 plays a key role in the biosynthesis of trehalose
physiological function
isozyme OstA2 mainly contributes to the trehalose pool of strain 1CP
physiological function
isozyme OtsA1 seems to be involved in the overproduction of trehalose lipids
physiological function
-
possible signaling role of trehalose-6-phosphate or trehalose in the dessication process, sugars are proposed to play a role in osmotic adjustment, to stabilize biomolecules and membranes, and to act as a replacement for water
physiological function
the fused trehalose-6-phosphate synthase/phosphatase TPSP consists of an N-terminal trehalose-6-phosphate synthase (TPS) and a C-terminal trehalose-6-phosphate phosphatase (TPP) domain. The gene is organized in an operon with a putative glycosyltransferase GT and a putative mechanosensitive channel MSC. The enzyme exhibits high phosphatase activity, but requires activation by the co-expressed GT for bifunctional synthase-phosphatase activity. The GT mediated activation of trehalose-6-phosphate synthase activity relies on the fusion of both, trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase domain, in the enzyme. Activation is mediated by complex-formation
physiological function
the Tps1 protein is essential to maintain ATP levels during heat shock. Tps1 is endowed with a regulatory function in energy homeostasis, which is essential to withstand adverse conditions and maintain cellular integrity. Tps1, not trehalose, is important for yeast viability in response to various kinds of stresses. Contribution of the Tps1 protein to thermotolerance and acquired thermotolerance, enzyme deletion mutants show highly reduced growth at 42°C in contrast to the wild-type enzyme
physiological function
the enzyme functions as a cytoskeletal element regulating cell morphology
physiological function
-
the enzyme is essential for the normal growth and development of Heortia vitessoides
physiological function
-
the enzyme regulates trehalose metabolism and also mediates trehalase regulation of chitin synthesis and degradation pathways, and control insect molting process
physiological function
the enzyme takes part in immune defense in Musca domestica via synthesizing its product trehalose
physiological function
trehalose phosphate synthase 5-dependent trehalose metabolism regulates Arabidopsis thaliana defenses against pathogens (necrotrophic Botrytis cinerea and biotrophic Pseudomonas syringae).The enzyme is necessary for trehalose synthesis after pathogen infection
physiological function
-
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
-
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
-
isozyme OtsA1 seems to be involved in the overproduction of trehalose lipids
-
physiological function
-
isozyme OstA2 mainly contributes to the trehalose pool of strain 1CP
-
physiological function
-
regulation of OtsA expression during cold shock, both low temperature and accumulation of trehalose can inhibit OtsA expression, overview
-
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
-
additional information
-
trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase form a complex
additional information
differences in muscle trehalose content in female and male animals due to polymorphisms
additional information
differences in muscle trehalose content in female and male animals due to polymorphisms
additional information
differences in muscle trehalose content in female and male animals due to polymorphisms
additional information
differences in muscle trehalose content in female and male animals due to polymorphisms
additional information
-
differences in muscle trehalose content in female and male animals due to polymorphisms
additional information
the conserved residues Arg9, Trp45, Tyr81, Trp90, Asp135 and Arg284 are involved in glycosyl acceptor binding, and residues Gly29, His159, Arg246, Lys251, Asp345 and Glu353 are involved in glycosyl donor binding. Homology modeling of the enzyme using the enzyme structure from Escherichia coli, OtsA, PDB ID 1GZ5, chain A, as the template
additional information
-
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
-
trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase form a complex
-
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Londesborough, J.; Vuorio, O.
Trehalose-6-phosphate synthase/phosphatase complex from bakers' yeast: purification of a proteolytically activated form
J. Gen. Microbiol.
137
323-330
1991
Saccharomyces cerevisiae
brenda
Lippert, K.; Galinski, E.A.; Trueper, H.G.
Biosynthesis and function of trehalose in Ectothiorhodospira halochloris
Antonie van Leeuwenhoek
63
85-91
1993
Halorhodospira halochloris
brenda
Bell, W.; Klaassen, P.; Ohnacker, M.; Boller, T.; Herweijer, M.; Schoppink, P.; van der Zee, P.; Wiemken, A.
Characterization of the 56-kDa subunit of yeast trehalose-6-phosphate synthase and cloning of its gene reveal its identity with the product of CIF1, a regulator of carbon catabolite inactivation
Eur. J. Biochem.
209
951-959
1992
Saccharomyces cerevisiae, Saccharomyces cerevisiae C13-ABYS86
brenda
Pan, Y.T.; Mitchell, M.; Elbein, A.D.
Studies on the trehalose-phosphate synthase of Mycobacterium smegmatis: binding of heparin to the enzyme
Arch. Biochem. Biophys.
186
392-400
1978
Mycolicibacterium smegmatis
brenda
Killick, K.A.
Trehalose 6-phosphate synthase from Dictyostelium discoideum: partial purification and characterization of the enzyme from young sorocarps
Arch. Biochem. Biophys.
196
121-133
1979
Dictyostelium discoideum
brenda
Betz, R.; Holldorf, A.W.
Kinetic and biological properties of trehalose phosphate synthase from Neurospora crassa
Biochem. Soc. Trans.
3
988-989
1975
Neurospora crassa
-
brenda
Murphy, T.A.; Wyatt, G.R.
The enzymes of glycogen and trehalose synthesis in silk moth fat body
J. Biol. Chem.
240
1500-1508
1965
Hyalophora cecropia
brenda
Lornitzo, F.A.; Goldman, D.S.
Purification and properties of the transglucosylase inhibitor of Mycobacterium tuberculosis
J. Biol. Chem.
239
2730-2734
1964
Mycobacterium tuberculosis
brenda
Candy, D.J.; Kilb, B.A.
The biosynthesis of trehalose in the locust fat body
Biochem. J.
78
531-536
1961
Schistocerca gregaria
brenda
Cabib, E.; Leloir, L.F.
The biosynthesis of trehalose phosphate
J. Biol. Chem.
231
259-275
1958
Saccharomyces pastorianus
brenda
Elbein, A.D.; Mitchell, M.
Effects of polyanions and polycations on the trehalose phosphate synthetase of Mycobacterium smegmatis
Carbohydr. Res.
37
223-238
1974
Mycolicibacterium smegmatis
brenda
Vandercammen, A.; Francois, J.; Hers, H.G.
Characterization of trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase of Saccharomyces cerevisiae
Eur. J. Biochem.
182
613-620
1989
Saccharomyces cerevisiae
brenda
Giaever, H.M.; Styrvold, O.; Kaasen, I.; Strom, A.R.
Biochemical and genetic characterization of osmoregulatory trehalose synthesis in Escherichia coli
J. Bacteriol.
170
2841-2849
1988
Escherichia coli
brenda
Lapp, D.; Patterson, B.W.; Elbein, A.D.
Properties of a trehalose phosphate synthetase from Mycobacterium smegmatis
J. Biol. Chem.
246
4567-4579
1971
Mycolicibacterium smegmatis
-
brenda
Arisan-Atac, I.; Wolschek, M.F.; Kubicek, C.P.
Trehalose-6-phosphate synthase A affects citrate accumulation by Aspergillus niger under conditions of high glycolytic flux
FEMS Microbiol. Lett.
140
77-83
1996
Aspergillus niger
brenda
Pan, Y.T.; Elbein, A.D.
Inhibition of the trehalose-P synthase of mycobacteria by various antibiotics
Arch. Biochem. Biophys.
335
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