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Information on EC 2.4.1.15 - alpha,alpha-trehalose-phosphate synthase (UDP-forming)
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EC Tree
2.4.1.15 alpha,alpha-trehalose-phosphate synthase (UDP-forming)IUBMB Comments
See also EC 2.4.1.36 [alpha,alpha-trehalose-phosphate synthase (GDP-forming)].
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Word Map
- 2.4.1.15
- trehalase
- disaccharide
- tpp
-
desiccation
-
thermotolerance
-
resurrection
- selaginella
-
anhydrobiosis
- udp-glc
- validamycin
- agriculture
- drug development
- analysis
- medicine
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
alpha,alpha-trehalose phosphate synthase (UDP-forming), alpha,alpha-trehalose-phosphate synthase (UDP-forming), AtTPS1, AtTPS6, GbTPS, glucosyltransferase, uridine diphosphoglucose phosphate, OtsA, OtsA1, OtsA2, phosphotrehalose-uridine diphosphate transglucosylase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha,alpha-trehalose phosphate synthase (UDP-forming)
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-
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glucosyltransferase, uridine diphosphoglucose phosphate
-
-
-
-
OtsA
OtsA1
OtsA2
phosphotrehalose-uridine diphosphate transglucosylase
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-
-
-
T6P synthase
TPS
TPS1
TPS2
TPSP
transglucosylase
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-
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-
trehalose 6-phosphate synthase
trehalose 6-phosphate synthase 1
trehalose 6-phosphate synthetase
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trehalose phosphate synthase
trehalose phosphate synthetase
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trehalose phosphate-uridine diphosphate glucosyltransferase
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-
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trehalose-6-phosphate synthase
trehalose-6-phosphate synthase 1
trehalose-6-phosphate synthase/phosphatase
the bifunctional enzyme consists of an N-terminal trehalose-6-phosphate synthase and a C-terminal trehalose-6-phosphate phosphatase domain
trehalose-P synthetase
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trehalosephosphate-UDP glucosyl transferase
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UDP-glucose:D-glucose-6-phosphate 1-alpha-D-glucosyltransferase
UDPglucose-glucose-phosphate glucosyltransferase
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-
-
-
TPS
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-
-
-
TPSP
the bifunctional enzyme consists of an N-terminal trehalose-6-phosphate synthase and a C-terminal trehalose-6-phosphate phosphatase domain
TPSP
Thermoproteus tenax ATCC 35583
the bifunctional enzyme consists of an N-terminal trehalose-6-phosphate synthase and a C-terminal trehalose-6-phosphate phosphatase domain
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TPSP
the bifunctional enzyme consists of an N-terminal trehalose-6-phosphate synthase and a C-terminal trehalose-6-phosphate phosphatase domain
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trehalose 6-phosphate synthase
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-
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trehalose phosphate synthase
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trehalose-6-phosphate synthase
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key subunit of the trehalose synthase complex
UDP-glucose:D-glucose-6-phosphate 1-alpha-D-glucosyltransferase
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate
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-
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UDP-alpha-D-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate
reaction mechanism
-
UDP-alpha-D-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate
ordered bi-bi mechanism
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UDP-alpha-D-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate
complex bimodal kinetics
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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 SOURCE
PATHWAYS
BRENDA
MetaCyc
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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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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
-
-
-
-
?
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
-
-
-
-
?
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-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-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
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-
?
UDP-glucose + D-fructose 6-phosphate
UDP + ?
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16% of the activity with D-glucose 6-phosphate
-
-
?
UDP-glucose + D-galactose
UDP + ?
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17% of the activity with D-glucose 6-phosphate
-
-
?
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-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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-
-
-
?
ADP-alpha-D-glucose + D-glucose 6-phosphate
ADP + alpha,alpha-trehalose 6-phosphate
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-
-
-
?
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
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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
-
-
?
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
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?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
Thermoproteus tenax ATCC 35583
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?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
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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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-
-
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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
-
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
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-
?
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
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-
-
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?
GDP-glucose + D-glucose 6-phosphate
trehalose 6-phosphate + GDP
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-
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?
GDP-glucose + D-glucose 6-phosphate
trehalose 6-phosphate + GDP
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13% of the activity with UDPglucose
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?
TDP-alpha-D-glucose + D-glucose 6-phosphate
TDP + alpha,alpha-trehalose 6-phosphate
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-
-
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?
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
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15.9% of the activity with UDPglucose
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-
?
TDP-glucose + glucose 6-phosphate
trehalose 6-phosphate + TDP
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-
-
-
?
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
Thermoproteus tenax ATCC 35583
-
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
Pleurotus ostreatus CCMSSC 00389
-
-
-
-
?
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
Pleurotus tuoliensis CCMSSC 00489
-
-
-
-
?
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
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
-
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
-
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
-
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
?
-
Pleurotus tuoliensis CCMSSC 00489
-
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 (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 SUBSTRATE
NATURAL 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
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-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
Pleurotus ostreatus CCMSSC 00389
-
-
-
-
?
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
Pleurotus tuoliensis CCMSSC 00489
-
-
-
-
?
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
-
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+
Cu2+
Fe2+
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
Ni2+
Zn2+
additional information
Co2+
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+
-
most appropriate cation to activate enzyme activity as it increases the activity by 7851fold at 12.5 mM
Mg2+
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+
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+
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
the addition of monovalent metal ions Na+, K+ and Li+ has no effect on the enzyme activity
additional information
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
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
-
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
-
chondroitin 4-sulfate, chondroitin 6-sulfate
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
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
-
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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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Dehydration
Accumulation of trehalose by overexpression of tps1, coding for trehalose-6-phosphate synthase, causes increased resistance to multiple stresses in the fission yeast schizosaccharomyces pombe
Dehydration
Metabolite/phytohormone-gene regulatory networks in soybean organs under dehydration conditions revealed by integration analysis.
Starvation
Nitrogen starvation in a Saccharomyces cerevisiae strain deleted in the trehalose-6-phosphate synthase complex.
Tuberculosis
Allosteric regulation of the partitioning of glucose-1-phosphate between glycogen and trehalose biosynthesis in Mycobacterium tuberculosis.
Tuberculosis
PURIFICATION AND PROPERTIES OF THE TRANSGLUCOSYLASE INHIBITOR OF MYCOBACTERIUM TUBERCULOSIS.
Tuberculosis
Synthesis and in Vitro Characterization of Trehalose-Based Inhibitors of Mycobacterial Trehalose 6-Phosphate Phosphatases.
Yersinia pseudotuberculosis Infections
Purification and properties of the adenosine diphosphoglucose: glycogen transglucosylase of Pasteurella pseudotuberculosis.
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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
0.2 - 1
UDP-alpha-D-glucose
pH 6.0, 60°C, wild-type enzyme
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
-
bifunctional fusion enzyme of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase
-
additional information
additional information
-
complex bimodal kinetics
-
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
-
bifunctional fusion enzyme of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase
-
3.2
glucose 6-phosphate
-
bifunctional fusion enzyme of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase
3.6
UDPglucose
-
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
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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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
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
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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
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
20.6
purified recombinant enzyme, substrates GDP-glucose and D-glucose 6-phosphate
7.33
purified recombinant enzyme, pH 6.0, 60°C, substrate UDP-glucose
95
purified recombinant enzyme, substrates ADP-glucose and D-glucose 6-phosphate
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
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
20 - 40
20 - 50
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
4 - 20
catalytic activity of OtsA at 4°C is 1.2fold greater than that at 20°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
20 - 40
-
nearly half of the activity is maintained at temperatures below 30°C, whereas most of the activities are lost at temperatures above 40°C
20 - 40
-
more than 59% activity between 20 and 40°C, the enzyme activity declines abruptly as the temperature climbed to 50°C and keeps constantly around 10% of the maximum until 90°C
20 - 50
-
20% of maximal activity at 20°C and 50°C, inactive at 65°C
20 - 50
drastic decrease in enzyme activity is observed at temperatures below 20°C and above 50°C
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from the alpine permafrost, CGMCC 1.8987, gene otsA
UniProt
brenda
bifunctional trehalose 6-phospate synthase and trehalose 6-phospate phosphatase enzyme
-
-
brenda
i.e. Mucormycosis agent or Rhizopus arrhizus var. delemar
UniProt
brenda
Thermoproteus tenax ATCC 35583
bifunctional trehalose-6-phosphate synthase/phosphatase, EC 2.4.1.15 and EC 3.1.3.12
SwissProt
brenda