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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
-
osmoprotectant
-
resurrection
- udp-glc
-
anhydrobiosis
- selaginella
- validamycin
- agriculture
- analysis
- medicine
- drug development
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, 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)
-
-
-
-
glucosyltransferase, uridine diphosphoglucose phosphate
-
-
-
-
OtsA
OtsA1
OtsA2
phosphotrehalose-uridine diphosphate transglucosylase
-
-
-
-
T6P synthase
TPS
TPS1
TPSP
transglucosylase
-
-
-
-
trehalose 6-phosphate synthase
trehalose 6-phosphate synthase 1
trehalose 6-phosphate synthetase
-
-
-
-
trehalose phosphate synthase
trehalose phosphate synthetase
-
-
-
-
trehalose phosphate-uridine diphosphate glucosyltransferase
-
-
-
-
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
-
-
-
-
trehalosephosphate-UDP glucosyl transferase
-
-
-
-
UDPglucose-glucose-phosphate glucosyltransferase
-
-
-
-
TPS
-
-
-
-
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
-
TPSP
; the bifunctional enzyme consists of an N-terminal trehalose-6-phosphate synthase and a C-terminal trehalose-6-phosphate phosphatase domain
-
trehalose 6-phosphate synthase
-
-
-
-
trehalose phosphate synthase
-
-
-
-
trehalose-6-phosphate synthase
-
key subunit of the trehalose synthase complex
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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
-
-
-
-
UDP-alpha-D-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate
ordered bi-bi mechanism
-
UDP-alpha-D-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate
complex bimodal kinetics
-
UDP-alpha-D-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate
reaction mechanism
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
hexosyl group transfer
-
-
-
-
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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
-
-
?
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
-
-
?
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 + lactose
UDP + ?
-
10% of the activity with D-glucose 6-phosphate
-
-
?
UDP-glucose + sucrose
UDP + ?
-
19% of the activity with D-glucose 6-phosphate
-
-
?
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
Thermoproteus tenax ATCC 35583
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
-
-
-
?
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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-
-
-
?
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
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
-
first step in trehalose biosynthesis, enzyme is essential for embryo maturation
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
step in trehalose biosynthesis
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
Q1KLW0
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
?
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
Q1KLW0
-
-
-
?
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
-
step in trehalose biosynthesis
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
with retention of the anomeric configuration of the UDP-sugar donor, reaction stereochemistry
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
in crude extracts of Propionibacterium freudenreichii, OtsA is specific for ADP-glucose, in contrast to the pure recombinant OtsA, which uses UDP-glucose, GDP-glucose and TDP-glucose, in addition to ADP-glucose. The substrate specificity of OtsA in cell extracts is lost during purification, and the recombinant OtsA becomes specific to ADP-glucose upon incubation with a dialysed cell extract
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
step in trehalose biosynthesis
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
step in trehalose biosynthesis
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
step in trehalose biosynthesis
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
the enzyme is highly specific for UDP-glucose and D-glucose 6-phosphate
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
the enzyme can utilize various nucleoside diphosphate monosaccharides. Maximal activity with UDP-glucose. Various phosphorylated monosaccharides D-glucose 6-phosphate, glucosamine-6-phosphate, fructose-6-phosphate and mannose-6-phosphate can be used as catalytic acceptors, with maximal activity towards D-glucose 6-phosphate
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
first step in one of 2 existing trehalose biosynthesis pathways, plays a role in osmoadaptation
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
best substrates, absolutely specific for D-glucose 6-phosphate
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
first step in one of 2 existing trehalose biosynthesis pathways, plays a role in osmoadaptation
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
best substrates, absolutely specific for D-glucose 6-phosphate
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
recombinant His10-tagged OtsA1 shows highest activity with ADP-glucose and UDP-glucose, whereas recombinant His10-tagged OtsA2 prefers UDP-glucose
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
recombinant His10-tagged OtsA1 shows highest activity with ADP-glucose and UDP-glucose, whereas recombinant His10-tagged OtsA2 prefers UDP-glucose
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
the enzyme is essential for Arabidopsis embryo development, TPS1 appears to play a vital role in responding to the increase in sucrose supply, which accompanies the onset of embryo maturation
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
AtTPS1 is a single-copy gene and is expressed constitutively at very low levels
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
trehalose-6-phosphate synthase A affects citrate accumulation by Aspergillus niger under conditions of high glycolytic flux
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
absolute specificity for glucose 6-phosphate
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
enzyme is osmotically inducible, mutants which are defective in the synthesis of the synthase have an impaired osmotic tolerance in glucose-mineral medium
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
specific for UDPglucose, no reaction with ADPglucose or GDPglucose
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
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
?
-
-
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
?
-
-
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
C7EZF1
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-1,1-trehalose 6-phosphate
-
step in trehalose biosynthesis
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
Q94AH8
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
first step in trehalose biosynthesis, enzyme is essential for embryo maturation
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
step in trehalose biosynthesis
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
Q1KLW0
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
C7EZF1
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
C7EZF1
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
Q1KLW0
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
step in trehalose biosynthesis
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
Q6IVK9
both TPS1 and TPS2 are required for high-temperature (37°C) growth and glycolysis but that the block at TPS2 results in the apparent toxic accumulation of trehalose-6-phosphate, which makes this enzyme a fungicidal target
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
J7G8S5
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
Q9Y119
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
P31677
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
step in trehalose biosynthesis
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
Q66Q98
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
P31688, Q00764
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
step in trehalose biosynthesis
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
step in trehalose biosynthesis
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
step in trehalose biosynthesis
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
Q7WUI7
first step in one of 2 existing trehalose biosynthesis pathways, plays a role in osmoadaptation
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
Q7WUI7
first step in one of 2 existing trehalose biosynthesis pathways, plays a role in osmoadaptation
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
E1U2Z7, E1U2Z8, E1U2Z9, E1U300
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
A0A0B5WYD4
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
A4K8Z1, A4K8Z2
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
A4K8Z1, A4K8Z2
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
Q9HIW6
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
Q9SYM4
the enzyme is essential for Arabidopsis embryo development, TPS1 appears to play a vital role in responding to the increase in sucrose supply, which accompanies the onset of embryo maturation
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
AtTPS1 is a single-copy gene and is expressed constitutively at very low levels
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
trehalose-6-phosphate synthase A affects citrate accumulation by Aspergillus niger under conditions of high glycolytic flux
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
enzyme is osmotically inducible, mutants which are defective in the synthesis of the synthase have an impaired osmotic tolerance in glucose-mineral medium
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
TPS1-encoded trehalose-6-phosphate synthase exerts an essential control on the influx into glycolysis. Tps1-mediated protein-protein interactions are important for control of glucose influx into yeast glycolysis
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
key enzyme for biosynthesis of trehalose, the major soluble carbohydrate in resting cells
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
the enzyme plays a role in the control of glycolysis
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
key enzyme for biosynthesis of trehalose, the major soluble carbohydrate in resting cells
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
alpha,alpha-trehalose 6-phosphate synthase is dispensable for growth on glucose but not for spore germination
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
-
the enzyme does not play a role in the control of glycolysis
-
?
additional information
?
-
-
the enzyme, encoded by gen tps1, is a regulator of glucose, abscisic acid, and stress signaling, trehalose is an osmoprotectant, trehalose content in wild-type and transgenic plants, overview
-
-
-
additional information
?
-
-
TPS1 may play a major role in coordinating cell wall biosynthesis and cell division with cellular metabolism during embryo development
-
-
-
additional information
?
-
-
trehalose is able to protect the integrity of the cells against a variety of environmental stresses such as desiccation, dehydration, heat, cold, and oxidation, probably via reduction of protein denaturation through protein-trehalose interactions, the enzyme might be a radical scavenger
-
-
-
additional information
?
-
-
trehalose is able to protect the integrity of the cells against a variety of environmental stresses such as desiccation, dehydration, heat, cold, and oxidation, probably via reduction of protein denaturation through protein-trehalose interactions, in flying insects trehalose content is especially high in hemolymph and thorax muscles and is consumed during flight
-
-
-
additional information
?
-
-
trehalose acts as a global protectant against abiotic stress, accumulation of trehalose leads to increased salt, drought, and cold resistance in plants
-
-
-
additional information
?
-
-
trehalose is able to protect the integrity of the cells against a variety of environmental stresses such as desiccation, dehydration, heat, cold, and oxidation, probably via reduction of protein denaturation through protein-trehalose interactions
-
-
-
additional information
?
-
-
the trehalose-6-phosphate synthase/phosphatase (OtsA–OtsB) pathway plays an important role in the synthesis of trehalose in response to stress
-
-
-
additional information
?
-
-
trehalose is able to protect the integrity of the cells against a variety of environmental stresses such as desiccation, dehydration, heat, cold, and oxidation, probably via reduction of protein denaturation through protein-trehalose interactions, the enzyme might be a radical scavenger
-
-
-
additional information
?
-
-
trehalose is able to protect the integrity of the cells against a variety of environmental stresses such as desiccation, dehydration, heat, cold, and oxidation, probably via reduction of protein denaturation through protein-trehalose interactions
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
Co2+
K+
KCl
-
upon an increase in the KCl concentration from 0 to 100 mM, the OtsA activity decreases by more than 40%, whereas it is not significantly affected when UDP or GDP-glucose is used as the substrate
Mg2+
Mn2+
NaCl
Zn2+
additional information
Co2+
1.91fold activation at 10 mM; the enzyme does not require divalent metal ions for catalysis, but Mg2+, Zn2+, Co2+ and Mn2+ can stimulate enzyme activity and maximal activation is found in the presence of Mg2+. 1.91fold activation by 10 mM Co2+
Mg2+
2.33fold activation at 10 mM; the enzyme does not require divalent metal ions for catalysis, but Mg2+, Zn2+, Co2+ and Mn2+ can stimulate enzyme activity and maximal activation is found in the presence of Mg2+. 2.33fold activation ba 10 mM Mg2+
Mn2+
1.16fold activation at 10 mM; the enzyme does not require divalent metal ions for catalysis, but Mg2+, Zn2+, Co2+ and Mn2+ can stimulate enzyme activity and maximal activation is found in the presence of Mg2+. 1.16fold activation by 10 mM Mn2+
NaCl
-
an increase in the concentration of NaCl from 0 to 100 mM leads to a decrease in the OtsA activity by more than 35% when ADP-glucose or TDP-glucose is the substrate. When UDP-glucose or GDP-glucose is used as substrate, the OtsA activity is increased by 10–30%
Zn2+
2.26fold activation at 10 mM; the enzyme does not require divalent metal ions for catalysis, but Mg2+, Zn2+, Co2+ and Mn2+ can stimulate enzyme activity and maximal activation is found in the presence of Mg2+. 2.26fold activation by 10 mM Zn2+
additional information
-
no or poor effects by CoCl2, CaCl2, BaCl2, and FeSO4
additional information
heparin in assays has no effect on the activity of recombinant OtsA1-His10
additional information
heparin in assays has no effect on the activity of recombinant OtsA1-His10
additional information
no effect by Li+ at 10 mM; the addition of monovalent metal ions Na+, K+ and Li+ has no effect on the enzyme activity
additional information
-
no effect by Li+ at 10 mM; the addition of monovalent metal ions Na+, K+ and Li+ has no effect on the enzyme activity
additional information
no requirement for divalent cations for activity
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
-
transglycosylase inhibitor is an oligonucleotide containing between 6 and 9 purine bases and no pyrimidine bases, noncompetitively inhibits the transglucosylase
-
additional information
-
no effect by sucrose and trehalose up to 0.4 M, no substrate and product inhibition
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
chondroitin
-
stimulation, particularly when a pyrimidine glucose nucleotide is used, rather than a purine glucose nucleotide
glycosyltransferase
the Thermoproteus tenax trehalose-6-phosphate synthase/phosphatase (TPSP) exhibits high phosphatase activity, but requires activation by the co-expressed glycosyltransferase for bifunctional synthase/phosphatase activity. The glycosyltransferase mediated activation of trehalose-6-phosphate synthase activity relies on the fusion of both, trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase domain, in the TPSP enzyme. Activation is mediated by complex-formation in vivo
-
chondroitin sulfate
-
polyanions heparin and chondroitin sulfate stimulate TPS activity with different glucosyl donors
chondroitin sulfate
-
activation; chondroitin 4-sulfate, chondroitin 6-sulfate
chondroitin sulfate
maximal activation at 0.0005 mg; maximal stimulation at 400 ng
heparin
-
polyanions heparin and chondroitin sulfate stimulate TPS activity with different glucosyl donors
heparin
the activity of OtsA2-His10 is significantly increased, most of all when UDP-glucose is used as substrate
heparin
-
stimulation, particularly when a pyrimidine glucose nucleotide is used, rather than a purine glucose nucleotide. Heparin helps to retain both stability and activity of the final purified enzyme
heparin
0.006 mg, stimulates; heparin can stimulate the activity of the enzyme, although the activity decreases while the concentration of heparin is above 600 ng
RNA
-
various RNA, particularly that isolated from Mycobacterium smegmatis chondroitin sulfate, activate
additional information
increase of trehalose in the first 2-3 h of cold shock
-
additional information
-
dependence on polyanion concentrations for optimum TPS activity, overview
-
additional information
-
when pyrimidine sugar nucleotides are used as substrates, there is an almost absolute requirement for a high molecular weight polyanion for activity. When the purine sugar nucleotides are used as substrates fairly good enzymatic activity is observed in absence of a polyanion, this activity increases 2 to 4fold in the presence of optimum concentrations of polyanion. Activation by the polyanion is inhibited by high salt concentrations as well as by high concentrations of mononucleoside phosphates
-
additional information
-
the trehalose-6-phosphate synthase of Saccharomyces cerevisiae shows 1.76fold enhanced activity after specific methylation at a cysteine residue through 14 kDa cysteine methyltransferase from Saccharomyces cerevisiae
-
additional information
-
no effect by sucrose and trehalose up tp 0.4 M
-
additional information
the enzymatic activity can be stimulated by divalent metal ions and polyanions heparin and chondroitin sulfate
-
additional information
-
the enzymatic activity can be stimulated by divalent metal ions and polyanions heparin and chondroitin sulfate
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.34
D-glucose 6-phosphate
pH 6.0, 60°C, N-loop truncation mutant enzyme
0.8
D-glucose 6-phosphate
recombinant enzyme, pH 7.0, 80°C, in presence of Mg2+
3
D-glucose 6-phosphate
-
37°C, pH 5.5, cosubstrate: UDP-glucose
4.2
D-glucose 6-phosphate
-
37°C, pH 5.5, cosubstrate: ADP-glucose
5.3
D-glucose 6-phosphate
-
37°C, pH 5.5, cosubstrate: TDP-glucose
7.1
D-glucose 6-phosphate
-
37°C, pH 5.5, cosubstrate: GDP-glucose
7.5
glucose 6-phosphate
-
bifunctional fusion enzyme of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase
0.74
UDP-alpha-D-glucose
pH 6.0, 60°C, N-loop truncation mutant enzyme
0.5
UDP-glucose
recombinant enzyme, pH 7.0, 80°C, in presence of Mg2+
0.04
UDPglucose
-
in presence of optimal concentration of a polyanion
5.1
UDPglucose
-
bifunctional fusion enzyme of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase
additional information
additional information
-
complex bimodal kinetics
-
additional information
additional information
-
bifunctional fusion enzyme of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase
-
additional information
additional information
-
the high catalytic efficiency of OtsA results from the high affinity of the enzyme for uridine 5'-diphosphoglucose at low temperatures
-
additional information
additional information
Q1KLW0
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Q1KLW0
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
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.1
2,6-diamino-4-(2,4-dichlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.1
2,6-diamino-4-(2-methylphenyl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.1
2,6-diamino-4-(2-methylphenyl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0002
2,6-diamino-4-(3,4-dichlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0005
2,6-diamino-4-(3,4-dichlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0012
2,6-diamino-4-(3-bromophenyl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0017
2,6-diamino-4-(3-bromophenyl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0012
2,6-diamino-4-(3-chlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0013
2,6-diamino-4-(3-chlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.005
2,6-diamino-4-(3-fluorophenyl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0061
2,6-diamino-4-(3-fluorophenyl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0026
2,6-diamino-4-(3-iodophenyl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0049
2,6-diamino-4-(3-iodophenyl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0918
2,6-diamino-4-(4,5-dihydrofuran-3-yl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.1
2,6-diamino-4-(4,5-dihydrofuran-3-yl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0631
2,6-diamino-4-(4,5-dihydrothiophen-3-yl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.1
2,6-diamino-4-(4,5-dihydrothiophen-3-yl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.1
2,6-diamino-4-(4-bromo-5-ethylthiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.1
2,6-diamino-4-(4-bromo-5-ethylthiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0008
2,6-diamino-4-(4-bromo-5-methylthiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.1
2,6-diamino-4-(4-bromo-5-methylthiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.004
2,6-diamino-4-(4-bromothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.011
2,6-diamino-4-(4-bromothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0045
2,6-diamino-4-(4-chlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0149
2,6-diamino-4-(4-chlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0129
2,6-diamino-4-(4-methylphenyl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0758
2,6-diamino-4-(4-methylphenyl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0287
2,6-diamino-4-(4-nitrophenyl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0419
2,6-diamino-4-(4-nitrophenyl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0045
2,6-diamino-4-(5-bromothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.023
2,6-diamino-4-(5-bromothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0059
2,6-diamino-4-(5-chlorothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0173
2,6-diamino-4-(5-chlorothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0665
2,6-diamino-4-(5-ethylthiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.1
2,6-diamino-4-(5-ethylthiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0054
2,6-diamino-4-(5-nitrothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0061
2,6-diamino-4-(5-nitrothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0026
2,6-diamino-4-(cyclohex-2-en-1-yl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0029
2,6-diamino-4-(cyclohex-2-en-1-yl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0031
2,6-diamino-4-(cyclohex-3-en-1-yl)-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0046
2,6-diamino-4-(cyclohex-3-en-1-yl)-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0014
2,6-diamino-4-cyclohexyl-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0019
2,6-diamino-4-cyclohexyl-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.1
2,6-diamino-4-phenyl-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
789
2,6-diamino-4-phenyl-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.00371
2,6-diamino-4-[3-(trifluoromethyl)phenyl]-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.00505
2,6-diamino-4-[3-(trifluoromethyl)phenyl]-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.1
2,6-diamino-4-[4-(trifluoromethyl)phenyl]-4H-thiopyran-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.1
2,6-diamino-4-[4-(trifluoromethyl)phenyl]-4H-thiopyran-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0014
3-amino-4-formyl-2-[2-oxo-2-(tricyclo[3.3.1.13,7]dec-1-yl)ethyl]cyclopent-3-ene-1,1,2-tricarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0046
3-amino-4-formyl-2-[2-oxo-2-(tricyclo[3.3.1.13,7]dec-1-yl)ethyl]cyclopent-3-ene-1,1,2-tricarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.1
6-amino-4-(3,4-dichlorophenyl)-2-thioxo-1,2,3,4-tetrahydropyridine-3,5-dicarbonitrile
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.1
6-amino-4-(3,4-dichlorophenyl)-2-thioxo-1,2,3,4-tetrahydropyridine-3,5-dicarbonitrile
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0062
8-chloro-11-(piperazin-1-yl)-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridine
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0066
8-chloro-11-(piperazin-1-yl)-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridine
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0086
8-hydroxy-2,4-dimethyl-7H-chromen-7-one
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0314
8-hydroxy-2,4-dimethyl-7H-chromen-7-one
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0094
methyl 2-chloro-5-(5-[(Z)-[3-(2,4-dimethylphenyl)-4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene]methyl]furan-2-yl)benzoate
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0147
methyl 2-chloro-5-(5-[(Z)-[3-(2,4-dimethylphenyl)-4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene]methyl]furan-2-yl)benzoate
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0028
O,O-diphenyl [(2E)-2-[2-(2-chlorophenyl)hydrazinylidene]-2-cyanoethanethioyl]phosphoramidothioate
Drosophila melanogaster
Q9Y119
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
0.0055
O,O-diphenyl [(2E)-2-[2-(2-chlorophenyl)hydrazinylidene]-2-cyanoethanethioyl]phosphoramidothioate
Ctenocephalides felis
J7G8S5
2 mM phosphoenol pyruvate, 2% (w/v) NaCl, 0.5% (w/v) KCl, 10 mM MgCl2, 1 mM dithiothreitol, 1.5 U/ml pyruvate kinase, pH 7.5 22 °C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.01
-
preparation of trehalose-6-phosphate synthase from Saccharomyces cerevisiae, preparation step soluble supernatant
0.011
-
TPS specific activity in glucose, yeast mutant strain tps2delta + pSAL4
0.013
-
TPS specific activity in galactose, yeast mutant strain tps1delta_tps2delta + pSAL4::TPS1
0.02
-
TPS specific activity in glucose, yeast mutant strain tps1delta_tps2delta + pSAL4::TPS1
0.063
-
TPS specific activity in galactose, yeast mutant strain tps2delta + pSAL4::TPS2
0.067
-
TPS specific activity in glucose, yeast mutant strain tps2delta + pSAL4::TPS2
0.073
-
TPS specific activity in glucose, yeast mutant strain tps2delta + pSAL4::TPS1-TPS2
0.078
-
TPS specific activity in galactose, yeast mutant strain tps2delta + pSAL4::TPS1-TPS2
0.081
-
TPS specific activity in galactose, yeast mutant strain tps1delta + pSAL4::TPS1-TPS2
0.086
-
TPS specific activity in glucose, yeast mutant strain tps1delta + pSAL4::TPS1-TPS2
0.088
-
TPS specific activity in galactose, yeast mutant strain tps1delta_tps2delta + pSAL4::TPS1-TPS2
0.093
-
TPS specific activity in glucose, yeast mutant strain tps1delta_tps2delta + pSAL4::TPS1-TPS2
0.144
-
TPS specific activity in glucose, yeast mutant strain tps1delta + pSAL4::TPS1
0.163
-
TPS specific activity in galactose, yeast mutant strain tps1delta + pSAL4::TPS1
0.49
-
preparation of trehalose-6-phosphate synthase from Saccharomyces cerevisiae, preparation step ammonimum sulfate fractionation
0.74
-
preparation of trehalose-6-phosphate synthase from Saccharomyces cerevisiae, preparation step HPGPLC on TSK G2000SW
1.58
7.33
purified recombinant enzyme, pH 6.0, 60°C, substrate UDP-glucose
20.6
purified recombinant enzyme, substrates GDP-glucose and D-glucose 6-phosphate
95
purified recombinant enzyme, substrates ADP-glucose and D-glucose 6-phosphate
106.7
purified recombinant enzyme, substrates TDP-glucose and D-glucose 6-phosphate
149.6
purified recombinant enzyme, substrates UDP-glucose and D-glucose 6-phosphate
150.5
purified native enzyme, pH 4.0, 37°C; purified native enzyme, pH 4.0, 37°C
additional information
1.58
-
preparation of trehalose-6-phosphate synthase from Saccharomyces cerevisiae, preparation step HPGPLC on HiLoad 16/60 Superdex 200
additional information
-
TPS activity is maximally at pH 8.5 with 2.11 U/mg, followed by 2.01 U/mg at pH 9.0, 1.93 U/mg at pH 9.5, and 1.21 U/mg at pH 10.5, but only 0.31 U/mg at pH 4.5
additional information
-
the activity of trehalose-6-phosphate synthase is concentration dependent
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.3
-
activity with ADP-glucose, UDP-glucose and TDP-glucose
6.5
7.5
8.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 10.5
-
TPS activity is maximally at pH 8.5 with 2.11 U/mg, followed by 2.01 U/mg at pH 9.0, 1.93 U/mg at pH 9.5, and 1.21 U/mg at pH 10.5, but only 0.31 U/mg at pH 4.5
5 - 6
-
pH 5.0: about 85% of maximal activity, pH 6.0: about 50% of maximal activity
5 - 7
pH 5.0: about 50% of maximal activity, pH 7.0: about 50% of maximal activity
5.5 - 8
-
pH 5.5: about 75% of maximal activity, pH 8.0: about 70% of maximal activity
6 - 8
drastic decrease in enzyme activity is observed at pH values below pH 6.0 and above pH 8.0
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
22
30 - 40
-
bifunctional fusion enzyme of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase
35
37
40
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 20
catalytic activity of OtsA at 4°C is 1.2fold greater than that at 20°C
20 - 60
activity range, at 40°C, the enzyme demonstrates 87.04% of its maximum activity. A rapid decrease in the enzyme activity occurs at 50°C with 35.27% of maximum activity, completely loss of activity above 60°C; activity range, at 40°C, the enzyme demonstrates 87.04% of its maximum activity. A rapid decrease in the enzyme activity occurs at 50°C with 35.27% of maximum activity, completely loss of activity above 60°C
20 - 50
drastic decrease in enzyme activity is observed at temperatures below 20°C and above 50°C
40 - 100
about half-maximal activity at 40°C, 80% of maximal activity at 100°C, inactive at 30°C
50 - 80
50°C: about 50% of maximal activity, 80°C: about 75% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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
; bifunctional trehalose-6-phosphate synthase/phosphatase, EC 2.4.1.15 and EC 3.1.3.12
SwissProt
brenda
Thermoproteus tenax ATCC 35583
bifunctional trehalose-6-phosphate synthase/phosphatase, EC 2.4.1.15 and EC 3.1.3.12
SwissProt
brenda
isolated from the alpine permafrost, CGMCC 1.8987, gene otsA
UniProt
brenda
isozyme 1; collected from the upper Chesapeake Bay, China
E1U2Z7
UniProt
brenda
isozyme 1a; collected from the upper Chesapeake Bay, China
UniProt
brenda
isozyme 1b; collected from the upper Chesapeake Bay, China
E1U2Z9
UniProt
brenda
isozyme 1c; collected from the upper Chesapeake Bay, China
UniProt
brenda
-
-
-
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
in both males and females, the darker muscles exhibit greater amounts of trehalose, trehalose 6-phosphate synthase, and trehalase activities than the light colored; in both males and females, the darker muscles exhibit greater amounts of trehalose, trehalose 6-phosphate synthase, and trehalase activities than the light colored; in both males and females, the darker muscles exhibit greater amounts of trehalose, trehalose 6-phosphate synthase, and trehalase activities than the light colored; in both males and females, the darker muscles exhibit greater amounts of trehalose, trehalose 6-phosphate synthase, and trehalase activities than the light colored
brenda
correlation between TPS activity in hemocytes and hemolymph trehalose levels is found during the molt cycle
brenda
additional information
expression of GbTPS is up-regulated by cold, NaCl, mannitol and drought treatments
brenda
expression of GbTPS is up-regulated by cold, NaCl, mannitol and drought treatments
brenda
additional information
-
bdelloids show low tps gene expression levels, but strong overexpression of the TPS genes is observed when bdelloids enter desiccation. Quantitative expression analysis
brenda
additional information
-
expression of AtTPS1 is low and not organ specific
brenda
additional information
-
very low levels of trehalose in plant tissue
brenda
additional information
-
gene AtTPS1 is widely expressed throughout the plant
brenda
additional information
-
gene AtTPS1 is widely expressed throughout the plant
-
brenda
additional information
-
ubiquitous expression of CasTPS in most tissues; ubiquitous expression of CasTPS in most tissues; ubiquitous expression of CasTPS in most tissues; ubiquitous expression of CasTPS in most tissues
brenda
additional information
E1U2Z7
ubiquitous expression of CasTPS in most tissues; ubiquitous expression of CasTPS in most tissues; ubiquitous expression of CasTPS in most tissues; ubiquitous expression of CasTPS in most tissues
brenda
additional information
ubiquitous expression of CasTPS in most tissues; ubiquitous expression of CasTPS in most tissues; ubiquitous expression of CasTPS in most tissues; ubiquitous expression of CasTPS in most tissues
brenda
additional information
E1U2Z9
ubiquitous expression of CasTPS in most tissues; ubiquitous expression of CasTPS in most tissues; ubiquitous expression of CasTPS in most tissues; ubiquitous expression of CasTPS in most tissues
brenda
additional information
ubiquitous expression of CasTPS in most tissues; ubiquitous expression of CasTPS in most tissues; ubiquitous expression of CasTPS in most tissues; ubiquitous expression of CasTPS in most tissues
brenda
additional information
activity of trehalose-6-phosphate synthase during larval-pupal development is significantly higher in diapause-type individuals than in nondiapause individuals and is closely correlated with the changes in the trehalose content. mRNA is detected at high levels in the late stage of sixth larval instar and the early middle stage of diapause-destined pupae
brenda
additional information
-
activity of trehalose-6-phosphate synthase during larval-pupal development is significantly higher in diapause-type individuals than in nondiapause individuals and is closely correlated with the changes in the trehalose content. mRNA is detected at high levels in the late stage of sixth larval instar and the early middle stage of diapause-destined pupae
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
additional information
-
the enzyme is markedly present in the vacuole and the cell wall, and to a lesser extent in the cytosol of transgenic Nicotiana tabacum
-
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
metabolism
physiological function
additional information
evolution
Arthrobacter strain A3 has only two trehalose synthesis pathways (OtsA/B and TreS), while other Arthrobacter spp. have three
evolution
-
Arabidopsis thaliana has 11 TPS or TPS-like proteins, which belong to two distinct clades: class I (AtTPS1-AtTPS4) and class II (AtTPS5-AtTPS11)
evolution
the enzyme belongs to the glucosyltransferase-GTB-type superfamily; the enzyme belongs to the glucosyltransferase-GTB-type superfamily
evolution
-
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
-
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
-
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
-
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
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
metabolism
-
the first step in trehalose biosynthesis involves trehalose 6-phosphate synthase, Tps1
metabolism
in the OtsAB pathway, a trehalose-6-phosphate synthase (TPS, OtsA) catalyzes the formation of trehalose-6-phosphate from a glucosyl nucleotide and glucose-6-phosphate; in the OtsAB pathway, a trehalose-6-phosphate synthase (TPS, OtsA) catalyzes the formation of trehalose-6-phosphate from a glucosyl nucleotide and glucose-6-phosphate
metabolism
-
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; 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
Q1KLW0
the multifunctional protein, OtsA, is indispensable for bacterial survival in various environments. The catalytic efficiency of OtsA is affected by its N-loop at low temperatures. The flexibility of the OtsA N-loop is related to the growth temperature of the respective bacterial species
physiological function
regulation of OtsA expression during cold shock, both low temperature and accumulation of trehalose can inhibit OtsA expression, overview
physiological function
trehalose phosphate synthase is the crucial enzyme for the biosynthesis of trehalose, the main haemolymph sugar of insects
physiological function
trehalose phosphate synthase is the crucial enzyme for the biosynthesis of trehalose, the main haemolymph sugar of insects
physiological function
DvTPS increases the salt tolerance of the organism, overview
physiological function
-
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
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
-
enzyme TPS1 is important throughout the life cycle with At least three catalytically active TPS isoforms
physiological function
isozyme OstA2 mainly contributes to the trehalose pool of strain 1CP; isozyme OtsA1 seems to be involved in the overproduction of trehalose lipids
physiological function
in fungi, trehalose-6-phosphate synthase 1 plays a key role in the biosynthesis of trehalose
physiological function
-
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
-
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 enzyme functions as a cytoskeletal element regulating cell morphology
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
-
isozyme OstA2 mainly contributes to the trehalose pool of strain 1CP; isozyme OtsA1 seems to be involved in the overproduction of trehalose lipids
-
physiological function
Thermoproteus tenax ATCC 35583
-
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 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
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
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differences in muscle trehalose content in female and male animals due to polymorphisms; differences in muscle trehalose content in female and male animals due to polymorphisms; differences in muscle trehalose content in female and male animals due to polymorphisms; differences in muscle trehalose content in female and male animals due to polymorphisms
additional information
E1U2Z7
differences in muscle trehalose content in female and male animals due to polymorphisms; differences in muscle trehalose content in female and male animals due to polymorphisms; differences in muscle trehalose content in female and male animals due to polymorphisms; differences in muscle trehalose content in female and male animals due to polymorphisms
additional information
differences in muscle trehalose content in female and male animals due to polymorphisms; differences in muscle trehalose content in female and male animals due to polymorphisms; differences in muscle trehalose content in female and male animals due to polymorphisms; differences in muscle trehalose content in female and male animals due to polymorphisms
additional information
E1U2Z9
differences in muscle trehalose content in female and male animals due to polymorphisms; differences in muscle trehalose content in female and male animals due to polymorphisms; differences in muscle trehalose content in female and male animals due to polymorphisms; differences in muscle trehalose content in female and male animals due to polymorphisms
additional information
differences in muscle trehalose content in female and male animals due to polymorphisms; differences in muscle trehalose content in female and male animals due to polymorphisms; differences in muscle trehalose content in female and male animals due to polymorphisms; differences in muscle trehalose content in female and male animals due to polymorphisms
additional information
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trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase form a comp