Information on EC 2.4.1.15 - alpha,alpha-trehalose-phosphate synthase (UDP-forming)

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY hide
2.4.1.15
-
RECOMMENDED NAME
GeneOntology No.
alpha,alpha-trehalose-phosphate synthase (UDP-forming)
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Metabolic pathways
-
-
metabolism of disaccharids
-
-
Starch and sucrose metabolism
-
-
trehalose biosynthesis I
-
-
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)].
CAS REGISTRY NUMBER
COMMENTARY hide
9030-07-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
strain SN223/29
UniProt
Manually annotated by BRENDA team
strain SN223/29
UniProt
Manually annotated by BRENDA team
isolated from the alpine permafrost, CGMCC 1.8987, gene otsA
UniProt
Manually annotated by BRENDA team
gene otsA
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
trehalose 6-phosphate synthase 1
SwissProt
Manually annotated by BRENDA team
strain H99
SwissProt
Manually annotated by BRENDA team
strain H99
SwissProt
Manually annotated by BRENDA team
gene cftps; gene cftps
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
bifunctional trehalose 6-phospate synthase and trehalose 6-phospate phosphatase enzyme
-
-
Manually annotated by BRENDA team
gene TPS
UniProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
gene tps1
-
-
Manually annotated by BRENDA team
isoform TPS 1
-
-
Manually annotated by BRENDA team
-
Uniprot
Manually annotated by BRENDA team
This UniProt-ID has been deleted; strain AS.1416
-
-
Manually annotated by BRENDA team
strain C13-ABYS86 lacking vacuolar proteases
-
-
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
-
SwissProt
Manually annotated by BRENDA team
strain RQ-1, gene otsA
SwissProt
Manually annotated by BRENDA team
strain RQ-1, gene otsA
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
malfunction
metabolism
-
the first step in trehalose biosynthesis involves trehalose 6-phosphate synthase, Tps1
physiological function
additional information
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP-alpha-D-glucose + D-glucose 6-phosphate
ADP + alpha,alpha-1,1-trehalose 6-phosphate
show the reaction diagram
ADP-alpha-D-glucose + D-glucose 6-phosphate
ADP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
show the reaction diagram
CDP-glucose + D-glucose 6-phosphate
trehalose 6-phosphate + CDP
show the reaction diagram
dTDP-glucose + glucose 6-phosphate
trehalose 6-phosphate + dTDP
show the reaction diagram
-
-
-
-
?
GDP-alpha-D-glucose + D-glucose 6-phosphate
GDP + alpha,alpha-1,1-trehalose 6-phosphate
show the reaction diagram
GDP-alpha-D-glucose + D-glucose 6-phosphate
GDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
GDP-glucose + D-glucose 6-phosphate
trehalose 6-phosphate + GDP
show the reaction diagram
TDP-alpha-D-glucose + D-glucose 6-phosphate
TDP + alpha,alpha-1,1-trehalose 6-phosphate
show the reaction diagram
-
-
-
-
?
TDP-alpha-D-glucose + D-glucose 6-phosphate
TDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
TDP-glucose + glucose 6-phosphate
trehalose 6-phosphate + TDP
show the reaction diagram
UDP-alpha-D-glucose + D-fructose 6-phosphate
UDP + ?
show the reaction diagram
activity with D-fructose 6-phosphate is about 10% compared to the activity with D-glucose 6-phosphate
-
-
?
UDP-alpha-D-glucose + D-fructose 6-phosphate
UDP + alpha,alpha-1,1-trehalose 6-phosphate
show the reaction diagram
-
maximum activity with glucose 6-phosphate, followed by mannose 6-phosphate and fructose 6-phosphate
-
-
?
UDP-alpha-D-glucose + D-galactose 6-phosphate
UDP + ?
show the reaction diagram
activity with D-galactose 6-phosphate is about 10% compared to the activity with D-glucose 6-phosphate
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-1,1-trehalose 6-phosphate
show the reaction diagram
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
UDP-alpha-D-glucose + D-mannose 6-phosphate
UDP + ?
show the reaction diagram
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
show the reaction diagram
-
maximum activity with glucose 6-phosphate, followed by mannose 6-phosphate and fructose 6-phosphate
-
-
?
UDP-glucose + D-fructose 6-phosphate
UDP + ?
show the reaction diagram
-
16% of the activity with D-glucose 6-phosphate
-
-
?
UDP-glucose + D-galactose
UDP + ?
show the reaction diagram
-
17% of the activity with D-glucose 6-phosphate
-
-
?
UDP-glucose + D-glucose
UDP + ?
show the reaction diagram
-
28% of the activity with D-glucose 6-phosphate
-
-
?
UDP-glucose + lactose
UDP + ?
show the reaction diagram
-
10% of the activity with D-glucose 6-phosphate
-
-
?
UDP-glucose + sucrose
UDP + ?
show the reaction diagram
-
19% of the activity with D-glucose 6-phosphate
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-1,1-trehalose 6-phosphate
show the reaction diagram
-
step in trehalose biosynthesis
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ba2+
-
activation
Cd2+
-
activation
Cu2+
-
activates 33% at 5 mM
Fe2+
-
activation
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
KHCO3
-
100-300 mM, activation
MnCl2
-
stimulation
NaCl
-
an increase in the concentration of NaCl from 0 to 100 mM leads to a decrease in the OtsA activity by more than 35% when ADP-glucose or TDP-glucose is the substrate. When UDP-glucose or GDP-glucose is used as substrate, the OtsA activity is increased by 1030%
NaHCO3
-
100-300 mM, activation
Ni2+
-
activation
ZnCl2
-
stimulation
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
(NH4)2SO4
-
1 mM
2,6-diamino-4-(2,4-dichlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
2,6-diamino-4-(2-methylphenyl)-4H-thiopyran-3,5-dicarbonitrile
2,6-diamino-4-(3,4-dichlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
2,6-diamino-4-(3-bromophenyl)-4H-thiopyran-3,5-dicarbonitrile
2,6-diamino-4-(3-chlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
2,6-diamino-4-(3-fluorophenyl)-4H-thiopyran-3,5-dicarbonitrile
2,6-diamino-4-(3-iodophenyl)-4H-thiopyran-3,5-dicarbonitrile
2,6-diamino-4-(4,5-dihydrofuran-3-yl)-4H-thiopyran-3,5-dicarbonitrile
2,6-diamino-4-(4,5-dihydrothiophen-3-yl)-4H-thiopyran-3,5-dicarbonitrile
2,6-diamino-4-(4-bromo-5-ethylthiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
2,6-diamino-4-(4-bromo-5-methylthiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
2,6-diamino-4-(4-bromothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
2,6-diamino-4-(4-chlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
2,6-diamino-4-(4-methylphenyl)-4H-thiopyran-3,5-dicarbonitrile
2,6-diamino-4-(4-nitrophenyl)-4H-thiopyran-3,5-dicarbonitrile
2,6-diamino-4-(5-bromothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
2,6-diamino-4-(5-chlorothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
2,6-diamino-4-(5-ethylthiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
2,6-diamino-4-(5-nitrothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
2,6-diamino-4-(cyclohex-2-en-1-yl)-4H-thiopyran-3,5-dicarbonitrile
2,6-diamino-4-(cyclohex-3-en-1-yl)-4H-thiopyran-3,5-dicarbonitrile
2,6-diamino-4-cyclohexyl-4H-thiopyran-3,5-dicarbonitrile
2,6-diamino-4-phenyl-4H-thiopyran-3,5-dicarbonitrile
2,6-diamino-4-[3-(trifluoromethyl)phenyl]-4H-thiopyran-3,5-dicarbonitrile
2,6-diamino-4-[4-(trifluoromethyl)phenyl]-4H-thiopyran-3,5-dicarbonitrile
2-mercaptoethanol
10% (v/v), 9% inhibition
3-amino-4-formyl-2-[2-oxo-2-(tricyclo[3.3.1.13,7]dec-1-yl)ethyl]cyclopent-3-ene-1,1,2-tricarbonitrile
6-amino-4-(3,4-dichlorophenyl)-2-thioxo-1,2,3,4-tetrahydropyridine-3,5-dicarbonitrile
8-chloro-11-(piperazin-1-yl)-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridine
8-hydroxy-2,4-dimethyl-7H-chromen-7-one
Ag+
-
45% inhibition at 5 mM
AMP
-
10 mM 23% inhibition
ATP
-
slight
Ba2+
10 mM, 38% inhibition
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
Cd2+
-
slightly inhibitory
cellobiose
-
-
Cemusol NPT-12
-
weak inhibition
-
circulin
-
noncompetitive inhibition, inhibits reaction with either UDPglucose or GDPglucose as glucosyl donor. Preincubation with heparin prevents inhibition. 0.05 mg/ml-0.2 mg/ml: 50% inhibition
Citric acid
-
2.5 mM, 82% residual activity
deoxycholate
-
-
dithiothreitol
10 mM, 27% inhibition
Diumycin
-
competitive inhibition, inhibits reaction with either UDPglucose or GDPglucose as glucosyl donor. Preincubation with heparin prevents inhibition. 0.05 mg/ml: 50% inhibition
-
ethanol
10% (v/v), 28% inhibition
Fe2+
-
slightly inhibitory
GDPglucose
-
noncompetitive to UDPglucose
glucose 6-phosphate
-
high concentrations
guanidine hydrochloride
10 mM, 63% inhibition
Isopropanol
10% (v/v), 14% inhibition
K+
10 mM, 10% inhibition
methanol
10% (v/v), 30% inhibition
methyl 2-chloro-5-(5-[(Z)-[3-(2,4-dimethylphenyl)-4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene]methyl]furan-2-yl)benzoate
Mg2+
-
inhibition in presence of 1 mM UDP or 1 mM UTP
Moenomycin
-
competitive inhibition, inhibits reaction with either UDPglucose or GDPglucose as glucosyl donor. Preincubation with heparin prevents inhibition. Preincubation with heparin prevents inhibition. 0.05 mg/ml: 50% inhibition
n-butanol
10% (v/v), 48% inhibition
N-ethylmaleimide
Na+
10 mM, 8% inhibition
Ni2+
10 mM, 21% inhibition
O,O-diphenyl [(2E)-2-[2-(2-chlorophenyl)hydrazinylidene]-2-cyanoethanethioyl]phosphoramidothioate
phosphate
Poly-D-lysine
-
-
Poly-DL-lysine
-
-
Poly-DL-ornithine
-
-
Poly-L-ornithine
-
-
Polyribonucleotide inhibitor from Mycobacterium tuberculosis
-
-
-
Sodium azide
-
2.5 mM, 83% residual activity
trehalose
Triton X-100
-
weak inhibition
UDP
-
10 mM, 65% inhibition
UDPglucose
-
competitive to GDPglucose
UDPglucuronate
-
-
UMP
-
10 mM, 43% inhibition
Urea
10 mM, 15% inhibition
additional information
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Chondroitin
-
stimulation, particularly when a pyrimidine glucose nucleotide is used, rather than a purine glucose nucleotide
chondroitin sulfate
D-fructose 6-phosphate
-
-
dermatan sulfate
-
activation
gamma-Carragenan
-
activation
-
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
-
heparan sulfate
-
activation
heparin
iodoacetamide
iodoacetic acid
Polyanions
-
activation
-
Polynucleotides
-
activation
TPS-activator protein
-
activation
-
Triton X-100
-
activation
Tween 80
additional information
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6
ADP-glucose
-
37C, pH 5.5
0.27 - 7.1
D-glucose 6-phosphate
0.4 - 2.17
GDP-glucose
1 - 16
GDPglucose
1.2 - 8.3
glucose 6-phosphate
3.7 - 7
glucose-6-phosphate
2 - 2.38
TDP-glucose
0.2 - 1
UDP-alpha-D-glucose
0.3 - 9.6
UDP-glucose
0.04 - 18
UDPglucose
additional information
additional information
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3.2 - 6.7
glucose 6-phosphate
3.6 - 7.3
UDPglucose
additional information
additional information
Escherichia coli
-
bifunctional fusion enzyme of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
additional information
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2 - 5
phosphate
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.1
2,6-diamino-4-(2,4-dichlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
0.0002 - 0.0005
2,6-diamino-4-(3,4-dichlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
0.0012 - 0.0017
2,6-diamino-4-(3-bromophenyl)-4H-thiopyran-3,5-dicarbonitrile
0.0013
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 - 0.0061
2,6-diamino-4-(3-fluorophenyl)-4H-thiopyran-3,5-dicarbonitrile
0.0026 - 0.0049
2,6-diamino-4-(3-iodophenyl)-4H-thiopyran-3,5-dicarbonitrile
0.0918 - 0.1
2,6-diamino-4-(4,5-dihydrofuran-3-yl)-4H-thiopyran-3,5-dicarbonitrile
0.0631 - 0.1
2,6-diamino-4-(4,5-dihydrothiophen-3-yl)-4H-thiopyran-3,5-dicarbonitrile
0.1
2,6-diamino-4-(4-bromo-5-ethylthiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
0.0008 - 0.1
2,6-diamino-4-(4-bromo-5-methylthiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
0.004 - 0.011
2,6-diamino-4-(4-bromothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
0.0045 - 0.0149
2,6-diamino-4-(4-chlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
0.0129 - 0.0758
2,6-diamino-4-(4-methylphenyl)-4H-thiopyran-3,5-dicarbonitrile
0.0287 - 0.0419
2,6-diamino-4-(4-nitrophenyl)-4H-thiopyran-3,5-dicarbonitrile
0.0045 - 0.023
2,6-diamino-4-(5-bromothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
0.0059 - 0.0173
2,6-diamino-4-(5-chlorothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
0.0665 - 0.1
2,6-diamino-4-(5-ethylthiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
0.0054 - 0.0061
2,6-diamino-4-(5-nitrothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
0.0026 - 0.0029
2,6-diamino-4-(cyclohex-2-en-1-yl)-4H-thiopyran-3,5-dicarbonitrile
0.0031 - 0.0046
2,6-diamino-4-(cyclohex-3-en-1-yl)-4H-thiopyran-3,5-dicarbonitrile
0.0014 - 0.0019
2,6-diamino-4-cyclohexyl-4H-thiopyran-3,5-dicarbonitrile
0.1 - 789
2,6-diamino-4-phenyl-4H-thiopyran-3,5-dicarbonitrile
0.00371 - 0.00505
2,6-diamino-4-[3-(trifluoromethyl)phenyl]-4H-thiopyran-3,5-dicarbonitrile
0.1
2,6-diamino-4-[4-(trifluoromethyl)phenyl]-4H-thiopyran-3,5-dicarbonitrile
0.0014 - 0.0046
3-amino-4-formyl-2-[2-oxo-2-(tricyclo[3.3.1.13,7]dec-1-yl)ethyl]cyclopent-3-ene-1,1,2-tricarbonitrile
0.1
6-amino-4-(3,4-dichlorophenyl)-2-thioxo-1,2,3,4-tetrahydropyridine-3,5-dicarbonitrile
0.0062 - 0.0066
8-chloro-11-(piperazin-1-yl)-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridine
0.0086 - 0.0314
8-hydroxy-2,4-dimethyl-7H-chromen-7-one
0.0094 - 0.0147
methyl 2-chloro-5-(5-[(Z)-[3-(2,4-dimethylphenyl)-4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene]methyl]furan-2-yl)benzoate
0.0028 - 0.0055
O,O-diphenyl [(2E)-2-[2-(2-chlorophenyl)hydrazinylidene]-2-cyanoethanethioyl]phosphoramidothioate
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
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
0.055
-
TPS specific activity in galactose, yeast wild type + pSAL4
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
0.079
-
TPS specific activity in glucose, yeast wild type + pSAL4
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
0.096
-
crude enzyme, pH 8.5, 37C
0.127
-
UDPglucose
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
1.48
-
pH 8.5, 37C
2.03
-
purified native enzyme, pH 8.5, 37C
4.8
-
activity with UDPglucose
7.05
-
purified enzyme
20.6
purified recombinant enzyme, substrates GDP-glucose and D-glucose 6-phosphate
24.2
-
activity with GDPglucose
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
additional information
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
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
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 40
-
bifunctional fusion enzyme of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 20
catalytic activity of OtsA at 4C is 1.2fold greater than that at 20C
16 - 37
tested activity range
40 - 100
about half-maximal activity at 40C, 80% of maximal activity at 100C, inactive at 30C
50 - 80
50C: about 50% of maximal activity, 80C: about 75% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4.55
-
115 kDa enzyme polypeptide, isoelectric focusing
4.69
-
67 kDa enzyme polypeptide, isoelectric focusing
4.83
-
50 kDa enzyme polypeptide, isoelectric focusing
5.83
calculated from sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
correlation between TPS activity in hemocytes and hemolymph trehalose levels is found during the molt cycle
Manually annotated by BRENDA team
additional information
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
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
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Burkholderia xenovorans (strain LB400)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
45000
-
gel filtration
54000
-
MALDI-TOF MS analysis
56210
-
calculated from sequence of cDNA
59000
-
estimated by HPGPLC using a Ultropak G2000SW column and by SDS-PAGE
63000
-
gel filtration
100000
-
predicted molecular mass, verified by Western blot analysis
220000
-
gel filtration
300000
-
complex of EC 2.4.1.15/EC 3.1.3.12, gel filtration
440000
-
native PAGE
630000
-
gel filtration
additional information
-
3 aggregation forms of 230, 440, and 660 kDa contain polypeptides of 50, 67, and 115 kDa polypeptides, only the 440 kDa form is catalytically active, native PAGE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oligomer
-
x * 115000 + x * 57000, complex of EC 2.4.1.15/EC 3.1.3.12, SDS-PAGE
tetramer
additional information
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
glycoprotein
-
protein/sugar ratio is 10.75
no glycoprotein
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant enzyme complexed with either substrate UDP-glucose or the inactive substrate analogue UDP-2-deoxy-2-fluoroglucose, hanging drop vapour diffusion method, 100 nl droplets of 10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, and 200 mM NaCl, with either 25 mM UDP-glucose and 50 mM 1-deoxy-glucose 6-phosphate or 25 mM UDP-2-deoxy-2-fluoroglucose and 20 mM glucose 6-phosphate, precipitant solution: 30% w/v PEG 4000, 200 mM ammonium acetate, 100 mM Tris-HCl, pH 8.0, 36 h, 25% ethylene glycol as cryoprotectant, X-ray diffraction structure determination and analysis at 2.0 A resolution
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
2
6 h, more than half of the activity remains
727099
4.5
-
40 min, 19% residual activity
702423
5 - 8
-
-
704738
5 - 10
-
stable
657760
8.5
-
stable at alkaline pH values, 100% stability at pH 8.5
702423
9
6 h, more than half of the activity remains
727099
additional information
-
the three fractions (aggregates of trehalose 6-phosphate synthase) elute from ion exchange chromatography are stable in a pH 511 range
675977
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0 - 40
-
stable within
48
-
5 min, 44% of its original activity is recovered
55
-
5 min, 5% of its original activity is recovered
70
10 h, more than 30% of the original activity remains
80
half-life: 193 min
90
half-life: 54 min
100
half-life: 31 min
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
heparin helps to retain both stability and activity of the final purified enzyme
-
in phosphate or acetate buffers, the activity of TpS1 is decreased to 25% and 30%, respectively, of activity in Tris-HCl buffer
stabilization during purification, 10fold by addition of 20 mM MgCl2, 50 mM NaCl, 2 M glycine betaine and 5 mM mercaptoethanol
-
stable to at least 4 successive freeze/thaw cycles
-
stable to dialysis against either water or 0.1 M Tris-maleate buffer, pH 7.0
-
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-12C, stable for at least 11 weeks
-
-12C, stored as lyophilized powder, stable for 7 months
-
-18C, 2-3 d, no loss of activity
-
-20C, 1 mM Bis-Tris buffer, pH 6.3
-
4-6C, 2 d, enzyme retains 75% of its activity after 2 d and 25% of its activity after 3 d
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Arabidopsis thaliana extracts are prepared, AtTPS1 expressed in yeast is analysed in yeast extracts
-
bifunctional fusion enzyme of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase
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crude extract is prepared, the enzyme is isolated by ammonium sulfate fractionation and high performance gel permeation liquid chromatography, using a HiLoad 16/60 Superdex 200 and a Ultropak TSK G2000SW column
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glutathione-S-transferase-Tps1p fusion protein expressed in E. coli
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heparin helps to retain both stability and activity of the final purified enzyme
-
native enzyme 22.1fold to homogeneity by several gel filtration steps
-
native enzyme 50fold by ammonium sulfate fractionation, gel filtration, and nickel-resin affinity chromatography
-
partial
recombinant enzyme from Escherichia coli
recombinant His-tagged TPS1 from Escherichia coli strain BL21 by nickel affinity chromatography
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain B21(DE3) by nickel affinity chromatography
recombinant soluble MalE-CfTPS fusion protein from Escherichia coli Rosetta (DE3) cells partially by by amylose-agarose affinity chromatography
separation of three aggregates of trehalose 6-phosphate synthase (molecular weights of 624000 Da, 224000 Da and 107000 Da) by gel filtration and ion exchange chromatography
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trehalose-6-phosphate synthase/phosphatase complex, EC 2.4.1.15/EC 3.1.3.12
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a translational trehalose-6-phosphate synthase - trehalose-6-phosphate phosphatase, TPS-TPP, gene-fusion is constructed and subcloned into the pBluescript SK vector, into the yeast expression vector pSal4, and into the pBin19 vector for transformation of Arabidopsis thaliana
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Agrobacterium tumefaciens-mediated transformation of Nicotiana tabacum. The enzyme is markedly present in the vacuoles and the cell wall, and to a lesser extent in the cytosol
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construction of a bifunctional fusion enzyme of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase and expression in Escherichia coli
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construction of a new transformation vector containing the AtTPS1 gene as a selection marker. Overexpression of AtTPS1 in tobacco allows selecting glucose insensitive transgenic shoots
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DNA and amino acid sequence determination and analysis, overexpression in transgenic flies, functional expression in HEK-293 cells
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expression in Escherichia coli
expression in Pichia pastoris
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expression of glutathione-S-transferase-Tps1p fusion protein in Escherichia coli
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expression of the TPS1 gene in transgenic Solanum tuberosum, usage of potato wild-type drought-sensitive cultivar White Lady; expression of the TPS1 gene in transgenic Solanum tuberosum, usage of potato wild-type drought-sensitive cultivar White Lady
expression of TPS1 driven by the ABI3 promoter rescues the severe embryo phenotype but not the vegetative phenotype of tps1
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functional expression of the enzyme as a fusion protein with Escherichia coli trehalose-6-phosphate phosphatase in transgenic Oryza sativa plants
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functional expression of the enzyme as a fusion protein with Escherichia coli trehalose-6-phosphate phosphatase in transgenic Oryza sativa plants, expression in human fibroblasts
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gene cftps, DNA and amino acid sequence determination and anaysis, phylogenetic analysis, expression of largely soluble MalE-CfTPS fusion protein in Escherichia coli Rosetta (DE3) cells
gene dmtps1, phylgenetic analysis, expression of His-tagged TPS1 in Escherichia coli strain BL21
gene otsA, cloned from genetic library, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli strain BL21
gene otsA, DNA amnd amino acid sequence determination and analysis
gene otsA, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain B21(DE3)
gene tps, a single copy, genetic structure, DNA and amino acid sequence determination and analysis, wild-type realtime PCR expression and promoter region analysis, expression in Saccharomyces cerevisiae tps1DELTA mutant YSH290 strain leading to no functional complementation
gene TPS1, Saccharomyces cerevisiae strain 10151 is used as host strain for transformation and overexpression, strains EP-1 and 14801 are used for preparing chromosomal DNAs
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into the pDONOR207 vector and after confirming the sequence subcloned into the pBIN-GW binary vector, into the expression vector pYES2, for transformation of yeast cells
overexpression in Arabidopsis thaliana plants under control of the 35S promotor
-
overexpression in the Bombyx mori baculovirus expression system
overexpression of the enzyme incresases stress resistance of yeast cells
-
pET-based system in BL21 cells
-
preparation of a recombinant strain carrying multiple copies of ggsA by cotransformation
-
the shuttle vectors pSAL4 and pSAL6, the YEplac195/KanMX plasmid, and the two-hybrid plasmids pGBT9 and pGAD242 are used, GFP-fusions are generated using pK7GWF2 and pHGWR2
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the TPS1 gene of Saccharomyces cerevisiae is cloned into pBluescript II SK, in addition a binary vector for transformation of potato plants is constructed
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transgenic Arabidopsis plants with T6P levels increased by expression of T6P synthase or decreased by expression of T6P phosphatase in the cytosol. Compared with wild type, leaves of T6P synthase-expressing plants have increased redox activation of ADP-glucose pyrophosphorylase and increased starch
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
a transitory increase in the expression of TPS2 and TPS1 genes is promoted in wild-type cells inresponse to acute, but not to gentleoxidative exposure
-
both low temperature and accumulation of trehalose can inhibit OtsA expression, increase of trehalose in the first 2.3 h of cold shock
lipopolysaccharide treatment results in increase in expression, enzyme activity, and hemolymph trehalose levels
with the increase of the salt concentration in the medium, the expression of DvTPS has a slight decrease of 17% in 5 M NaCl compared with 0.5 M condition
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
H223Y
-
catalytically more active than wild-type enzyme
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
analysis
-
trehalose-6-phosphate synthase is an intrinsic selection marker for plant transformation
drug development
medicine
-
the enzyme should be a valuable target for chemotherapeutic intervention in tuberculosis
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