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

EC NUMBER
COMMENTARY
2.4.1.15
-
RECOMMENDED NAME
GeneOntology No.
alpha,alpha-trehalose-phosphate synthase (UDP-forming)
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
UDP-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-
-
-
-
UDP-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
ordered bi-bi mechanism
-
UDP-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
complex bimodal kinetics
-
UDP-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
reaction mechanism
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hexosyl group transfer
-
-
-
-
hexosyl group transfer
Q66Q98, -
-
hexosyl group transfer
-
-
hexosyl group transfer
-
-
PATHWAY
KEGG Link
MetaCyc Link
Metabolic pathways
-
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)].
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
alpha,alpha-trehalose phosphate synthase (UDP-forming)
-
-
-
-
alpha,alpha-trehalose-phosphate synthase (UDP-forming)
-
-
AtTPS6
Q94AH8
-
GbTPS
Q5D6D9
-
glucosyltransferase, uridine diphosphoglucose phosphate
-
-
-
-
OtsA
C7EZF1
-
OtsA
Q1KLW0
-
OtsA
C7EZF1
-
-
OtsA
Q1KLW0
-
-
phosphotrehalose-uridine diphosphate transglucosylase
-
-
-
-
T6P synthase
-
-
TPS
-
-
-
-
TPS
Cyberlindnera jadinii NCIM/ Y500
-
-
-
TPS
Thermus thermophilus RQ-1
Q7WUI7
-
-
TPS1
Cryptococcus neoformans H99
Q6IVK9
-
-
TPS1
Saccharomyces cerevisiae AS.1416
-
-
-
transglucosylase
-
-
-
-
trehalose 6-phosphate synthase
-
-
-
-
trehalose 6-phosphate synthase
-
-
trehalose 6-phosphate synthase
-
-
trehalose 6-phosphate synthase 1
B8QRI5
-
trehalose 6-phosphate synthase 1
-
-
trehalose 6-phosphate synthase 1
Saccharomyces cerevisiae AS.1416
-
-
-
trehalose 6-phosphate synthetase
-
-
-
-
trehalose phosphate synthase
-
-
-
-
trehalose phosphate synthase
J7G8S5
-
trehalose phosphate synthase
Q9Y119
-
trehalose phosphate synthetase
-
-
-
-
trehalose phosphate-uridine diphosphate glucosyltransferase
-
-
-
-
trehalose-6-P synthase
-
-
trehalose-6-phosphate synthase
-
-
trehalose-6-phosphate synthase
Q94AH8
-
trehalose-6-phosphate synthase
Q1KLW0
-
trehalose-6-phosphate synthase
Q1KLW0
-
-
trehalose-6-phosphate synthase
-
-
trehalose-6-phosphate synthase
J7G8S5
-
trehalose-6-phosphate synthase
-
-
trehalose-6-phosphate synthase
Cyberlindnera jadinii NCIM/ Y500
-
-
-
trehalose-6-phosphate synthase
-
-
trehalose-6-phosphate synthase
Q9Y119
-
trehalose-6-phosphate synthase
-
-
trehalose-6-phosphate synthase
C8XTB4
-
trehalose-6-phosphate synthase
-
-
trehalose-6-phosphate synthase
-
-
trehalose-6-phosphate synthase
-
-
trehalose-6-phosphate synthase
-
key subunit of the trehalose synthase complex
trehalose-6-phosphate synthase
-
-
trehalose-6-phosphate synthase
Q7WUI7
-
trehalose-6-phosphate synthase
Thermus thermophilus RQ-1
Q7WUI7
-
-
trehalose-6-phosphate synthase 1
-
-
trehalose-6-phosphate synthase 1
P31688, Q00764
-
trehalose-P synthetase
-
-
-
-
trehalosephosphate-UDP glucosyl transferase
-
-
-
-
UDPglucose-glucose-phosphate glucosyltransferase
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9030-07-3
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain SN223/29
UniProt
Manually annotated by BRENDA team
strain SN223/29
UniProt
Manually annotated by BRENDA team
gene otsA
UniProt
Manually annotated by BRENDA team
isolated from the alpine permafrost, CGMCC 1.8987, gene otsA
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
trehalose 6-phosphate synthase 1
SwissProt
Manually annotated by BRENDA team
strain H99
SwissProt
Manually annotated by BRENDA team
Cryptococcus neoformans H99
strain H99
SwissProt
Manually annotated by BRENDA team
gene cftps; gene cftps
UniProt
Manually annotated by BRENDA team
Cyberlindnera jadinii NCIM/ Y500
-
-
-
Manually annotated by BRENDA team
bifunctional trehalose 6-phospate synthase and trehalose 6-phospate phosphatase enzyme
-
-
Manually annotated by BRENDA team
gene otsA
-
-
Manually annotated by BRENDA team
gene tps1
-
-
Manually annotated by BRENDA team
isoform TPS 1
-
-
Manually annotated by BRENDA team
strain C13-ABYS86 lacking vacuolar proteases
-
-
Manually annotated by BRENDA team
This UniProt-ID has been deleted; strain AS.1416
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae AS.1416
This UniProt-ID has been deleted; strain AS.1416
-
-
Manually annotated by BRENDA team
Saccharomyces cerevisiae C13-ABYS86
strain C13-ABYS86 lacking vacuolar proteases
-
-
Manually annotated by BRENDA team
Hook. and Grev. Spring
-
-
Manually annotated by BRENDA team
strain RQ-1, gene otsA
SwissProt
Manually annotated by BRENDA team
Thermus thermophilus RQ-1
strain RQ-1, gene otsA
SwissProt
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
evolution
C7EZF1
Arthrobacter strain A3 has only two trehalose synthesis pathways (OtsA/B and TreS), while other Arthrobacter spp. have three
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
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
C7EZF1
regulation of OtsA expression during cold shock, both low temperature and accumulation of trehalose can inhibit OtsA expression, overview
physiological function
-, J7G8S5
trehalose phosphate synthase is the crucial enzyme for the biosynthesis of trehalose, the main haemolymph sugar of insects
physiological function
Q9Y119
trehalose phosphate synthase is the crucial enzyme for the biosynthesis of trehalose, the main haemolymph sugar of insects
physiological function
C8XTB4, -
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
-
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
-
metabolism
-
the first step in trehalose biosynthesis involves trehalose 6-phosphate synthase, Tps1
additional information
-
trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase form a complex
additional information
Cyberlindnera jadinii NCIM/ Y500
-
trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase form a complex
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ADP-glucose + D-glucose 6-phosphate
trehalose 6-phosphate + ADP
show the reaction diagram
-
-
-
-
?
ADP-glucose + D-glucose 6-phosphate
trehalose 6-phosphate + ADP
show the reaction diagram
-
-
-
-
?
ADP-glucose + D-glucose 6-phosphate
trehalose 6-phosphate + ADP
show the reaction diagram
-
13.4% of the activity with GDPglucose
-
-
?
ADP-glucose + D-glucose 6-phosphate
ADP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
Q7WUI7, -
less effective than UDP-glucose
-
-
?
ADP-glucose + D-glucose 6-phosphate
ADP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-
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-glucose + D-glucose 6-phosphate
ADP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
Cyberlindnera jadinii, Cyberlindnera jadinii NCIM/ Y500
-
ADP-glucose is the best donor substrate
-
-
?
ADP-glucose + D-glucose 6-phosphate
ADP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
Thermus thermophilus RQ-1
Q7WUI7
less effective than UDP-glucose
-
-
?
ADP-glucose + D-glucose 6-phosphate
ADP + alpha,alpha-1,1-trehalose 6-phosphate
show the reaction diagram
A8QX04
4% of the activity with UDP-glucose
-
-
?
CDP-glucose + D-glucose 6-phosphate
trehalose 6-phosphate + CDP
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-glucose + D-glucose 6-phosphate
trehalose 6-phosphate + GDP
show the reaction diagram
-
-
-
-
?
GDP-glucose + D-glucose 6-phosphate
trehalose 6-phosphate + GDP
show the reaction diagram
-
-
-
-
?
GDP-glucose + D-glucose 6-phosphate
trehalose 6-phosphate + GDP
show the reaction diagram
-
18.4% of the activity with UDP-glucose
-
-
?
GDP-glucose + D-glucose 6-phosphate
trehalose 6-phosphate + GDP
show the reaction diagram
-
13% of the activity with UDPglucose
-
-
?
GDP-glucose + D-glucose 6-phosphate
GDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
Q7WUI7, -
much less effective than UDP-glucose
-
-
?
GDP-glucose + D-glucose 6-phosphate
GDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-
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-glucose + D-glucose 6-phosphate
GDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
Cyberlindnera jadinii, Cyberlindnera jadinii NCIM/ Y500
-
cf. EC 2.4.1.36
-
-
?
GDP-glucose + D-glucose 6-phosphate
GDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
Thermus thermophilus RQ-1
Q7WUI7
much less effective than UDP-glucose
-
-
?
GDP-glucose + D-glucose 6-phosphate
GDP + alpha,alpha-1,1-trehalose 6-phosphate
show the reaction diagram
-
-
-
-
?
TDP-glucose + D-glucose 6-phosphate
TDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-
-
-
-
?
TDP-glucose + D-glucose 6-phosphate
TDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
Q7WUI7, -
less effective than UDP-glucose
-
-
?
TDP-glucose + D-glucose 6-phosphate
TDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-
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-glucose + D-glucose 6-phosphate
TDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
Cyberlindnera jadinii NCIM/ Y500
-
-
-
-
?
TDP-glucose + D-glucose 6-phosphate
TDP + alpha,alpha-1,1-trehalose 6-phosphate
show the reaction diagram
-
-
-
-
?
TDP-glucose + glucose 6-phosphate
trehalose 6-phosphate + TDP
show the reaction diagram
-
-
-
-
?
TDP-glucose + glucose 6-phosphate
trehalose 6-phosphate + TDP
show the reaction diagram
-
15.9% of the activity with UDPglucose
-
-
?
UDP-glucose + D-fructose 6-phosphate
UDP + ?
show the reaction diagram
-
16% of the activity with D-glucose 6-phosphate
-
-
?
UDP-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-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 + D-glucose 6-phosphate
UDP + alpha,alpha-1,1-trehalose 6-phosphate
show the reaction diagram
-
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-1,1-trehalose 6-phosphate
show the reaction diagram
A8QX04
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-1,1-trehalose 6-phosphate
show the reaction diagram
B5TD29, -
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-1,1-trehalose 6-phosphate
show the reaction diagram
-
step in trehalose biosynthesis
-
-
?
UDP-glucose + D-glucose 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-glucose 6-phosphate
UDP + alpha,alpha-1,1-trehalose 6-phosphate
show the reaction diagram
A8QX04
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
Q66Q98, -
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
Q6IVK9
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
Q94AH8
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
P31688, Q00764
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-, Q1KLW0
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
C7EZF1
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
Q9Y119
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-, J7G8S5
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
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
show the reaction diagram
-
first step in trehalose biosynthesis, enzyme is essential for embryo maturation
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-
step in trehalose biosynthesis
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-
step in trehalose biosynthesis
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-
step in trehalose biosynthesis
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-
step in trehalose biosynthesis
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-
step in trehalose biosynthesis
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
Q7WUI7, -
best substrates, absolutely specific for D-glucose 6-phosphate
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-
the enzyme is highly specific for UDP-glucose and D-glucose 6-phosphate
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-
with retention of the anomeric configuration of the UDP-sugar donor, reaction stereochemistry
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
Q6IVK9
both TPS1 and TPS2 are required for high-temperature (37C) 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-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-
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-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
Q9Y119
the enzyme is substrate-specific
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-, J7G8S5
the enzyme is substrate-specific
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
Q1KLW0
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
Saccharomyces cerevisiae AS.1416
-
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
Cyberlindnera jadinii NCIM/ Y500
-
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
C7EZF1
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
Thermus thermophilus RQ-1
Q7WUI7
first step in one of 2 existing trehalose biosynthesis pathways, plays a role in osmoadaptation, best substrates, absolutely specific for D-glucose 6-phosphate
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
Cryptococcus neoformans H99
Q6IVK9
-, both TPS1 and TPS2 are required for high-temperature (37C) 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-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 + 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
-
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
show the reaction diagram
-
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
show the reaction diagram
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
show the reaction diagram
-
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
show the reaction diagram
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
show the reaction diagram
-
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
show the reaction diagram
-
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
show the reaction diagram
-
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
show the reaction diagram
-
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
show the reaction diagram
Q9SYM4
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
show the reaction diagram
-
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
show the reaction diagram
-
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
show the reaction diagram
-
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
show the reaction diagram
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
show the reaction diagram
-
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
show the reaction diagram
-
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
show the reaction diagram
-
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
show the reaction diagram
-
absolute specificity for glucose 6-phosphate
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
show the reaction diagram
-
absolute specificity for glucose 6-phosphate
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
show the reaction diagram
-
absolute specificity for glucose 6-phosphate
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
show the reaction diagram
-
specific for UDPglucose, no reaction with ADPglucose or GDPglucose
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
show the reaction diagram
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
AtTPS1 is a single-copy gene and is expressed constitutively at very low levels
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
show the reaction diagram
-
the enzyme does not play a role in the control of glycolysis
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
show the reaction diagram
-
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
show the reaction diagram
-
key enzyme for biosynthesis of trehalose, the major soluble carbohydrate in resting cells
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
show the reaction diagram
-
the enzyme plays a role in the control of glycolysis
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
show the reaction diagram
Saccharomyces cerevisiae C13-ABYS86
-
-, key enzyme for biosynthesis of trehalose, the major soluble carbohydrate in resting cells
-
?
GDP-glucose + D-glucose 6-phosphate
GDP + alpha,alpha-1,1-trehalose 6-phosphate
show the reaction diagram
A8QX04
23% of the activity with UDP-glucose
-
-
?
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
?
-
-
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
?
-
-
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 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
?
-
-
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
?
-
Q7WUI7, -
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
?
-
-
substrate specificity, no activity with trehalose, maltose, or fructose as acceptor substrates
-
-
-
additional information
?
-
-
the trehalose-6-phosphate synthase/phosphatase (OtsAOtsB) pathway plays an important role in the synthesis of trehalose in response to stress
-
-
-
additional information
?
-
-
TPS1 may play a major role in coordinating cell wall biosynthesis and cell division with cellular metabolism during embryo development
-
-
-
additional information
?
-
A8QX04
no substrate: CDP-glucose, fructose 6-phosphate
-
-
-
additional information
?
-
-
no substrates: fructose, fructose 6-phosphate, glucose, sucrose, and trehalose
-
-
-
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
?
-
C8XTB4, -
yeast functional complementation analysis shows that DvTPS has neither trehalose-6-phosphate synthase nor trehalose-6-phosphate phospatase activity
-
-
-
additional information
?
-
Cyberlindnera jadinii NCIM/ Y500
-
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
?
-
A8QX04
no substrate: CDP-glucose, fructose 6-phosphate
-
-
-
additional information
?
-
Thermus thermophilus RQ-1
Q7WUI7
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-1,1-trehalose 6-phosphate
show the reaction diagram
-
step in trehalose biosynthesis
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
Q66Q98, -
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
Q94AH8
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
P31688, Q00764
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-, Q1KLW0
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
C7EZF1
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
Q9Y119
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-, J7G8S5
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
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
show the reaction diagram
-
first step in trehalose biosynthesis, enzyme is essential for embryo maturation
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-
step in trehalose biosynthesis
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-
step in trehalose biosynthesis
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-
step in trehalose biosynthesis
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-
step in trehalose biosynthesis
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
-
step in trehalose biosynthesis
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
Q6IVK9
both TPS1 and TPS2 are required for high-temperature (37C) 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-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
Q1KLW0
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
Cyberlindnera jadinii NCIM/ Y500
-
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
C7EZF1
-
-
-
?
UDP-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
Thermus thermophilus RQ-1
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
show the reaction diagram
Cryptococcus neoformans H99
Q6IVK9
both TPS1 and TPS2 are required for high-temperature (37C) 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
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
show the reaction diagram
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
show the reaction diagram
-
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
show the reaction diagram
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
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
show the reaction diagram
-
AtTPS1 is a single-copy gene and is expressed constitutively at very low levels
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
show the reaction diagram
-
the enzyme does not play a role in the control of glycolysis
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
show the reaction diagram
-
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
show the reaction diagram
-
key enzyme for biosynthesis of trehalose, the major soluble carbohydrate in resting cells
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
show the reaction diagram
-
the enzyme plays a role in the control of glycolysis
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
show the reaction diagram
Saccharomyces cerevisiae C13-ABYS86
-
key enzyme for biosynthesis of trehalose, the major soluble carbohydrate in resting cells
-
?
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
?
-
-
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
?
-
-
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 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
?
-
-
the trehalose-6-phosphate synthase/phosphatase (OtsAOtsB) pathway plays an important role in the synthesis of trehalose in response to stress
-
-
-
additional information
?
-
-
TPS1 may play a major role in coordinating cell wall biosynthesis and cell division with cellular metabolism during embryo development
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ba2+
-
activation
Ca2+
-
activation
Ca2+
-
activates at physiological concentrations
Cd2+
-
activation
Co2+
-
activation
Co2+
Q7WUI7, -
stimulates
Cu2+
-
activates 33% at 5 mM
Fe2+
-
activation
K+
-
maximal activation at 400 mM KCl
K+
-
strongly stimulates
K+
-
activates maximal at 50 mM by 176%, 160% at 400 mM
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
Mg2+
-
optimal concentration is 1-2 mM
Mg2+
-
optimal concentration: 3-6 mM MgCl2
Mg2+
-
activation
Mg2+
-
20 mM, enhances 2fold; activation
Mg2+
-
activation
Mg2+
-
25 mM, 2fold increase of activity
Mg2+
-
2fold stimulation at 5 mM
Mg2+
-
activation
Mg2+
-
activates at low concentration up to 5 mM
Mg2+
Q7WUI7, -
stimulates
Mg2+
-
10 mM, required for maximal activity
Mg2+
A8QX04
95% stimulation
Mg2+
-
2.5fold activation at 5 mM, best at 70 mM
Mn2+
-
activation
Mn2+
-
10 mM, 2fold increase of activity
Mn2+
A8QX04
20% stimulation
Mn2+
-
best divalent cation, 2.6fold activation at 5 mM, best at 70 mM
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
Zn2+
-
activation
Zn2+
-
2.2fold activation at 5 mM
ZnCl2
-
stimulation
MnCl2
-
stimulation
additional information
-
no effect by Na+
additional information
Q7WUI7, -
no requirement for divalent cations for activity
additional information
-
no or poor effects by CoCl2, CaCl2, BaCl2, and FeSO4
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2,6-diamino-4-(2,4-dichlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
-, J7G8S5
-
2,6-diamino-4-(2,4-dichlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
Q9Y119
-
2,6-diamino-4-(2-methylphenyl)-4H-thiopyran-3,5-dicarbonitrile
-, J7G8S5
-
2,6-diamino-4-(2-methylphenyl)-4H-thiopyran-3,5-dicarbonitrile
Q9Y119
-
2,6-diamino-4-(3,4-dichlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
-, J7G8S5
-
2,6-diamino-4-(3,4-dichlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
Q9Y119
-
2,6-diamino-4-(3-bromophenyl)-4H-thiopyran-3,5-dicarbonitrile
-, J7G8S5
-
2,6-diamino-4-(3-bromophenyl)-4H-thiopyran-3,5-dicarbonitrile
Q9Y119
-
2,6-diamino-4-(3-chlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
-, J7G8S5
-
2,6-diamino-4-(3-chlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
Q9Y119
-
2,6-diamino-4-(3-fluorophenyl)-4H-thiopyran-3,5-dicarbonitrile
-, J7G8S5
-
2,6-diamino-4-(3-fluorophenyl)-4H-thiopyran-3,5-dicarbonitrile
Q9Y119
-
2,6-diamino-4-(3-iodophenyl)-4H-thiopyran-3,5-dicarbonitrile
-, J7G8S5
-
2,6-diamino-4-(3-iodophenyl)-4H-thiopyran-3,5-dicarbonitrile
Q9Y119
-
2,6-diamino-4-(4,5-dihydrofuran-3-yl)-4H-thiopyran-3,5-dicarbonitrile
-, J7G8S5
-
2,6-diamino-4-(4,5-dihydrofuran-3-yl)-4H-thiopyran-3,5-dicarbonitrile
Q9Y119
-
2,6-diamino-4-(4,5-dihydrothiophen-3-yl)-4H-thiopyran-3,5-dicarbonitrile
-, J7G8S5
-
2,6-diamino-4-(4,5-dihydrothiophen-3-yl)-4H-thiopyran-3,5-dicarbonitrile
Q9Y119
-
2,6-diamino-4-(4-bromo-5-ethylthiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
-, J7G8S5
-
2,6-diamino-4-(4-bromo-5-ethylthiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
Q9Y119
-
2,6-diamino-4-(4-bromo-5-methylthiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
-, J7G8S5
-
2,6-diamino-4-(4-bromo-5-methylthiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
Q9Y119
-
2,6-diamino-4-(4-bromothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
-, J7G8S5
-
2,6-diamino-4-(4-bromothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
Q9Y119
-
2,6-diamino-4-(4-chlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
-, J7G8S5
-
2,6-diamino-4-(4-chlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
Q9Y119
-
2,6-diamino-4-(4-methylphenyl)-4H-thiopyran-3,5-dicarbonitrile
-, J7G8S5
-
2,6-diamino-4-(4-methylphenyl)-4H-thiopyran-3,5-dicarbonitrile
Q9Y119
-
2,6-diamino-4-(4-nitrophenyl)-4H-thiopyran-3,5-dicarbonitrile
-, J7G8S5
-
2,6-diamino-4-(4-nitrophenyl)-4H-thiopyran-3,5-dicarbonitrile
Q9Y119
-
2,6-diamino-4-(5-bromothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
-, J7G8S5
-
2,6-diamino-4-(5-bromothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
Q9Y119
-
2,6-diamino-4-(5-chlorothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
-, J7G8S5
-
2,6-diamino-4-(5-chlorothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
Q9Y119
-
2,6-diamino-4-(5-ethylthiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
-, J7G8S5
-
2,6-diamino-4-(5-ethylthiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
Q9Y119
-
2,6-diamino-4-(5-nitrothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
-, J7G8S5
-
2,6-diamino-4-(5-nitrothiophen-2-yl)-4H-thiopyran-3,5-dicarbonitrile
Q9Y119
-
2,6-diamino-4-(cyclohex-2-en-1-yl)-4H-thiopyran-3,5-dicarbonitrile
-, J7G8S5
-
2,6-diamino-4-(cyclohex-2-en-1-yl)-4H-thiopyran-3,5-dicarbonitrile
Q9Y119
-
2,6-diamino-4-(cyclohex-3-en-1-yl)-4H-thiopyran-3,5-dicarbonitrile
-, J7G8S5
-
2,6-diamino-4-(cyclohex-3-en-1-yl)-4H-thiopyran-3,5-dicarbonitrile
Q9Y119
-
2,6-diamino-4-cyclohexyl-4H-thiopyran-3,5-dicarbonitrile
-, J7G8S5
-
2,6-diamino-4-cyclohexyl-4H-thiopyran-3,5-dicarbonitrile
Q9Y119
-
2,6-diamino-4-phenyl-4H-thiopyran-3,5-dicarbonitrile
-, J7G8S5
-
2,6-diamino-4-phenyl-4H-thiopyran-3,5-dicarbonitrile
Q9Y119
-
2,6-diamino-4-[3-(trifluoromethyl)phenyl]-4H-thiopyran-3,5-dicarbonitrile
-, J7G8S5
-
2,6-diamino-4-[3-(trifluoromethyl)phenyl]-4H-thiopyran-3,5-dicarbonitrile
Q9Y119
-
2,6-diamino-4-[4-(trifluoromethyl)phenyl]-4H-thiopyran-3,5-dicarbonitrile
-, J7G8S5
-
2,6-diamino-4-[4-(trifluoromethyl)phenyl]-4H-thiopyran-3,5-dicarbonitrile
Q9Y119
-
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
-, J7G8S5
-
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
Q9Y119
-
6-amino-4-(3,4-dichlorophenyl)-2-thioxo-1,2,3,4-tetrahydropyridine-3,5-dicarbonitrile
-, J7G8S5
-
6-amino-4-(3,4-dichlorophenyl)-2-thioxo-1,2,3,4-tetrahydropyridine-3,5-dicarbonitrile
Q9Y119
-
8-chloro-11-(piperazin-1-yl)-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridine
-, J7G8S5
-
8-chloro-11-(piperazin-1-yl)-6,11-dihydro-5H-benzo[5,6]cyclohepta[1,2-b]pyridine
Q9Y119
-
8-hydroxy-2,4-dimethyl-7H-chromen-7-one
-, J7G8S5
-
8-hydroxy-2,4-dimethyl-7H-chromen-7-one
Q9Y119
-
Ag+
-
45% inhibition at 5 mM
AMP
-
10 mM 23% 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
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
Diumycin
-
competitive inhibition, inhibits reaction with either UDPglucose or GDPglucose as glucosyl donor. Preincubation with heparin prevents inhibition. 0.05 mg/ml: 50% inhibition
-
Fe2+
-
slightly inhibitory
-
GDPglucose
-
noncompetitive to UDPglucose
glucose 6-phosphate
-
high concentrations
methyl 2-chloro-5-(5-[(Z)-[3-(2,4-dimethylphenyl)-4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene]methyl]furan-2-yl)benzoate
-, J7G8S5
-
methyl 2-chloro-5-(5-[(Z)-[3-(2,4-dimethylphenyl)-4-oxo-2-thioxo-1,3-thiazolidin-5-ylidene]methyl]furan-2-yl)benzoate
Q9Y119
-
Mg2+
-
inhibition in presence of 1 mM UDP or 1 mM UTP
N-ethylmaleimide
-
1 mM, 83% residual activity
N-ethylmaleimide
-
68% inhibition at 1 mM
NaCl
-
25 mM or higher
NaCl
-
0.2 M, 35% loss of activity
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%
O,O-diphenyl [(2E)-2-[2-(2-chlorophenyl)hydrazinylidene]-2-cyanoethanethioyl]phosphoramidothioate
-, J7G8S5
-
O,O-diphenyl [(2E)-2-[2-(2-chlorophenyl)hydrazinylidene]-2-cyanoethanethioyl]phosphoramidothioate
Q9Y119
-
phosphate
-
33 mM, 50% inhibition
phosphate
-
noncompetitive with respect to noth UDPglucose or glucose 6-phosphate; potent noncompetitive inhibitor
phosphate
-
enzyme is less sensitive to in vitro inhibition at 50C than at 30C. Fructose-6-phosphate partially relieves the inhibitory effect of phosphate at 30C but not at 50C
phosphate
-
10 mM, 85% inhibition
Poly-DL-ornithine
-
-
Poly-L-ornithine
-
-
Polyribonucleotide inhibitor from Mycobacterium tuberculosis
-
-
-
Sodium azide
-
2.5 mM, 83% residual activity
trehalose
-
non-competitive
trehalose
-
non-competitive to UDPglucose
Triton X-100
-
weak inhibition
UDP
-
10 mM, 65% inhibition
UDPglucose
-
competitive to GDPglucose
UMP
-
10 mM, 43% inhibition
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
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
-
additional information
A8QX04
not inhibitory: 2-mercaptoethanol
-
additional information
-, J7G8S5
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
Q9Y119
inhibitor screening amongst over 115000 synthetic compounds, structure-function relationship analysis of 4-substituted 2,6-diamino-3,5-dicyano-4H-thiopyrans, overview
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
CDTA
-
2.5 mM, 134% of initial activity
Chondroitin
-
stimulation, particularly when a pyrimidine glucose nucleotide is used, rather than a purine glucose nucleotide
chondroitin sulfate
-
activation
chondroitin sulfate
-
activation; chondroitin 4-sulfate, chondroitin 6-sulfate
chondroitin sulfate
-
activation
chondroitin sulfate
-
polyanions heparin and chondroitin sulfate stimulate TPS activity with different glucosyl donors
D-fructose 6-phosphate
-
-
dermatan sulfate
-
activation
EDTA
-
2.5 mM, 121% of initial activity
gamma-Carragenan
-
activation
-
Heparan sulfate
-
activation
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
-
polyanions heparin and chondroitin sulfate stimulate TPS activity with different glucosyl donors
iodoacetamide
-
1 mM, 245% of initial activity
iodoacetamide
-
activates 39% at 1 mM
iodoacetic acid
-
0.1 mM, 185% of initial activity
Polyanions
-
activation
-
Polynucleotides
-
activation
RNA
-
various RNA, particularly that isolated from Mycobacterium smegmatis chondroitin sulfate, activate
TPS-activator protein
-
activation
-
Triton X-100
-
activation
Tween 80
-
activation
Tween 80
-
slight activation
iodoacetic acid
-
activates 47.5% at 1 mM
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
-
no effect by sucrose and trehalose up tp 0.4 M
-
additional information
-
dependence on polyanion concentrations for optimum TPS activity, overview
-
additional information
C7EZF1
increase of trehalose in the first 2-3 h of cold shock
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.6
-
ADP-glucose
-
37C, pH 5.5
0.8
-
D-glucose 6-phosphate
Q7WUI7, -
recombinant enzyme, pH 7.0, 80C, in presence of Mg2+
3
-
D-glucose 6-phosphate
-
37C, pH 5.5, cosubstrate: UDP-glucose
3.9
-
D-glucose 6-phosphate
-
pH 7.0, 30C
4.2
-
D-glucose 6-phosphate
-
37C, pH 5.5, cosubstrate: ADP-glucose
4.5
-
D-glucose 6-phosphate
-
pH 8.5, 37C
5.3
-
D-glucose 6-phosphate
-
37C, pH 5.5, cosubstrate: TDP-glucose
7.1
-
D-glucose 6-phosphate
-
37C, pH 5.5, cosubstrate: GDP-glucose
0.4
-
GDP-glucose
-
37C, pH 5.5
2.17
-
GDP-glucose
-
pH 8.5, 37C
1
-
GDPglucose
-
in absence or presence of a polyanion
1
-
glucose 6-phosphate
-
reaction with GDPglucose
1.2
-
glucose 6-phosphate
-
reaction with UDPglucose
2
-
glucose 6-phosphate
-
-
2
-
glucose 6-phosphate
-
GDPglucose
3.5
-
glucose 6-phosphate
-
-
5
-
glucose 6-phosphate
-
-
7.5
-
glucose 6-phosphate
-
bifunctional fusion enzyme of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase
8.3
-
glucose 6-phosphate
-
-
3.7
-
glucose-6-phosphate
-
-
4
-
glucose-6-phosphate
-
with GDPglucose as glucosyl donor
2
-
TDP-glucose
-
37C, pH 5.5
2.38
-
TDP-glucose
-
pH 8.5, 37C
0.3
-
UDP-glucose
-
37C, pH 5.5
0.5
-
UDP-glucose
Q7WUI7, -
recombinant enzyme, pH 7.0, 80C, in presence of Mg2+
2
-
UDP-glucose
-
pH 8.5, 37C
9.6
-
UDP-glucose
-
pH 7.0, 30C
0.04
-
UDPglucose
-
in presence of optimal concentration of a polyanion
0.3
-
UDPglucose
-
-
0.8
-
UDPglucose
-
-
1.6
-
UDPglucose
-
-
5.1
-
UDPglucose
-
bifunctional fusion enzyme of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase
8.6
-
UDPglucose
-
-
7
-
glucose-6-phosphate
-
with UDPglucose as glucosyl donor
additional information
-
additional information
-
complex bimodal kinetics
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
bifunctional fusion enzyme of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase
-
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
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
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
7.3
-
UDPglucose
-
-
6.7
-
glucose 6-phosphate
-
-
additional information
-
additional information
-
bifunctional fusion enzyme of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase
-
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
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
0
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.1
-
2,6-diamino-4-(2,4-dichlorophenyl)-4H-thiopyran-3,5-dicarbonitrile
-, 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
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
-, 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
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
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
-, 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
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
-, 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
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
-, 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
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
-, 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
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
-, 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
-, 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
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
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
-, 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
-, 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
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
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
-, 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
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
-, 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
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
-, 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
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
-, 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
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
-, 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
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
-, 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
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
-, 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
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
-, 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
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
-, 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
-, 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
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
-, 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
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
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
-, 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
-, 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
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
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
-, 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
-, 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
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
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
-, 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
-, 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
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
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
-, 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
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
-, 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
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
-, 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
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
-, 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
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
0.055
-
-
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
1.58
-
-
preparation of trehalose-6-phosphate synthase from Saccharomyces cerevisiae, preparation step HPGPLC on HiLoad 16/60 Superdex 200
1.58
-
-
pH 8.5, 37C, presence of heparin
2.03
-
-
purified native enzyme, pH 8.5, 37C
4.8
-
-
activity with UDPglucose
7.05
-
-
purified enzyme
20.6
-
Q7WUI7, -
purified recombinant enzyme, substrates GDP-glucose and D-glucose 6-phosphate
24.2
-
-
activity with GDPglucose
95
-
Q7WUI7, -
purified recombinant enzyme, substrates ADP-glucose and D-glucose 6-phosphate
106.7
-
Q7WUI7, -
purified recombinant enzyme, substrates TDP-glucose and D-glucose 6-phosphate
149.6
-
Q7WUI7, -
purified recombinant enzyme, substrates UDP-glucose and D-glucose 6-phosphate
additional information
-
-
-
additional information
-
-
the activity of trehalose-6-phosphate synthase is concentration dependent
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
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.3
-
-
activity with ADP-glucose, UDP-glucose and TDP-glucose
5.5
-
-
activitry with GDP-glucose
6
-
Q7WUI7, -
-
6.5
-
-
potassium phosphate buffer
7
-
-
Tris/HCl buffer
7.5
-
A8QX04
-
7.5
-
-, Q1KLW0
assay at
7.5
-
-, J7G8S5
assay at
7.5
-
Q9Y119
assay at
8.5
-
-
activity assay
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
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
5.5
8
-
pH 5.5: about 75% of maximal activity, pH 8.0: about 70% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
C7EZF1
-
22
-
-, J7G8S5
assay at room temperature
22
-
Q9Y119
assay at room temperature
30
40
-
bifunctional fusion enzyme of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase
35
-
A8QX04
-
37
-
-
activity assay
37
-
-, Q1KLW0
assay at
98
-
Q7WUI7, -
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
20
C7EZF1
catalytic activity of OtsA at 4C is 1.2fold greater than that at 20C
16
37
-, Q1KLW0
tested activity range
40
100
Q7WUI7, -
about half-maximal activity at 40C, 80% of maximal activity at 100C, inactive at 30C
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
-
-, Q5D6D9
calculated from sequence
6.1
-
A8D372
calculated
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
B8QRI5, -
correlation between TPS activity in hemocytes and hemolymph trehalose levels is found during the molt cycle
Manually annotated by BRENDA team
-, Q5D6D9
expression of GbTPS is up-regulated by cold, NaCl, mannitol and drought treatments
Manually annotated by BRENDA team
-, Q5D6D9
expression of GbTPS is up-regulated by cold, NaCl, mannitol and drought treatments
Manually annotated by BRENDA team
additional information
-
expression of AtTPS1 is low and not organ specific
Manually annotated by BRENDA team
additional information
-
very low levels of trehalose in plant tissue
Manually annotated by BRENDA team
additional information
B5TD29, -
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
Manually annotated by BRENDA team
additional information
C8XTB4, -
DvTPS expression pattern, overview
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
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
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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 ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 55000, isozyme TPS1, x * 100000, isozyme TPS2, x * 105000, isozyme TPS3, SDS-PAGE; x * 56200, calculation from nucleotide sequence
?
-
x * 45000, aggregation to dimer or oligomer, SDS-PAGE
?
Q7WUI7, -
x * 52000, recombinant enzyme, SDS-PAGE
?
-, Q5D6D9
x * 97000, calculated from sequence
?
A8QX04
x * 51000, calculated
?
B5TD29, -
x * 60000, SDS-PAGE
?
A8D372
x * 91976, calculated
?
-
x * 58000, SDS-PAGE
?
-
x * 60000, SDS-PAGE
?
-
x * 51000, calculated
-
?
Cyberlindnera jadinii NCIM/ Y500
-
x * 60000, SDS-PAGE
-
?
Saccharomyces cerevisiae C13-ABYS86
-
x * 55000, isozyme TPS1, x * 100000, isozyme TPS2, x * 105000, isozyme TPS3, SDS-PAGE; x * 56200, calculation from nucleotide sequence
-
oligomer
-
x * 115000 + x * 57000, complex of EC 2.4.1.15/EC 3.1.3.12, SDS-PAGE
tetramer
-
4 * 58000, SDS-PAGE
tetramer
-
4 * 115000, SDS-PAGE
?
Thermus thermophilus RQ-1
-
x * 52000, recombinant enzyme, SDS-PAGE
-
additional information
-
Tps1p subunit exhibits TPS catalytic activity in the absence of other TPS complex proteins
additional information
-
two domain enzyme
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
protein/sugar ratio is 10.75
no glycoprotein
-
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.5
-
-
40 min, 19% residual activity
8.5
-
-
stable at alkaline pH values, 100% stability at pH 8.5
additional information
-
-
the three fractions (aggregates of trehalose 6-phosphate synthase) elute from ion exchange chromatography are stable in a pH 511 range
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
80
-
Q7WUI7, -
half-life: 193 min
90
-
Q7WUI7, -
half-life: 54 min
100
-
Q7WUI7, -
half-life: 31 min
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
in phosphate or acetate buffers, the activity of TpS1 is decreased to 25% and 30%, respectively, of activity in Tris-HCl buffer
A8QX04
stable to at least 4 successive freeze/thaw cycles
-
stabilization during purification, 10fold by addition of 20 mM MgCl2, 50 mM NaCl, 2 M glycine betaine and 5 mM mercaptoethanol
-
stable to dialysis against either water or 0.1 M Tris-maleate buffer, pH 7.0
-
heparin helps to retain both stability and activity of the final purified enzyme
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-12C, stable for at least 11 weeks
-
4-6C, 2 d, enzyme retains 75% of its activity after 2 d and 25% of its activity after 3 d
-
-18C, 2-3 d, no loss of activity
-
-12C, stored as lyophilized powder, stable for 7 months
-
-20C, 1 mM Bis-Tris buffer, pH 6.3
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
Arabidopsis thaliana extracts are prepared, AtTPS1 expressed in yeast is analysed in yeast extracts
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain B21(DE3) by nickel affinity chromatography
-, Q1KLW0
recombinant soluble MalE-CfTPS fusion protein from Escherichia coli Rosetta (DE3) cells partially by by amylose-agarose affinity chromatography
-, J7G8S5
native enzyme 22.1fold to homogeneity by several gel filtration steps
-
recombinant His-tagged TPS1 from Escherichia coli strain BL21 by nickel affinity chromatography
Q9Y119
bifunctional fusion enzyme of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase
-
crude extract is prepared, the enzyme is isolated by ammonium sulfate fractionation and high performance gel permeation liquid chromatography, using a HiLoad 16/60 Superdex 200 and a Ultropak TSK G2000SW column
-
glutathione-S-transferase-Tps1p fusion protein expressed in E. coli
-
heparin helps to retain both stability and activity of the final purified enzyme
-
trehalose-6-phosphate synthase/phosphatase complex, EC 2.4.1.15/EC 3.1.3.12
-
native enzyme 50fold by ammonium sulfate fractionation, gel filtration, and nickel-resin 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
-
recombinant enzyme from Escherichia coli
Q7WUI7, -
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Escherichia coli
A8QX04
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 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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expression of TPS1 driven by the ABI3 promoter rescues the severe embryo phenotype but not the vegetative phenotype of tps1
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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
Q94AH8
overexpression in Arabidopsis thaliana plants under control of the 35S promotor
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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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transgenic Arabidopsis plants with T6P levels increased by expression of T6P synthase or decreased by expression of T6P phosphatase in the cytosol. Compared with wild type, leaves of T6P synthase-expressing plants have increased redox activation of ADP-glucose pyrophosphorylase and increased starch
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gene otsA, DNA amnd amino acid sequence determination and analysis
C7EZF1
gene otsA, expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain B21(DE3)
-, Q1KLW0
preparation of a recombinant strain carrying multiple copies of ggsA by cotransformation
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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
-, J7G8S5
DNA and amino acid sequence determination and analysis, overexpression in transgenic flies, functional expression in HEK-293 cells
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gene dmtps1, phylgenetic analysis, expression of His-tagged TPS1 in Escherichia coli strain BL21
Q9Y119
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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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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pET-based system in BL21 cells
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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
C8XTB4, -
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-, Q5D6D9
overexpression in the Bombyx mori baculovirus expression system
B5TD29, -
expression in Pichia pastoris
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expression in Escherichia coli
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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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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
P31688, Q00764
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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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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overexpression of the enzyme incresases stress resistance of yeast cells
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gene otsA, cloned from genetic library, DNA and amino acid sequence determination and analysis, overexpression in Escherichia coli strain BL21
Q7WUI7, -
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
both low temperature and accumulation of trehalose can inhibit OtsA expression, increase of trehalose in the first 2.3 h of cold shock
C7EZF1
both low temperature and accumulation of trehalose can inhibit OtsA expression, increase of trehalose in the first 2.3 h of cold shock
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lipopolysaccharide treatment results in increase in expression, enzyme activity, and hemolymph trehalose levels
B8QRI5, -
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
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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
C8XTB4, -
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
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enzyme-deficient mutant embryos develop more slowly than the wild-type, and do not progress past the torpedo stage to cotyledon stage, overview
additional information
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transgenic plants overexpressing the intrinsic enzyme display higher dehydration resistance and a slightly increased trehalose level, but no other phenotype alterations, transgenic seedling are glucose- and abscisic-acid stress insensitive and are larger than wild-type seedlings, overview
additional information
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hemizygous TPS1/tps1 plants are transformed with an ABI3::AtTPS1 cDNA, ABI3 promoter drives expression in developing and germinating seeds but not thereafter, the ABI3::TPS1 complemented tps1 plantlets accumulate sugars and starch, transcripts associated with carbohydrate metabolism are altered and ABA-responsive transcripts are constitutively induced in ABI3::TPS1 tps1 plantlets, phenotypes, overview
additional information
-, Q1KLW0
construction of N-loop exchange mutations of the otsA gene, the mutants show altered catalytic efficiencies at temperatures from 16 to 37C compared to the wild-type enzyme, overview
additional information
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construction of N-loop exchange mutations of the otsA gene, the mutants show altered catalytic efficiencies at temperatures from 16 to 37C compared to the wild-type enzyme, overview
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additional information
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expression of TPSP in Saccharomyces cerevisiae is able to restore the growth on glucose of both Saccharomyces tps1Delta and tps1Delta tps2Delta mutants as well as the thermotolerance of the tps2Delta mutant
additional information
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overexpression of the enzyme in flies increases their tolerance to anoxia and shortens the recovery time
additional information
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construction of transgenic Oryza sativa plants expressing the catalytically active enzyme as a fusion protein with trehalose-6-phosphate phosphatase of Escherichia coli under control of the ubiquitin promotor from Zea mays, the transgenic plants produce high levels of trehalose in seeds and leaves, carbohydrate profile of seeds, but not of leaves, is altered, plants show no growth inhibition or altered phenotype
additional information
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construction of transgenic Oryza sativa plants expressing the catalytically active enzyme as a fusion protein with trehalose-6-phosphate phosphatase of Escherichia coli under control of the ubiquitin promotor from Zea mays, the transgenic plants produce high levels of trehalose in seeds and leaves, carbohydrate profile of seeds, but not of leaves, is altered, plants show no growth inhibition or altered phenotype, expression in human fibroblasts renders the cells less sensitive to drought compared to wild-type cells
H223Y
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catalytically more active than wild-type enzyme
additional information
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activity of T6P synthase and the accumulation of trehalose during ethanol fermentation are significantly improved by overexpression of TPS1, and especially at 38C cmpared to 30C, no obvious difference occurs in the activity of T6P synthase and the trehalose concentration for wild-type strain 10151, and transformed strains 10151-URA3 and 10151-pI-RED1, indicating that the expression of URA3 and YAP1 genes, markers of the expression plasmid, does not affect the synthesis of trehalose
additional information
P31688, Q00764
transgenic Solanum tunerosum plants expressing the yeast TPS1 gene show enhanced drought tolerance, 379 genes of known function in potato show at least a 2fold change in expression across genotypes, stress levels or the interaction between these factors, wild-type leaves have twice as many genes with altered expression in response to stress than TPS1 transgenic leaves, the transgenic and wildtype plants show different contents in sugar metabolites in leaves under drought conditions, four transcription factors are uniquely up-regulated in TPS1 transgenic leaves, phenotypes, overview. Microarray transcriptional and metabolic analysis of the transgenic, drought-tolerant potato line; transgenic Solanum tunerosum plants expressing the yeast TPS1 gene show enhanced drought tolerance, 379 genes of known function in potato show at least a 2fold change in expression across genotypes, stress levels or the interaction between these factors, wild-type leaves have twice as many genes with altered expression in response to stress than TPS1 transgenic leaves, the transgenic and wildtype plants show different contents in sugar metabolites in leaves under drought conditions, four transcription factors are uniquely up-regulated in TPS1 transgenic leaves, phenotypes, overview. Microarray transcriptional and metabolic analysis of the transgenic, drought-tolerant potato line
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
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trehalose-6-phosphate synthase is an intrinsic selection marker for plant transformation
drug development
-, J7G8S5
TPS is a potential insecticidal molecular target, 4-substituted 2,6-diamino-3,5-dicyano-4H-thiopyrans may serve as lead compounds for the development of insecticides with a distinct mode of action
drug development
Q9Y119
TPS is a potential insecticidal molecular target, 4-substituted 2,6-diamino-3,5-dicyano-4H-thiopyrans may serve as lead compounds in for the development of insecticides with a distinct mode of action
medicine
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the enzyme should be a valuable target for chemotherapeutic intervention in tuberculosis
agriculture
Q66Q98, -
a new strategy to increase drought tolerance and yield in legumes by overexpressing trehalose-6-phosphate synthase in the symbiotic bacterium Rhizobium etli is shown
agriculture
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the results demonstrate that engineering trehalose metabolism with a yeast TPS-TPP bifunctional enzyme confers multiple stress protection in plants, comprising a potential tool to improve stress-tolerance in crops
agriculture
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improvement of drought tolerance of potato plants