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Information on EC 2.4.1.231 - alpha,alpha-trehalose phosphorylase (configuration-retaining)
for references in articles please use BRENDA:EC2.4.1.231
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EC Tree 2 Transferases
2.4 Glycosyltransferases
2.4.1 Hexosyltransferases
2.4.1.231 alpha,alpha-trehalose phosphorylase (configuration-retaining)
IUBMB Comments
Unlike EC 2.4.1.64, α,α-trehalose phosphorylase, this enzyme retains its anomeric configuration. Vanadate is a strong competitive inhibitor of this reversible reaction.
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
showSynonyms
potpase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
ScTPase
TP2
TP3
trehalose phosphorylase
treP
TP2
-
a loop 3 variant of Lactobacillus acidophilus maltose phosphorylase
TP2
-
a loop 3 variant of Lactobacillus acidophilus maltose phosphorylase
-
TP3
-
a loop 3 variant of Lactobacillus acidophilus maltose phosphorylase
TP3
-
a loop 3 variant of Lactobacillus acidophilus maltose phosphorylase
-
trehalose phosphorylase
-
-
-
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
alpha,alpha-trehalose + phosphate = alpha-D-glucose + alpha-D-glucose 1-phosphate
mechanism
-
alpha,alpha-trehalose + phosphate = alpha-D-glucose + alpha-D-glucose 1-phosphate
mechanism
-
alpha,alpha-trehalose + phosphate = alpha-D-glucose + alpha-D-glucose 1-phosphate
-
-
-
-
alpha,alpha-trehalose + phosphate = alpha-D-glucose + alpha-D-glucose 1-phosphate
saturation transfer difference NMR spectroscopy shows that the binding of alpha,alpha-trehalose and alpha-D-glucose to ScTPase depend on additional binding of a co-substrate
-
alpha,alpha-trehalose + phosphate = alpha-D-glucose + alpha-D-glucose 1-phosphate
mechanism
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycosyl group transfer
-
-
-
-
phospho group transfer
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
MetaCyc
trehalose degradation V
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SYSTEMATIC NAME
IUBMB Comments
alpha,alpha-trehalose:phosphate alpha-D-glucosyltransferase
Unlike EC 2.4.1.64, alpha,alpha-trehalose phosphorylase, this enzyme retains its anomeric configuration. Vanadate is a strong competitive inhibitor of this reversible reaction.
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CAS REGISTRY NUMBER
COMMENTARY
37205-59-7
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-dehydro-D-glucose + alpha-D-glucose 1-phosphate
? + phosphate
-
Substrates: -
Products: -
Products: -
?
2-deoxy-D-glucose + alpha-D-glucose 1-phosphate
?
-
Substrates: 8% of the activity with alpha-D-glucose
Products: -
Products: -
r
2-deoxy-D-glucose + alpha-D-glucose 1-phosphate
? + phosphate
-
Substrates: -
Products: -
Products: -
?
2-fluoro-D-glucose + alpha-D-glucose 1-phosphate
?
-
Substrates: 15% of the activity with alpha-D-glucose
Products: -
Products: -
r
2-fluoro-D-glucose + alpha-D-glucose 1-phosphate
? + phosphate
-
Substrates: -
Products: -
Products: -
?
2-keto-D-glucose + alpha-D-glucose 1-phosphate
?
-
Substrates: 50% of the activity with alpha-D-glucose
Products: -
Products: -
r
alpha,alpha-trehalose + arsenate
alpha-D-glucose + alpha-D-glucose 1-arsenate
-
Substrates: -
Products: -
Products: -
r
D-mannose + alpha-D-glucose 1-phosphate
?
-
Substrates: 3% of the activity with alpha-D-glucose
Products: -
Products: -
r
D-mannose + alpha-D-glucose 1-phosphate
? + phosphate
-
Substrates: -
Products: -
Products: -
?
alpha,alpha-trehalose + arsenate
alpha-D-glucose 1-arsenate + alpha-D-glucose
-
Substrates: 30% of the activity with phosphate
Products: -
Products: -
?
alpha,alpha-trehalose + arsenate
alpha-D-glucose 1-arsenate + alpha-D-glucose
-
Substrates: -
Products: alpha-D-glucose 1-arsenate is unstable, therefore the net reaction gives two mol of alpha-D-glucose
Products: alpha-D-glucose 1-arsenate is unstable, therefore the net reaction gives two mol of alpha-D-glucose
r
alpha,alpha-trehalose + arsenate
alpha-D-glucose 1-arsenate + alpha-D-glucose
-
Substrates: -
Products: -
Products: -
r
alpha,alpha-trehalose + phosphate
alpha-D-glucose + alpha-D-glucose 1-phosphate
-
Substrates: -
Products: -
Products: -
r
alpha,alpha-trehalose + phosphate
alpha-D-glucose + alpha-D-glucose 1-phosphate
-
Substrates: key role in trehalose metabolism
Products: -
Products: -
r
alpha,alpha-trehalose + phosphate
alpha-D-glucose + alpha-D-glucose 1-phosphate
-
Substrates: -
Products: -
Products: -
r
alpha,alpha-trehalose + phosphate
alpha-D-glucose + alpha-D-glucose 1-phosphate
-
Substrates: key role in trehalose metabolism
Products: -
Products: -
r
alpha,alpha-trehalose + phosphate
alpha-D-glucose + alpha-D-glucose 1-phosphate
-
Substrates: -
Products: -
Products: -
?
alpha,alpha-trehalose + phosphate
alpha-D-glucose + alpha-D-glucose 1-phosphate
-
Substrates: -
Products: -
Products: -
r
alpha,alpha-trehalose + phosphate
alpha-D-glucose + alpha-D-glucose 1-phosphate
Substrates: -
Products: -
Products: -
r
alpha,alpha-trehalose + phosphate
alpha-D-glucose + alpha-D-glucose 1-phosphate
-
Substrates: -
Products: -
Products: -
r
alpha,alpha-trehalose + phosphate
alpha-D-glucose + alpha-D-glucose 1-phosphate
-
Substrates: -
Products: -
Products: -
?
alpha,alpha-trehalose + phosphate
alpha-D-glucose + alpha-D-glucose 1-phosphate
-
Substrates: -
Products: -
Products: -
?
alpha,alpha-trehalose + phosphate
alpha-D-glucose + alpha-D-glucose 1-phosphate
Substrates: -
Products: -
Products: -
r
alpha,alpha-trehalose + phosphate
alpha-D-glucose + alpha-D-glucose 1-phosphate
-
Substrates: -
Products: -
Products: -
r
alpha,alpha-trehalose + phosphate
alpha-D-glucose + alpha-D-glucose 1-phosphate
Substrates: -
Products: -
Products: -
r
alpha,alpha-trehalose + phosphate
alpha-D-glucose + alpha-D-glucose 1-phosphate
-
Substrates: -
Products: -
Products: -
?
alpha,alpha-trehalose + phosphate
alpha-D-glucose + alpha-D-glucose 1-phosphate
-
Substrates: -
Products: -
Products: -
r
alpha,alpha-trehalose + phosphate
alpha-D-glucose + alpha-D-glucose 1-phosphate
-
Substrates: -
Products: -
Products: -
?
alpha,alpha-trehalose + phosphate
alpha-D-glucose + alpha-D-glucose 1-phosphate
-
Substrates: -
Products: reverse reaction only utilizes the alpha-anomers of D-glucose-1-phosphate and D-glucose and gives exclusively the alpha,alpha-product
Products: reverse reaction only utilizes the alpha-anomers of D-glucose-1-phosphate and D-glucose and gives exclusively the alpha,alpha-product
r
alpha,alpha-trehalose + phosphate
alpha-D-glucose + alpha-D-glucose 1-phosphate
-
Substrates: -
Products: -
Products: -
r
alpha,alpha-trehalose + phosphate
alpha-D-glucose + alpha-D-glucose 1-phosphate
-
Substrates: -
Products: -
Products: -
?
alpha-D-glucose + alpha-D-glucose 1-phosphate
alpha,alpha-trehalose + phosphate
Substrates: -
Products: -
Products: -
r
alpha-D-glucose + alpha-D-glucose 1-phosphate
alpha,alpha-trehalose + phosphate
-
Substrates: beta-D-glucose 1-phosphate is not turned over by the enzyme
Products: -
Products: -
r
alpha-D-glucose + alpha-D-glucose 1-phosphate
alpha,alpha-trehalose + phosphate
Substrates: -
Products: -
Products: -
r
alpha-D-glucose + alpha-D-glucose 1-phosphate
alpha,alpha-trehalose + phosphate
Substrates: ratio of phosphorolysis to hydrolysis is 46000
Products: -
Products: -
r
alpha-D-glucose + alpha-D-glucose 1-phosphate
alpha,alpha-trehalose + phosphate
Substrates: ratio of phosphorolysis to hydrolysis is 46000
Products: -
Products: -
r
alpha-D-glucose 1-fluoride + phosphate
alpha-D-glucose 1-phosphate + fluoride
-
Substrates: -
Products: -
Products: -
?
alpha-D-glucose 1-fluoride + phosphate
alpha-D-glucose 1-phosphate + fluoride
-
Substrates: poor substrate, alpha-D-glucose 1-fluoride is recognized as a substrate analogue of alpha,alpha-trehalose but not of alpha-D-glucose 1-phosphate
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in trehalose catabolism
Products: -
Products: -
?
additional information
?
-
-
Substrates: the maltose phosphorylase loop 3 variants TP2 and TP3 are capable of phosphorolysing trehalose (alpha, alpha1) as well as maltose (alpha-1,4),but show no activity towards kojibiose (alpha-1,2), nigerose (alpha-1,3) or isomaltose (alpha-1,6). The catalytic efficiency of TP3 towards trehalose is 19fold higher than of TP2
Products: -
Products: -
?
additional information
?
-
-
Substrates: the maltose phosphorylase loop 3 variants TP2 and TP3 are capable of phosphorolysing trehalose (alpha, alpha1) as well as maltose (alpha-1,4),but show no activity towards kojibiose (alpha-1,2), nigerose (alpha-1,3) or isomaltose (alpha-1,6). The catalytic efficiency of TP3 towards trehalose is 19fold higher than of TP2
Products: -
Products: -
?
additional information
?
-
-
Substrates: no measurable activity is found with D-arabinose, D-fructose, D-fucose, D-galactose, D-lyxose, D-mannoheptaose, D-ribose and D-xylose
Products: -
Products: -
?
additional information
?
-
Substrates: during heat stress, trehalose phosphorylase shows reversible activity
Products: -
Products: -
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
Substrates: the enzyme is involved in trehalose catabolism
Products: -
Products: -
?
alpha,alpha-trehalose + phosphate
alpha-D-glucose + alpha-D-glucose 1-phosphate
-
Substrates: key role in trehalose metabolism
Products: -
Products: -
r
alpha,alpha-trehalose + phosphate
alpha-D-glucose + alpha-D-glucose 1-phosphate
-
Substrates: key role in trehalose metabolism
Products: -
Products: -
r
alpha,alpha-trehalose + phosphate
alpha-D-glucose + alpha-D-glucose 1-phosphate
-
Substrates: -
Products: -
Products: -
?
alpha,alpha-trehalose + phosphate
alpha-D-glucose + alpha-D-glucose 1-phosphate
-
Substrates: -
Products: -
Products: -
r
alpha,alpha-trehalose + phosphate
alpha-D-glucose + alpha-D-glucose 1-phosphate
-
Substrates: -
Products: -
Products: -
r
alpha,alpha-trehalose + phosphate
alpha-D-glucose + alpha-D-glucose 1-phosphate
Substrates: -
Products: -
Products: -
r
alpha,alpha-trehalose + phosphate
alpha-D-glucose + alpha-D-glucose 1-phosphate
-
Substrates: -
Products: -
Products: -
r
alpha,alpha-trehalose + phosphate
alpha-D-glucose + alpha-D-glucose 1-phosphate
-
Substrates: -
Products: -
Products: -
?
alpha,alpha-trehalose + phosphate
alpha-D-glucose + alpha-D-glucose 1-phosphate
-
Substrates: -
Products: -
Products: -
r
alpha,alpha-trehalose + phosphate
alpha-D-glucose + alpha-D-glucose 1-phosphate
-
Substrates: -
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-deoxy-2-fluoro-alpha-D-glucose 1-fluoride
-
inhibits reaction with alpha,alpha-trehalose
alpha-D-glucose 1-fluoride
-
competitive with respect to alpha,alpha-trehalose in the phosphorolysis direction
nitrogen
-
low nitrogen positively regulates the enzyme activity of TreP in the synthesis of trehalose and inhibits the enzyme activity of phosphorylase
orthovanadate
-
competitive against phosphate and alpha-D-glucopyranosyl phosphate, inhibits forward and reverse reaction
phosphate
-
phosphate 50 mM causes total supression in wild-type but enhances mutant K512 activity
vanadate
-
phosphate mimic, inhibits phosphorolysis of alpha-D-glucose 1-fluoride by forming a ternary complex
vanadate
-
strong inhibitor for wildtype ScTPase and weak inhibitor for mutant K512A but no mutant R507A is not inhibited at all
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
guanidine
-
no effect on wild-type but guanidine causes a 45fold enhancement of mutant R507A activity
nitrogen
-
low nitrogen positively regulates the enzyme activity of TreP in the synthesis of trehalose and inhibits the enzyme activity of phosphorylase
propargylamine
-
no effect on wild-type but propagylamine causes a 23fold enhancement of mutant K512A activity
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
mutant K512A (phosphate): no saturation, Kcat/Km (phosphate): 0.0014/Msec
-
22
alpha,alpha-trehalose
-
loop 3 variant TP3, in 40 mM phosphate-citrate pH 6.2 at 45°C
53
alpha,alpha-trehalose
-
loop 3 variant TP2, in 40 mM phosphate-citrate pH 6.2 at 45°C
2.2
alpha-D-glucose 1-phosphate
30°C, pH 6.6, recombinant enzyme
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.33
alpha,alpha-trehalose
-
loop 3 variant TP2, in 40 mM phosphate-citrate pH 6.2 at 45°C
2.7
alpha,alpha-trehalose
-
loop 3 variant TP3, in 40 mM phosphate-citrate pH 6.2 at 45°C
14.1
alpha-D-glucose 1-phosphate
30°C, pH 6.6, recombinant enzyme
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0062
alpha,alpha-trehalose
-
loop 3 variant TP2, in 40 mM phosphate-citrate pH 6.2 at 45°C
0.12
alpha,alpha-trehalose
-
loop 3 variant TP3, in 40 mM phosphate-citrate pH 6.2 at 45°C
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
5.9
alpha-D-glucose 1-phosphate
30°C, pH 6.6, recombinant enzyme
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6.2
6.6
6.8
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5 - 6.8
-
pH 5.5: about 80% of maximal activity, pH 75% of maximal activity, synthesis of alpha,alpha-trehalose
5.5 - 7.8
-
pH 5.5: about 75% of maximal activity, pH 7.8: about 80% of maxuimal activity, phosphorolysis
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
bifunctional trehalose synthase/trehalose phosphorylase
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
Highest Expressing Human Cell Lines
Cell Line LinksPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
physiological function
additional information
trehalose phosphorylase is a potential allergen, identified by IgE immunoblotting and mass spectrometry
malfunction
-
knockdown of transcription factor general control nonderepressible 4 (GCN4) and trehalose phosphorylase leads to growth inhibition of Ganoderma lucidum mycelia
malfunction
Ganoderma lucidum ACCC53264
-
knockdown of transcription factor general control nonderepressible 4 (GCN4) and trehalose phosphorylase leads to growth inhibition of Ganoderma lucidum mycelia
-
physiological function
heat shock can induce a stress response in the mycelia through the regulation of genes related to trehalose metabolism and the subsequent promotion and control of the transcription and translation of enzymes. The degradation of trehalose is stronger than its synthesis under heat stress
physiological function
-
the intracellular trehalose content in low temperature tolerant strain VH3 is higher than that in low temperature sensitive V23 under low temperature stress. In the first 2 h of low temperature stress, the expression of trehalose-6-phosphate phosphatase gene decreases, while the expression of trehalose phosphorylase gene increases. The expression levels of trehalose-6-phosphate phosphatase and trehalose phosphatase genes in VH3 is significantly higher than that in V23 from 6 h to 8 h of low temperature stress
physiological function
intracellular trehalose significantly accumulates in the mycelia in response to 37 °C heat shock. For the trehalose phosphorylase, the degradation of trehalose is stronger than its synthesis under heat stress
physiological function
heat stress inhibits the growth of both heat-sensitive and less-sensitive strains, the inhibition is more significant for the sensitive strain. Heat stress leads to the increase of lipid peroxidation and intracellular trehalose accumulation, with a higher level in the heat-sensitive strain, and this effect is independent of exogenous trehalose application. Trehalose plays protective roles on heat resistance of the two strains and the protective effects are more remarkable in the sensitive strain. The trehalose metabolic enzymes in the sensitive strain act more positively to accumulate trehalose than those in the less-sensitive strain
physiological function
-
the transcription factor general control nonderepressible 4 (GCN4)/trehalose phosphorylase module promotes trehalose accumulation in response to abiotic stresses to improve the stress tolerance of Ganoderma lucidum
physiological function
Ganoderma lucidum ACCC53264
-
the transcription factor general control nonderepressible 4 (GCN4)/trehalose phosphorylase module promotes trehalose accumulation in response to abiotic stresses to improve the stress tolerance of Ganoderma lucidum
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). TREPH_PLEPU
739
0
82028
Swiss-Prot
other Location (Reliability: 2)
TREPH_PLESA
751
0
83653
Swiss-Prot
Secretory Pathway (Reliability: 1)
A0A067P9S7_PLEO1
Pleurotus ostreatus (strain PC15)
737
0
81814
TrEMBL
-
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
120000
60000
61000
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
tetramer
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D379N
ratio of phosphorolysis to hydrolysis decreases by a factor of 287500
H403A
ratio of phosphorolysis to hydrolysis decreases by a factor of 2190
K512A
R507A
D379N
-
ratio of phosphorolysis to hydrolysis decreases by a factor of 287500
-
H403A
-
ratio of phosphorolysis to hydrolysis decreases by a factor of 2190
-
K512A
-
ratio of phosphorolysis to hydrolysis decreases by a factor of 511111
-
R507A
-
ratio of phosphorolysis to hydrolysis decreases by a factor of 575000
-
K512A
ratio of phosphorolysis to hydrolysis decreases by a factor of 511111
K512A
-
kcat/Km (phosphate): 0.0014/Msec, vanadate shows a weaker inhibitory effect compared to wild-type, propargylamine leads to a 23fold increase in activity, phosphate 50 mM enhances basal hydrolase activity
R507A
ratio of phosphorolysis to hydrolysis decreases by a factor of 575000
R507A
-
Km (phosphate) 103 mM, kcat/Km (phosphate): 0.0004/Msec, vanadate shows no inhibitory effect, guanidine leads to a 45fold increase in activity
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20
-
unstable, loses activity within a few hours, glycerol, PEG 4000 or trehalose stabilize
30
4
-
unstable, loses activity within a few hours, glycerol, PEG 4000 or trehalose stabilize
40
additional information
-
PoTPase has a half life of approximately 1 h at 30°C
30
-
half-life: approximately 1 h in absence of stabilizing compound, 11.5 h in presence of 300 mM alpha,alpha-trehalose, 6.5 h in presence of 20% w/v glycerol, 70 h in presence of 26% w/v polyethylenglycol. Covalent modification of PoTPase with activated derivatives of PEG 5000 increases the stability by up to 600fold
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
highly unstable during purification, glycerol, phosphate, dithiothreitol and PMSF stabilize
-
unstable protein, half-life of no more than approximately 1.3 h in 20mM MES buffer, 25°C, pH 7.0. The enzyme can be stabilized on addition of alpha,alpha-trehalose (300 mM) which yields a half-life of 11.5 h. In the presence of 20% (w/v) glycerol, and 9 and 26% (w/v) PEG-4000, half-life is 6.5 h, 16 h and 70 h, respectively. Large improvements in stability by covalent protein modification with activated derivatives of PEG-5000
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
trehalose phosphorylase from the basidiomycete Pleurotus ostreatus (PoTPase) is isolated from fungal fruit bodies through 500-fold purification with a yield of 44%
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
the transcription factor, general control nonderepressible 4 (GCN4) directly binds and activates the expression of trehalose synthase (TreP). Low nitrogen condition increases the interaction between GCN4 and TreP promoter, thereby improving the gene expression and protein accumulation of TreP
the transcription factor, general control nonderepressible 4 (GCN4) directly binds and activates the expression of trehalose synthase (TreP). Low nitrogen condition increases the interaction between GCN4 and TreP promoter, thereby improving the gene expression and protein accumulation of TreP
-
the transcription factor, general control nonderepressible 4 (GCN4) directly binds and activates the expression of trehalose synthase (TreP). Low nitrogen condition increases the interaction between GCN4 and TreP promoter, thereby improving the gene expression and protein accumulation of TreP
Ganoderma lucidum ACCC53264
-
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
-
sucrose is converted to alpha,alpha-trehalose in about 60% yield using a coupled enzyme system composed of sucrose phosphorylase from Leuconostoc mesenteroides, glucose isomerase from Streptomyces murinus and the appropriately stabilized PoTPase
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Eis, C.; Albert, M.; Dax, K.; Nidetzky, B.
The stereochemical course of the reaction mechanism of trehalose phosphorylase from Schizophyllum commune
FEBS Lett.
440
440-443
1998
Schizophyllum commune
brenda
Eis, C.; Nidetzky, B.
Characterization of trehalose phosphorylase from Schizophyllum commune
Biochem. J.
341
385-393
1999
Schizophyllum commune
brenda
Eis, C.; Nidetzky, B.
Substrate-binding recognition and specificity of trehalose phosphorylase from Schizophyllum commune examined in steady-state kinetic studies with deoxy and deoxyfluoro substrate analogues and inhibitors
Biochem. J.
363
335-340
2002
Schizophyllum commune
brenda
Eis, C.; Watkins, M.; Prohaska, T.; Nidetzky, B.
Fungal trehalose phosphorylase: kinetic mechanism, pH-dependence of the reaction and some structural properties of the enzyme from Schizophyllum commune
Biochem. J.
356
757-767
2001
Schizophyllum commune
brenda
Han, S.E.; Kwon, H.B.; Lee, S.B.; Yi, B.Y.; Murayama, I.; Kitamoto, Y.; Byun, M.O.
Cloning and characterization of a gene encoding trehalose phosphorylase (TP) from Pleurotus sajor-caju
Protein Expr. Purif.
30
194-202
2003
Lentinus sajor-caju (Q9UV63)
brenda
Kitamoto, Y.; Akashi, H.; Tanaka, H.; Mori, N.
alpha-Glucose-1-phosphate formation by a novel trehalose phosphorylase from Flammulina velutipes
FEMS Microbiol. Lett.
55
147-149
1988
Flammulina velutipes
-
brenda
Kitamoto, Y.; Osaki, N.; Tanaka, H.; Sasaki, H.; Mori, N.
Purification and properties of alpha-glucose 1-phosphate-forming trehalose phosphorylase from a basidiomycete, Pleurotus ostreatus
Mycoscience
41
607-613
2000
Pleurotus ostreatus
-
brenda
Kitamoto, Y.; Tanaka, H.; Osaki, N.
Survey of alpha-glucose 1-phosphate forming trehalose phosphorylase and trehalase in various fungi including basidiomycetous mushrooms
Mycoscience
39
327-331
1998
Agaricus sp., Polyporales
-
brenda
Nidetzky, B.; Eis, C.
alpha-Retaining glucosyl transfer catalysed by trehalose phosphorylase from Schizophyllum commune: mechanistic evidence obtained from steady-state kinetic studies with substrate analogues and inhibitors
Biochem. J.
360
727-736
2001
Schizophyllum commune
brenda
Saito, K.; Kase, T.; Takahashi, E.; Horinouchi, S.
Purification and characterization of a trehalose synthase from the basidiomycete Grifola frondosa
Appl. Environ. Microbiol.
64
4340-4345
1998
Grifola frondosa
brenda
Wannet, W.J.; Op den Camp, H.J.; Wisselink, H.W.; van der Drift, C.; Van Griensven, L.J.; Vogels, G.D.
Purification and characterization of trehalose phosphorylase from the commercial mushroom Agaricus bisporus
Biochim. Biophys. Acta
1425
177-188
1998
Agaricus bisporus, Agaricus bisporus Horst U1
brenda
Dmitryjuk, M.; Zoltowska, K.
Trehalose catabolism enzymes in tissues of Ascaris suum (Nematoda)
Helminthologia
41
63-66
2004
Ascaris suum
-
brenda
Goedl, C.; Griessler, R.; Schwarz, A.; Nidetzky, B.
Structure-function relationships for Schizophyllum commune trehalose phosphorylase and their implications for the catalytic mechanism of family GT-4 glycosyltransferases
Biochem. J.
397
491-500
2006
Schizophyllum commune (Q2HZZ3), Schizophyllum commune BT 2115 (Q2HZZ3)
brenda
Schwarz, A.; Goedl, C.; Minani, A.; Nidetzky, B.
Trehalose phosphorylase from Pleurotus ostreatus: characterization and stabilization by covalent modification, and application for the synthesis of alpha,alpha-trehalose
J. Biotechnol.
129
140-150
2007
Pleurotus ostreatus
brenda
Brecker, L.; Schwarz, A.; Goedl, C.; Kratzer, R.; Tyl, C.E.; Nidetzky, B.
Studying non-covalent enzyme carbohydrate interactions by STD NMR
Carbohydr. Res.
343
2153-2161
2008
Schizophyllum commune
brenda
Goedl, C.; Nidetzky, B.
The phosphate site of trehalose phosphorylase from Schizophyllum commune probed by site-directed mutagenesis and chemical rescue studies
FEBS J.
275
903-913
2008
Schizophyllum commune
brenda
Nakai, H.; Petersen, B.O.; Westphal, Y.; Dilokpimol, A.; Abou Hachem, M.; Duus, J.?.; Schols, H.A.; Svensson, B.
Rational engineering of Lactobacillus acidophilus NCFM maltose phosphorylase into either trehalose or kojibiose dual specificity phosphorylase
Protein Eng. Des. Sel.
23
781-787
2010
Lactobacillus acidophilus, Lactobacillus acidophilus NCFM
brenda
Liu, X.; Wu, X.; Gao, W.; Qu, J.; Chen, Q.; Huang, C.; Zhang, J.
Protective roles of trehalose in Pleurotus pulmonarius during heat stress response
J. Integr. Agric.
18
428-437
2019
Pleurotus pulmonarius (A6YRN9)
-
brenda
Liu, J.H.; Shang, X.D.; Liu, J.Y.; Tan, Q.
Changes in trehalose content, enzyme activity and gene expression related to trehalose metabolism in Flammulina velutipes under heat shock
Microbiology
162
1274-1285
2016
Flammulina velutipes (A0A0G2SWS6)
brenda
Zhao, X.; Song, X.; Li, Y.; Yu, C.; Zhao, Y.; Gong, M.; Shen, X.; Chen, M.
Gene expression related to trehalose metabolism and its effect on Volvariella volvacea under low temperature stress
Sci. Rep.
8
11011
2018
Volvariella volvacea
brenda
Shi, L.; Lian, L.; Wang, L.; Zhang, S.; Han, Q.; Shi, L.; Chen, H.; Zhao, M.
General control nonderepressible 4 activates the transcription of trehalose phosphorylase to improve trehalose production and abiotic stress tolerance in Ganoderma lucidum
Int. J. Biol. Macromol.
311
143840
2025
Ganoderma lucidum, Ganoderma lucidum ACCC53264
brenda
Rangkakulnuwat, P.; Aluksanasuwan, S.; Somsuan, K.; Chiangjong, W.; Walker, A.; Thongklang, N.; Lao-Araya, M.
Trehalose phosphorylase as a novel potential allergen in a case of allergic reaction due to oyster mushroom (Pleurotus ostreatus) ingestion
J. Allergy Clin. Immunol. Glob.
2
100095
2023
Pleurotus pulmonarius (A6YRN9)
brenda
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