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Information on EC 3.2.1.93 - alpha,alpha-phosphotrehalase for references in articles please use BRENDA:EC3.2.1.93
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EC Tree
The enzyme appears in viruses and cellular organisms
Synonyms
Alpha,alpha-phosphotrehalase, BlTreA, phosphotrehalase, TreA, trehalose-6-phosphate hydrolase,
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Alpha,alpha-phosphotrehalase
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trehalose-6-phosphate hydrolase
BlTreA
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TreA
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trehalose-6-phosphate hydrolase
A0A447SCD5
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trehalose-6-phosphate hydrolase
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trehalose-6-phosphate hydrolase
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trehalose-6-phosphate hydrolase
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alpha,alpha-trehalose 6-phosphate + H2O = D-glucose + D-glucose 6-phosphate
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hydrolysis of O-glycosyl bond
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alpha,alpha-trehalose-6-phosphate phosphoglucohydrolase
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4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
4-nitrophenyl alpha-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
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alpha,alpha-trehalose 6-phosphate + H2O
alpha-D-glucose + alpha-D-glucose 6-phosphate
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alpha,alpha-trehalose 6-phosphate + H2O
D-glucose + D-glucose 6-phosphate
additional information
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regulatory function on sugar influx
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4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
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4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
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alpha,alpha-trehalose 6-phosphate + H2O
D-glucose + D-glucose 6-phosphate
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alpha,alpha-trehalose 6-phosphate + H2O
D-glucose + D-glucose 6-phosphate
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alpha,alpha-trehalose 6-phosphate + H2O
D-glucose + D-glucose 6-phosphate
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alpha,alpha-trehalose 6-phosphate + H2O
D-glucose + D-glucose 6-phosphate
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alpha,alpha-trehalose 6-phosphate + H2O
D-glucose + D-glucose 6-phosphate
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alpha,alpha-trehalose 6-phosphate + H2O
D-glucose + D-glucose 6-phosphate
additional information
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regulatory function on sugar influx
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alpha,alpha-trehalose 6-phosphate + H2O
D-glucose + D-glucose 6-phosphate
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alpha,alpha-trehalose 6-phosphate + H2O
D-glucose + D-glucose 6-phosphate
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alpha,alpha-trehalose 6-phosphate + H2O
D-glucose + D-glucose 6-phosphate
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NaCl
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6fold stimulation at 1 mM with 4-nitrophenyl alpha-glucopyranoside as substrate, no stimulation with alpha-trehalose 6-phosphate
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5.8 - 13.6
4-nitrophenyl alpha-D-glucopyranoside
1.8 - 5.9
alpha,alpha-trehalose 6-phosphate
5.8
4-nitrophenyl alpha-D-glucopyranoside
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pH 8.0, 30°C, wild-type enzyme
7.4
4-nitrophenyl alpha-D-glucopyranoside
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pH 8.0, 30°C, mutant enzyme K284A
11.4
4-nitrophenyl alpha-D-glucopyranoside
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pH 8.0, 30°C, mutant enzyme H282A
12.2
4-nitrophenyl alpha-D-glucopyranoside
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pH 8.0, 30°C, mutant enzyme H281A
13.6
4-nitrophenyl alpha-D-glucopyranoside
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pH 8.0, 30°C, mutant enzyme K292A
1.8
alpha,alpha-trehalose 6-phosphate
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2.5
alpha,alpha-trehalose 6-phosphate
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pH 8.0, 30°C, wild-type enzyme
3.2
alpha,alpha-trehalose 6-phosphate
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pH 8.0, 30°C, mutant enzyme K284A
4.9
alpha,alpha-trehalose 6-phosphate
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pH 8.0, 30°C, mutant enzyme H282A
5.3
alpha,alpha-trehalose 6-phosphate
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pH 8.0, 30°C, mutant enzyme H281A
5.9
alpha,alpha-trehalose 6-phosphate
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pH 8.0, 30°C, mutant enzyme K292A
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0.3 - 30.3
4-nitrophenyl alpha-D-glucopyranoside
0.4 - 46.7
alpha,alpha-trehalose 6-phosphate
0.3
4-nitrophenyl alpha-D-glucopyranoside
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pH 8.0, 30°C, mutant enzyme K292A
12.4
4-nitrophenyl alpha-D-glucopyranoside
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pH 8.0, 30°C, mutant enzyme H281A
22.6
4-nitrophenyl alpha-D-glucopyranoside
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pH 8.0, 30°C, mutant enzyme H282A
25.6
4-nitrophenyl alpha-D-glucopyranoside
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pH 8.0, 30°C, mutant enzyme K284A
30.3
4-nitrophenyl alpha-D-glucopyranoside
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pH 8.0, 30°C, wild-type enzyme
0.4
alpha,alpha-trehalose 6-phosphate
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pH 8.0, 30°C, mutant enzyme K292A
19.1
alpha,alpha-trehalose 6-phosphate
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pH 8.0, 30°C, mutant enzyme H281A
34.8
alpha,alpha-trehalose 6-phosphate
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pH 8.0, 30°C, mutant enzyme H282A
39.5
alpha,alpha-trehalose 6-phosphate
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pH 8.0, 30°C, mutant enzyme K284A
46.7
alpha,alpha-trehalose 6-phosphate
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pH 8.0, 30°C, wild-type enzyme
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0.02 - 5.3
4-nitrophenyl alpha-D-glucopyranoside
0.1 - 18.9
alpha,alpha-trehalose 6-phosphate
0.02
4-nitrophenyl alpha-D-glucopyranoside
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pH 8.0, 30°C, mutant enzyme K292A
1
4-nitrophenyl alpha-D-glucopyranoside
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pH 8.0, 30°C, mutant enzyme H281A
2
4-nitrophenyl alpha-D-glucopyranoside
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pH 8.0, 30°C, mutant enzyme H282A
3.5
4-nitrophenyl alpha-D-glucopyranoside
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pH 8.0, 30°C, mutant enzyme K284A
5.3
4-nitrophenyl alpha-D-glucopyranoside
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pH 8.0, 30°C, wild-type enzyme
0.1
alpha,alpha-trehalose 6-phosphate
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pH 8.0, 30°C, mutant enzyme K292A
3.6
alpha,alpha-trehalose 6-phosphate
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pH 8.0, 30°C, mutant enzyme H281A
7.2
alpha,alpha-trehalose 6-phosphate
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pH 8.0, 30°C, mutant enzyme H282A
12.2
alpha,alpha-trehalose 6-phosphate
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pH 8.0, 30°C, mutant enzyme K284A
18.9
alpha,alpha-trehalose 6-phosphate
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pH 8.0, 30°C, wild-type enzyme
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30
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assay at
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UniProt
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UniProt
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168
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in symbiosis Glycine max
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UniProt
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A0A447SCD5
UniProt
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168
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bacteroids
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Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / NBRC 12200 / NCIMB 9375 / NRRL NRS-1264 / Gibson 46)
Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / NBRC 12200 / NCIMB 9375 / NRRL NRS-1264 / Gibson 46)
Bacillus licheniformis (strain ATCC 14580 / DSM 13 / JCM 2505 / NBRC 12200 / NCIMB 9375 / NRRL NRS-1264 / Gibson 46)
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crystal structures of Bacillus licheniformis TreA and its R201Q mutant complexed with 4-nitrophenyl-alpha-D-glucopyranoside are presented at 2.0 and 2.05 A resolution, respectively
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D203E
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no detectable activity with alpha,alpha-trehalose 6-phosphate or 4-nitrophenyl alpha-D-glucopyranoside
D329E
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no detectable activity with alpha,alpha-trehalose 6-phosphate or 4-nitrophenyl alpha-D-glucopyranoside
E254D
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no detectable activity with alpha,alpha-trehalose 6-phosphate or 4-nitrophenyl alpha-D-glucopyranoside
H281A
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kcat/Km for 4-nitrophenyl alpha-D-glucopyranoside is reduced 5.3fold as compared to wild-type value, kcat/Km for alpha,alpha-trehalose 6-phosphate is reduced 5.25fold as compared to wild-type value
H282A
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kcat/Km for 4-nitrophenyl alpha-D-glucopyranoside is reduced 2.65fold as compared to wild-type value, kcat/Km for alpha,alpha-trehalose 6-phosphate is reduced 2.6fold as compared to wild-type value
K284A
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kcat/Km for 4-nitrophenyl alpha-D-glucopyranoside is reduced 1.5fold as compared to wild-type value, kcat/Km for alpha,alpha-trehalose 6-phosphate is reduced 1.5fold as compared to wild-type value
K292A
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kcat/Km for 4-nitrophenyl alpha-D-glucopyranoside is reduced 265fold as compared to wild-type value, kcat/Km for alpha,alpha-trehalose 6-phosphate is reduced 189fold as compared to wild-type value
D203E
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no detectable activity with alpha,alpha-trehalose 6-phosphate or 4-nitrophenyl alpha-D-glucopyranoside
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E254D
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no detectable activity with alpha,alpha-trehalose 6-phosphate or 4-nitrophenyl alpha-D-glucopyranoside
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H281A
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kcat/Km for 4-nitrophenyl alpha-D-glucopyranoside is reduced 5.3fold as compared to wild-type value, kcat/Km for alpha,alpha-trehalose 6-phosphate is reduced 5.25fold as compared to wild-type value
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K284A
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kcat/Km for 4-nitrophenyl alpha-D-glucopyranoside is reduced 1.5fold as compared to wild-type value, kcat/Km for alpha,alpha-trehalose 6-phosphate is reduced 1.5fold as compared to wild-type value
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K292A
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kcat/Km for 4-nitrophenyl alpha-D-glucopyranoside is reduced 265fold as compared to wild-type value, kcat/Km for alpha,alpha-trehalose 6-phosphate is reduced 189fold as compared to wild-type value
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additional information
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enzyme gene disruption mutant, unable to grow on trehalose, while trehalose uptake remains unaffected. Cryoprotective effect of trehalose is reduced
additional information
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enzyme gene disruption mutant, unable to grow on trehalose, while trehalose uptake remains unaffected. Cryoprotective effect of trehalose is reduced
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overexpressed in Escherichia coli
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expressed in Saccharomyces cerevisiae
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expression in Escherichia coli M15 cells
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sorbitol, sucrose, and trehalose at a concentration of 0.75 M improve the refolding yields of guanidine hydrochloride-denatured BlTreA, probably due to the fact that these sugars favor the formation of tertiary architectures. Sorbitol is more effective than any of the other two sugars; sorbitol, sucrose, and trehalose at a concentration of 0.75 M improve the refolding yields of guanidine hydrochloride-denatured enzyme. Far-UV CD measurements demonstrate the ability of sugar osmolytes to shift the secondary structure of guanidine hydrochloride-denatured enzyme towards near-native conformations. ANS fluorescence intensity measurements reveal a reduction of exposed hydrophobic surfaces upon the treatment of denatured enzyme with sugar osmolytes
A0A447SCD5
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Salminen, S.O.; Streeter, J.G.
Enzymes of alpha,alpha-trehalose metabolism in soybean nodules
Plant Physiol.
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538-541
1986
Bradyrhizobium japonicum
brenda
Bhumiratana, A.; Anderson, R.L.; Costilow, R.N.
Trehalose metabolism by Bacillus popillae
J. Bacteriol.
119
484-493
1974
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Helfert, C.; Gotsche, S.; Dahl, M.K.
Cleavage of trehalose-phosphate in Bacillus subtilis is catalysed by a phospho-alpha(1,1)-glucosidase encoded by the treA gene
Mol. Microbiol.
16
111-120
1995
Bacillus subtilis
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Gotsche, S.; Dahl, M.K.
Purification and characterization of the phospho-alpha(1,1)glucosidase (TreA) of Bacillus subtilis 168
J. Bacteriol.
177
2721-2726
1995
Bacillus subtilis 168, Bacillus subtilis
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van Vaeck, C.; Wera, S.; van Dijck, P.; Thevelein, J.M.
Analysis and modification of trehalose 6-phosphate levels in the yeast Saccharomyces cerevisiae with the use of Bacillus subtilis phosphotrehalase
Biochem. J.
353
157-162
2001
Bacillus subtilis
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Duong, T.; Barrangou, R.; Russell, W.M.; Klaenhammer, T.R.
Characterization of the tre locus and analysis of trehalose cryoprotection in Lactobacillus acidophilus NCFM
Appl. Environ. Microbiol.
72
1218-1225
2006
Lactobacillus acidophilus, Lactobacillus acidophilus NCFM
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Lin, M.G.; Chi, M.C.; Naveen, V.; Li, Y.C.; Lin, L.L.; Hsiao, C.D.
Bacillus licheniformis trehalose-6-phosphate hydrolase structures suggest keys to substrate specificity
Acta Crystallogr. Sect. D
72
59-70
2016
Bacillus licheniformis, Bacillus licheniformis (Q65MI2), Bacillus licheniformis DSM13 (Q65MI2)
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Chen, J.H.; Chi, M.C.; Lin, M.G.; Lin, L.L.; Wang, T.F.
Beneficial effect of sugar osmolytes on the refolding of guanidine hydrochloride-denatured trehalose-6-phosphate hydrolase from Bacillus licheniformis
BioMed Res. Int.
2015
806847
2015
Bacillus licheniformis 168 (Q65MI2), Bacillus licheniformis (A0A447SCD5), Bacillus licheniformis, Bacillus licheniformis (Q65MI2)
brenda
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3.2.1.93 alpha,alpha-phosphotrehalase
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