We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Information on EC 3.2.1.93 - alpha,alpha-phosphotrehalase for references in articles please use BRENDA:EC3.2.1.93
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
The enzyme appears in viruses and cellular organisms
Synonyms
Alpha,alpha-phosphotrehalase, BlTreA, phosphotrehalase, TreA, trehalose-6-phosphate hydrolase,
more
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Alpha,alpha-phosphotrehalase
-
-
-
-
trehalose-6-phosphate hydrolase
BlTreA
-
TreA
-
trehalose-6-phosphate hydrolase
A0A447SCD5
-
trehalose-6-phosphate hydrolase
-
trehalose-6-phosphate hydrolase
-
-
trehalose-6-phosphate hydrolase
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
alpha,alpha-trehalose 6-phosphate + H2O = D-glucose + D-glucose 6-phosphate
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
hydrolysis of O-glycosyl bond
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
alpha,alpha-trehalose-6-phosphate phosphoglucohydrolase
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
4-nitrophenyl alpha-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
-
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha-D-glucose + alpha-D-glucose 6-phosphate
-
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
D-glucose + D-glucose 6-phosphate
additional information
?
-
-
regulatory function on sugar influx
-
-
-
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
D-glucose + D-glucose 6-phosphate
-
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
D-glucose + D-glucose 6-phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
D-glucose + D-glucose 6-phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
D-glucose + D-glucose 6-phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
D-glucose + D-glucose 6-phosphate
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
alpha,alpha-trehalose 6-phosphate + H2O
D-glucose + D-glucose 6-phosphate
additional information
?
-
-
regulatory function on sugar influx
-
-
-
alpha,alpha-trehalose 6-phosphate + H2O
D-glucose + D-glucose 6-phosphate
-
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
D-glucose + D-glucose 6-phosphate
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
D-glucose + D-glucose 6-phosphate
-
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NaCl
-
6fold stimulation at 1 mM with 4-nitrophenyl alpha-glucopyranoside as substrate, no stimulation with alpha-trehalose 6-phosphate
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
pH 8.0, 30°C, wild-type enzyme
7.4
4-nitrophenyl alpha-D-glucopyranoside
-
pH 8.0, 30°C, mutant enzyme K284A
11.4
4-nitrophenyl alpha-D-glucopyranoside
-
pH 8.0, 30°C, mutant enzyme H282A
12.2
4-nitrophenyl alpha-D-glucopyranoside
-
pH 8.0, 30°C, mutant enzyme H281A
13.6
4-nitrophenyl alpha-D-glucopyranoside
-
pH 8.0, 30°C, mutant enzyme K292A
1.8
alpha,alpha-trehalose 6-phosphate
-
-
-
2.5
alpha,alpha-trehalose 6-phosphate
-
pH 8.0, 30°C, wild-type enzyme
3.2
alpha,alpha-trehalose 6-phosphate
-
pH 8.0, 30°C, mutant enzyme K284A
4.9
alpha,alpha-trehalose 6-phosphate
-
pH 8.0, 30°C, mutant enzyme H282A
5.3
alpha,alpha-trehalose 6-phosphate
-
pH 8.0, 30°C, mutant enzyme H281A
5.9
alpha,alpha-trehalose 6-phosphate
-
pH 8.0, 30°C, mutant enzyme K292A
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
pH 8.0, 30°C, mutant enzyme K292A
12.4
4-nitrophenyl alpha-D-glucopyranoside
-
pH 8.0, 30°C, mutant enzyme H281A
22.6
4-nitrophenyl alpha-D-glucopyranoside
-
pH 8.0, 30°C, mutant enzyme H282A
25.6
4-nitrophenyl alpha-D-glucopyranoside
-
pH 8.0, 30°C, mutant enzyme K284A
30.3
4-nitrophenyl alpha-D-glucopyranoside
-
pH 8.0, 30°C, wild-type enzyme
0.4
alpha,alpha-trehalose 6-phosphate
-
pH 8.0, 30°C, mutant enzyme K292A
19.1
alpha,alpha-trehalose 6-phosphate
-
pH 8.0, 30°C, mutant enzyme H281A
34.8
alpha,alpha-trehalose 6-phosphate
-
pH 8.0, 30°C, mutant enzyme H282A
39.5
alpha,alpha-trehalose 6-phosphate
-
pH 8.0, 30°C, mutant enzyme K284A
46.7
alpha,alpha-trehalose 6-phosphate
-
pH 8.0, 30°C, wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
pH 8.0, 30°C, mutant enzyme K292A
1
4-nitrophenyl alpha-D-glucopyranoside
-
pH 8.0, 30°C, mutant enzyme H281A
2
4-nitrophenyl alpha-D-glucopyranoside
-
pH 8.0, 30°C, mutant enzyme H282A
3.5
4-nitrophenyl alpha-D-glucopyranoside
-
pH 8.0, 30°C, mutant enzyme K284A
5.3
4-nitrophenyl alpha-D-glucopyranoside
-
pH 8.0, 30°C, wild-type enzyme
0.1
alpha,alpha-trehalose 6-phosphate
-
pH 8.0, 30°C, mutant enzyme K292A
3.6
alpha,alpha-trehalose 6-phosphate
-
pH 8.0, 30°C, mutant enzyme H281A
7.2
alpha,alpha-trehalose 6-phosphate
-
pH 8.0, 30°C, mutant enzyme H282A
12.2
alpha,alpha-trehalose 6-phosphate
-
pH 8.0, 30°C, mutant enzyme K284A
18.9
alpha,alpha-trehalose 6-phosphate
-
pH 8.0, 30°C, wild-type enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
30
-
-
assay at
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
-
-
brenda
-
UniProt
brenda
-
UniProt
brenda
168
-
-
brenda
in symbiosis Glycine max
-
-
brenda
-
-
-
brenda
-
-
-
brenda
-
UniProt
brenda
-
A0A447SCD5
UniProt
brenda
-
-
-
brenda
168
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
bacteroids
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
-
brenda
-
-
brenda
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
D203E
-
no detectable activity with alpha,alpha-trehalose 6-phosphate or 4-nitrophenyl alpha-D-glucopyranoside
D329E
-
no detectable activity with alpha,alpha-trehalose 6-phosphate or 4-nitrophenyl alpha-D-glucopyranoside
E254D
-
no detectable activity with alpha,alpha-trehalose 6-phosphate or 4-nitrophenyl alpha-D-glucopyranoside
H281A
-
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
-
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
-
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
-
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
-
no detectable activity with alpha,alpha-trehalose 6-phosphate or 4-nitrophenyl alpha-D-glucopyranoside
-
E254D
-
no detectable activity with alpha,alpha-trehalose 6-phosphate or 4-nitrophenyl alpha-D-glucopyranoside
-
H281A
-
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
-
K284A
-
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
-
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
-
additional information
-
enzyme gene disruption mutant, unable to grow on trehalose, while trehalose uptake remains unaffected. Cryoprotective effect of trehalose is reduced
additional information
-
enzyme gene disruption mutant, unable to grow on trehalose, while trehalose uptake remains unaffected. Cryoprotective effect of trehalose is reduced
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
overexpressed in Escherichia coli
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
expressed in Saccharomyces cerevisiae
-
expression in Escherichia coli M15 cells
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Salminen, S.O.; Streeter, J.G.
Enzymes of alpha,alpha-trehalose metabolism in soybean nodules
Plant Physiol.
81
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
:
frenda
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
brenda
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
brenda
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
brenda
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
brenda
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)
brenda
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
Select items on the left to see more content.
html completed