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Information on EC 3.2.1.93 - alpha,alpha-phosphotrehalase
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3.2.1.93 alpha,alpha-phosphotrehalaseSpecify your search results
Word Map
- 3.2.1.93
- oligo-1,6-glucosidase
-
phosphotransferase
- hydrolases
- glucose-6-phosphate
- licheniformis
- trehalases
- guanidine
- maltose
- cereus
-
fecal
- glycosidase
-
osmolarity
- gdnhcl
- maltodextrins
- p-nitrophenyl
The enzyme appears in viruses and cellular organisms
Synonyms
trehalose-6-phosphate hydrolase, bltrea, phosphotrehalase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
BlTreA
TreA
trehalose-6-phosphate hydrolase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
alpha,alpha-trehalose 6-phosphate + H2O = D-glucose + D-glucose 6-phosphate
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
alpha,alpha-trehalose-6-phosphate phosphoglucohydrolase
-
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CAS REGISTRY NUMBER
COMMENTARY
54576-93-1
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl alpha-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucose
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
alpha-D-glucose + alpha-D-glucose 6-phosphate
-
-
-
?
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
-
-
-
?
alpha,alpha-trehalose 6-phosphate + H2O
D-glucose + D-glucose 6-phosphate
Paenibacillus popilliae NRRC B-2309MC
-
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
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
Paenibacillus popilliae NRRC B-2309MC
-
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
NaCl
-
6fold stimulation at 1 mM with 4-nitrophenyl alpha-glucopyranoside as substrate, no stimulation with alpha-trehalose 6-phosphate
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Show AA Sequence and Transmembrane Helices (4257 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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
A0A447SCD5, Q65MI2
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, Q65MI2
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Paenibacillus popilliae, Paenibacillus popilliae NRRC B-2309MC
brenda
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, Bacillus subtilis 168
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 (Q65MI2), Bacillus licheniformis, 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 (A0A447SCD5), Bacillus licheniformis (Q65MI2), Bacillus licheniformis, Bacillus licheniformis 168 (Q65MI2)
brenda
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