Any feedback?
Please rate this page
(enzyme.php)
(0/150)

BRENDA support

BRENDA Home
show all | hide all No of entries

Information on EC 3.1.3.12 - trehalose-phosphatase and Organism(s) Escherichia coli and UniProt Accession P31678

for references in articles please use BRENDA:EC3.1.3.12
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
     3 Hydrolases
         3.1 Acting on ester bonds
             3.1.3 Phosphoric-monoester hydrolases
                3.1.3.12 trehalose-phosphatase
Specify your search results
Select one or more organisms in this record: ?
This record set is specific for:
Escherichia coli
UNIPROT: P31678 not found.
Show additional data
Do not include text mining results
Include (text mining) results
Include results (AMENDA + additional results, but less precise)
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
trehalose-6-phosphate phosphatase, attps1, ostpp1, gob-1, trehalose 6-phosphate phosphatase, otsb2, trehalose-6-phosphate synthase/phosphatase, trehalose phosphate phosphatase, t6p phosphatase, trehalose-phosphate phosphatase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
trehalose 6-phosphatase
-
-
-
-
trehalose 6-phosphate phosphatase
trehalose phosphate phosphatase
-
-
-
-
trehalose-6-phophate synthase/phosphatase
-
-
trehalose-6-phosphate synthase/phosphatase
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
alpha,alpha-trehalose-6-phosphate phosphohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9025-72-3
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
show the reaction diagram
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
show the reaction diagram
trehalose-6-phosphate + H2O
trehalose + phosphate
show the reaction diagram
-
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
show the reaction diagram
-
-
-
?
trehalose 6-phosphate + H2O
trehalose + phosphate
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.5 - 2.6
trehalose 6-phosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
14.3 - 14.6
trehalose 6-phosphate
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.2
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 40
-
both the chimeric enzyme and the equimolar mixture of trehalose 6-phosphate synthetase/trehalose 6-phosphate phosphatase
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
A7UHA1_ECOLX
266
0
29177
TrEMBL
-
A0A6G8E6T5_ECOLX
266
0
29203
TrEMBL
-
A0A8H1TUX4_ECOLX
266
0
29207
TrEMBL
-
A0A830VFJ3_ECOLX
265
0
29284
TrEMBL
-
A0A5F1DYR6_ECOLX
267
0
29408
TrEMBL
-
A0A376WWZ3_ECOLX
110
0
12026
TrEMBL
-
C3T5B2_ECOLX
266
0
29232
TrEMBL
-
A0A7D7HKL2_ECOLX
267
0
29325
TrEMBL
-
A0A828GE29_ECOLX
265
0
29184
TrEMBL
-
A0A8H1XIR1_ECOLX
266
0
29147
TrEMBL
-
A0A827B8I3_ECOLX
267
0
29248
TrEMBL
-
A0A4C7B3I2_ECOLX
266
0
29222
TrEMBL
-
A0A828AJV7_ECOLX
265
0
29269
TrEMBL
-
A0A1U9T4N8_ECOLX
266
0
29204
TrEMBL
-
A0A3L9I523_ECOLX
170
0
18724
TrEMBL
-
A0A6D0IDS8_ECOLX
226
0
24677
TrEMBL
-
A0A2X8Q3V0_ECOLX
266
0
29147
TrEMBL
-
A0A085NZW8_ECOLX
266
0
29205
TrEMBL
-
A0A827K129_ECOLX
267
0
29305
TrEMBL
-
A0A826QZF1_ECOLX
267
0
29246
TrEMBL
-
A0A377D338_ECOLX
140
0
15586
TrEMBL
-
A0A765X5W7_ECOLX
265
0
29166
TrEMBL
-
A0A3L5H4I1_ECOLX
248
0
26921
TrEMBL
-
A0A8B5LIM8_ECOLX
266
0
29205
TrEMBL
-
A0A376RHI0_ECOLX
140
0
15574
TrEMBL
-
A0A376YBN3_ECOLX
266
0
29175
TrEMBL
-
A0A368IVK6_ECOLX
266
0
29173
TrEMBL
-
A0A7A0S3H5_ECOLX
266
0
29147
TrEMBL
-
A0A826WZ08_ECOLX
267
0
29512
TrEMBL
-
A0A6L7CMM9_ECOLX
183
0
20097
TrEMBL
-
A0A6D0NV77_ECOLX
266
0
29182
TrEMBL
-
A0A3Q0MZ25_ECOLX
266
0
29277
TrEMBL
-
A0A346HPQ2_ECOLX
266
0
29163
TrEMBL
-
A0A0A0H0P9_ECOLX
285
0
31569
TrEMBL
-
A0A3K0JXN4_ECOLX
266
0
29108
TrEMBL
-
A0A8H0EVE5_ECOLX
266
0
29223
TrEMBL
-
A0A8H0PUH2_ECOLX
266
0
29203
TrEMBL
-
A0A0K5LNC3_ECOLX
266
0
29141
TrEMBL
-
A0A484X1Z8_ECOLX
77
0
8531
TrEMBL
-
A0A1M0CUY9_ECOLX
266
0
29090
TrEMBL
-
A0A826XL94_ECOLX
267
0
29276
TrEMBL
-
A0A826YXY2_ECOLX
267
0
29301
TrEMBL
-
A0A827LD69_ECOLX
265
0
29156
TrEMBL
-
A0A3F3P1N3_ECOLX
266
0
29191
TrEMBL
-
A0A0J2BEG5_ECOLX
266
0
29148
TrEMBL
-
A0A1Q6BH07_ECOLX
266
0
29127
TrEMBL
-
A0A2U9KPQ8_ECOLX
266
0
29161
TrEMBL
-
A0A8H0XKK2_ECOLX
266
0
29191
TrEMBL
-
A0A827QRT1_ECOLX
266
0
29067
TrEMBL
-
A0A828PFE2_ECOLX
266
0
29143
TrEMBL
-
A0A2T3UCH4_ECOLX
266
0
29191
TrEMBL
-
A0A8B5LXR3_ECOLX
266
0
29174
TrEMBL
-
A0A8H9AQT0_ECOLX
266
0
29119
TrEMBL
-
A0A7A3B0B8_ECOLX
267
0
29273
TrEMBL
-
A0A6L9DQY9_ECOLX
266
0
29175
TrEMBL
-
A0A377A5E7_ECOLX
253
0
27563
TrEMBL
-
A0A2X6JEI5_ECOLX
266
0
29160
TrEMBL
-
A0A0K4MXE5_ECOLX
265
0
29212
TrEMBL
-
A0A838ALZ6_ECOLX
267
0
29262
TrEMBL
-
A0A827X7B2_ECOLX
266
0
29108
TrEMBL
-
A0A827GH57_ECOLX
265
0
29174
TrEMBL
-
A0A7H9LTP1_ECOLX
267
0
29301
TrEMBL
-
A0A246NT99_ECOLX
266
0
29217
TrEMBL
-
A0A2X1NJQ0_ECOLX
266
0
29173
TrEMBL
-
A0A6D0HF53_ECOLX
266
0
29122
TrEMBL
-
A0A0J8XZE3_ECOLX
266
0
29161
TrEMBL
-
C1KFX6_ECOLX
266
0
29175
TrEMBL
-
A0A4Y8GZ95_ECOLX
266
0
29161
TrEMBL
-
A0A793TTC6_ECOLX
266
0
29124
TrEMBL
-
A0A826YXH3_ECOLX
266
0
29164
TrEMBL
-
A0A827KUX8_ECOLX
267
0
29274
TrEMBL
-
A0A6D0IKC2_ECOLX
82
0
8876
TrEMBL
-
A0A376RIC3_ECOLX
142
0
15856
TrEMBL
-
A0A376X1T8_ECOLX
111
0
12361
TrEMBL
-
A0A5F1UUM8_ECOLX
266
0
29170
TrEMBL
-
A0A0D6ISI6_ECOLX
266
0
29134
TrEMBL
-
A0A8H0DU54_ECOLX
266
0
29233
TrEMBL
-
A0A8G8WN74_ECOLX
266
0
29162
TrEMBL
-
A0A5R1M5W6_ECOLX
266
0
29219
TrEMBL
-
A0A377B9W1_ECOLX
229
0
25468
TrEMBL
-
A0A484X2M3_ECOLX
203
0
22399
TrEMBL
-
A0A1V3W1T9_ECOLX
266
0
29218
TrEMBL
-
A0A7D7HZR4_ECOLX
266
0
29258
TrEMBL
-
A0A2W6NU58_ECOLX
266
0
29247
TrEMBL
-
A0A376SA05_ECOLX
85
0
9923
TrEMBL
-
A0A366YK32_ECOLX
266
0
29148
TrEMBL
-
A0A6G4JXK1_ECOLX
266
0
29171
TrEMBL
-
A0A3L1NF29_ECOLX
266
0
29189
TrEMBL
-
A0A7B1QWF9_ECOLX
266
0
29093
TrEMBL
-
Q6PQ83_ECOLX
266
0
29203
TrEMBL
-
A0A376S8P3_ECOLX
104
0
11056
TrEMBL
-
A0A066T1M6_ECOLX
266
0
29164
TrEMBL
-
A0A1Q9REV6_ECOLX
266
0
29189
TrEMBL
-
A0A6D0EKW6_ECOLX
154
0
16601
TrEMBL
-
A0A5N8HJK3_ECOLX
221
0
24153
TrEMBL
-
A0A6C8S835_ECOLX
266
0
29207
TrEMBL
-
A0A6L7CGS5_ECOLX
253
0
27620
TrEMBL
-
A0A827ZKY6_ECOLX
265
0
29271
TrEMBL
-
A0A0A1A932_ECOLX
266
0
29191
TrEMBL
-
A0A4Y8ERP2_ECOLX
266
0
29145
TrEMBL
-
A0A8H0NSE4_ECOLX
266
0
29215
TrEMBL
-
A0A4C3QXN2_ECOLX
266
0
29191
TrEMBL
-
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37400
-
SDS-PAGE
53610
-
deduced from cDNA
88300
-
chimeric enzyme which contains trehalose 6-phosphate synthetase and trehalose 6-phosphate phosphatase, SDS-PAGE
973000
-
calculated from amino acid sequence
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
-
1 * 37400, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
a bifunctional fusion enzyme is constructed by fusing genes for trehalose 6-phosphate synthetase and trehalose 6-phosphate phosphatase, this enzyme catalysing sequential reactions has kinetic advantages over a mixture of both enzymes
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
trehalose has been implicated in tolerance to abiotic stress in plants, so the response to heat stress of seeds from the transgenic lines of Solanum lycopersicum cv. Joyful and seeds from wild-type plants are compared. Wild-type heat-treated seeds have a germination rate of 17%, while four transgenic lines have germination rates over 50% following heat stress at 55°C. In one heat-treated transgenic line, 100% of the seeds germinated, and therefore had a germination rate six times that of seeds from wild-type plants. Quantitative PCR reveals that the expression of diverse genes that respond to heat stress is enhanced in TPSP transgenic seeds compared to wild-type seeds 150 min after the onset of heat stress. The enhanced germination rate and expression of these genes in the transgenic seeds are essentially mimicked in wild-type seeds treated with 1 mM exogenous trehalose. Accumulated trehalose and associated metabolites may act as signaling molecules that enhance the expression of heat stress-responsive genes and confer heat-stress tolerance to seeds. Changed of transcript levels of imbibed seeds in TPSP transgenic and wild type with exogenous trehalose under no heat-treated condition, overview
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
50
-
the termal stability of chimeric enzyme and equimolare mixture are quite similar
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
trehalose can have a positive effect in preventing recombinant protein aggregation
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
the chimeric gene
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloned as an operon and expressed in Escherichia coli M15(pREP4)
-
commentary
-
expressed in Escherichia coli
-
heterologous expression of enzyme in Cornebacterium glutamicum, the new recombinant strain shows a five- to sixfold increase in the enzymatic activity of the trehalose 6-phosphate synthase and –phosphatase system
-
heterologous expression of enzyme in corynebacterium glutamicum, the new recombinant strain shows a five- to sixfold increase in the enzymatic activity of the trehalose 6-phosphate synthase and –phosphatase system
-
recombinant overexpression of trehalose-6-phosphate synthase/phosphatase (TPSP) in transgenic Solanum lycopersicum cv. Joyful leading to enhanced level of trehalose in the seeds
the chimeric gene is expressed in Escherichia coli
-
the chimeric gene is expressed in Escherichia coli, a bifunctional fusion enzyme is constructed by fusing genes for trehalose 6-phosphate synthetase and trehalose 6-phosphate phosphatase, this enzyme catalysing sequential reactions has kinetic advantages over a mixture of both enzymes
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
biotechnology
-
The transformation of rice plants with a gene that encodes a bifunctional fusion enzyme of trehalose-6-phosphate synthase and – phosphatase from Escherischia coli increases the trehalose levels in these plants, shows no visible growth inhibition. The production of trehalose in these plants results in increased tolerance to drought, salt, and cold stresses.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Borgia, P.T.; Miao, Y.; Dodge, C.L.
The orlA gene from Aspergillus nidulans encodes a trehalose-6-phosphate phosphatase necessary for normal growth and chitin synthesis at elevated temperatures
Mol. Microbiol.
20
1287-1296
1996
Aspergillus nidulans, Saccharomyces cerevisiae, Escherichia coli
Manually annotated by BRENDA team
Seo, H.S.; Koo, Y.J.; Lim, J.Y.; Song, J.T.; Kim, C.H.; Kim, J.K.; Lee, J.S.; Choi, Y.D.
Characterization of a bifunctional enzyme fusion of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase of Escherichia coli
Appl. Environ. Microbiol.
66
2484-2490
2000
Escherichia coli
Manually annotated by BRENDA team
Padilla, L.; Kramer, R.; Stephanopoulos, G.; Agosin, E.
Overproduction of trehalose: heterologous expression of Escherichia coli trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase in Corynebacterium glutamicum
Appl. Environ. Microbiol.
70
370-376
2004
Escherichia coli
Manually annotated by BRENDA team
Kong, X.; Liu, Y.; Gou, X.; Zhang, H.; Wang, X.; Zhang, J.
Directed Evolution of Operon of Trehalose-6-phosphate Synthase/Phosphatase from Escherichia coli
Biochem. Biophys. Res. Commun.
280
396-400
2001
Saccharomyces cerevisiae, Escherichia coli
Manually annotated by BRENDA team
Jang, I.C.; Oh, S.J.; Seo, J.S.; Choi, W.B.; Song, S.I.; Kim, C.H.; Kim, Y.S.; Seo, H.S.; Choi, Y.D.; Nahm, B.H.; Kim, J.K.
Expression of a bifunctional fusion of the Escherichia coli genes for trehalose-6-phosphate synthase and trehalose-6-phosphate phosphatase in transgenic rice plants increases trehalose accumulation and abiotic stress tolerance without stunting growth
Plant Physiol.
131
516-524
2003
Escherichia coli
Manually annotated by BRENDA team
Schultz, T.; Liu, J.; Capasso, P.; de Marco, A.
The solubility of recombinant proteins expressed in Escherichia coli is increased by otsA and otsB co-transformation
Biochem. Biophys. Res. Commun.
355
234-239
2007
Escherichia coli
Manually annotated by BRENDA team
Joseph, T.C.; Rajan, L.A.; Thampuran, N.; James, R.
Functional Characterization of Trehalose Biosynthesis Genes from E. coli: An Osmolyte Involved in Stress Tolerance
Mol. Biotechnol.
46
20-25
2010
Escherichia coli
Manually annotated by BRENDA team
Lyu, J.; Park, J.; Kim, J.; Bae, C.; Jeong, W.; Min, S.; Liu, J.
Enhanced tolerance to heat stress in transgenic tomato seeds and seedlings overexpressing a trehalose-6-phosphate synthase/phosphatase fusion gene
Plant Biotechnol. Rep.
12
399-408
2018
Escherichia coli (P31677 AND P31678)
-
Manually annotated by BRENDA team