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Information on EC 2.4.1.15 - alpha,alpha-trehalose-phosphate synthase (UDP-forming) and Organism(s) Escherichia coli and UniProt Accession P31677
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2.4.1.15 alpha,alpha-trehalose-phosphate synthase (UDP-forming)IUBMB Comments
See also EC 2.4.1.36 [alpha,alpha-trehalose-phosphate synthase (GDP-forming)].
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Word Map
- 2.4.1.15
- trehalase
- disaccharide
- tpp
-
desiccation
-
thermotolerance
-
resurrection
- udp-glc
- validamycin
-
anhydrobiosis
- selaginella
- agriculture
- drug development
- medicine
- analysis
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Synonyms
trehalose-6-phosphate synthase, transglucosylase, trehalose 6-phosphate synthase, trehalose phosphate synthase, tps-2, trehalose-6-phosphate synthase 1, t6p synthase, trehalose-6p synthase, trehalose-6-p synthase, t-6-p, 
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topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
alpha,alpha-trehalose phosphate synthase (UDP-forming)
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glucosyltransferase, uridine diphosphoglucose phosphate
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OtsA
phosphotrehalose-uridine diphosphate transglucosylase
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TPS
transglucosylase
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trehalose 6-phosphate synthase
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trehalose 6-phosphate synthetase
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trehalose phosphate synthase
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trehalose phosphate synthetase
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trehalose phosphate-uridine diphosphate glucosyltransferase
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trehalose-6-phosphate synthase
trehalose-P synthetase
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trehalosephosphate-UDP glucosyl transferase
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UDP-glucose:D-glucose-6-phosphate 1-alpha-D-glucosyltransferase
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UDPglucose-glucose-phosphate glucosyltransferase
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TPS
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-glucose + D-glucose 6-phosphate = UDP + alpha,alpha-trehalose 6-phosphate
reaction mechanism
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
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PATHWAY SOURCE
PATHWAYS
BRENDA
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SYSTEMATIC NAME
IUBMB Comments
UDP-glucose:D-glucose-6-phosphate 1-alpha-D-glucosyltransferase
See also EC 2.4.1.36 [alpha,alpha-trehalose-phosphate synthase (GDP-forming)].
CAS REGISTRY NUMBER
COMMENTARY
9030-07-3
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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
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
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-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
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-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
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-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
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step in trehalose biosynthesis
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-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
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with retention of the anomeric configuration of the UDP-sugar donor, reaction stereochemistry
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-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
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?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
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enzyme is osmotically inducible, mutants which are defective in the synthesis of the synthase have an impaired osmotic tolerance in glucose-mineral medium
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?
additional information
?
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trehalose acts as a global protectant against abiotic stress, accumulation of trehalose leads to increased salt, drought, and cold resistance in plants
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-
?
additional information
?
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trehalose is able to protect the integrity of the cells against a variety of environmental stresses such as desiccation, dehydration, heat, cold, and oxidation, probably via reduction of protein denaturation through protein-trehalose interactions
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-
?
additional information
?
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donor subsite interactions, enzyme-substrate binding conformation, the N-terminal loop, residues 9-22, is responsible for the more relaxed coformation of the binary enzyme-UDP-sugar complex, overview
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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
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
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-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
-
-
?
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
-
step in trehalose biosynthesis
-
-
?
UDPglucose + glucose 6-phosphate
trehalose 6-phosphate + UDP
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enzyme is osmotically inducible, mutants which are defective in the synthesis of the synthase have an impaired osmotic tolerance in glucose-mineral medium
-
?
additional information
?
-
-
trehalose acts as a global protectant against abiotic stress, accumulation of trehalose leads to increased salt, drought, and cold resistance in plants
-
-
?
additional information
?
-
-
trehalose is able to protect the integrity of the cells against a variety of environmental stresses such as desiccation, dehydration, heat, cold, and oxidation, probably via reduction of protein denaturation through protein-trehalose interactions
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
7.5
glucose 6-phosphate
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bifunctional fusion enzyme of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase
additional information
additional information
-
bifunctional fusion enzyme of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase
-
5.1
UDPglucose
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bifunctional fusion enzyme of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
bifunctional fusion enzyme of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase
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3.2
glucose 6-phosphate
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bifunctional fusion enzyme of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase
3.6
UDPglucose
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bifunctional fusion enzyme of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 40
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bifunctional fusion enzyme of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
in complex with UDP and D-glucose 6-phosphate, using 14% (w/v) PEG 4000, 0.15 M NaOAc, 0.1 M imidazole buffer (pH 7.5), and 200 mM NaCl
apoenzyme, sitting drop vapor diffusion method, using 0.1 M Tris, pH 8.5, and 25% (w/v) PEG3350
purified recombinant enzyme complexed with either substrate UDP-glucose or the inactive substrate analogue UDP-2-deoxy-2-fluoroglucose, hanging drop vapour diffusion method, 100 nl droplets of 10 mg/ml protein in 20 mM Tris-HCl, pH 8.0, and 200 mM NaCl, with either 25 mM UDP-glucose and 50 mM 1-deoxy-glucose 6-phosphate or 25 mM UDP-2-deoxy-2-fluoroglucose and 20 mM glucose 6-phosphate, precipitant solution: 30% w/v PEG 4000, 200 mM ammonium acetate, 100 mM Tris-HCl, pH 8.0, 36 h, 25% ethylene glycol as cryoprotectant, X-ray diffraction structure determination and analysis at 2.0 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
construction of transgenic Oryza sativa plants expressing the catalytically active enzyme as a fusion protein with trehalose-6-phosphate phosphatase of Escherichia coli under control of the ubiquitin promotor from Zea mays, the transgenic plants produce high levels of trehalose in seeds and leaves, carbohydrate profile of seeds, but not of leaves, is altered, plants show no growth inhibition or altered phenotype
additional information
-
construction of transgenic Oryza sativa plants expressing the catalytically active enzyme as a fusion protein with trehalose-6-phosphate phosphatase of Escherichia coli under control of the ubiquitin promotor from Zea mays, the transgenic plants produce high levels of trehalose in seeds and leaves, carbohydrate profile of seeds, but not of leaves, is altered, plants show no growth inhibition or altered phenotype, expression in human fibroblasts renders the cells less sensitive to drought compared to wild-type cells
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
bifunctional fusion enzyme of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase
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nickel chelating bead chromatography and Superdex S200 gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
construction of a bifunctional fusion enzyme of trehalose-6-phosphate synthetase and trehalose-6-phosphate phosphatase and expression in Escherichia coli
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functional expression of the enzyme as a fusion protein with Escherichia coli trehalose-6-phosphate phosphatase in transgenic Oryza sativa plants
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functional expression of the enzyme as a fusion protein with Escherichia coli trehalose-6-phosphate phosphatase in transgenic Oryza sativa plants, expression in human fibroblasts
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Giaever, H.M.; Styrvold, O.; Kaasen, I.; Strom, A.R.
Biochemical and genetic characterization of osmoregulatory trehalose synthesis in Escherichia coli
J. Bacteriol.
170
2841-2849
1988
Escherichia coli
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
Gibson, R.P.; Lloyd, R.M.; Charnock, S.J.; Davies, G.J.
Characterization of Escherichia coli OtsA, a trehalose-6-phosphate synthase from glycosyltransferase family 20
Acta Crystallogr. Sect. D
58
349-351
2002
Escherichia coli
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
Gibson, R.P.; Tarling, C.A.; Roberts, S.; Withers, S.G.; Davies, G.J.
The donor subsite of trehalose-6-phosphate synthase: binary complexes with UDP-glucose and UDP-2-deoxy-2-fluoro-glucose at 2 A resolution
J. Biol. Chem.
279
1950-1955
2004
Escherichia coli
Chen, Q.; Haddad, G.G.
Role of trehalose phosphate synthase and trehalose during hypoxia: from flies to mammals
J. Exp. Biol.
207
3125-3129
2004
Candida albicans, Drosophila melanogaster, Escherichia coli, Saccharomyces cerevisiae, Schizosaccharomyces pombe
Gibson, R.P.; Turkenburg, J.P.; Charnock, S.J.; Lloyd, R.; Davies, G.J.
Insights into trehalose synthesis provided by the structure of the retaining glucosyltransferase OtsA
Chem. Biol.
9
1337-1346
2002
Escherichia coli (P31677)
Kaasen, I.; McDougall, J.; Strom, A.R.
Analysis of the otsBA operon for osmoregulatory trehalose synthesis in Escherichia coli and homology of the OtsA and OtsB proteins to the yeast trehalose-6-phosphate synthase/phosphatase complex
Gene
145
9-15
1994
Escherichia coli
Wang, S.; Zhao, Y.; Yi, L.; Shen, M.; Wang, C.; Zhang, X.; Yang, J.; Peng, Y.L.; Wang, D.; Liu, J.
Crystal structures of Magnaporthe oryzae trehalose-6-phosphate synthase (MoTps1) suggest a model for catalytic process of Tps1
Biochem. J.
476
3227-3240
2019
Escherichia coli (A0A376VH75), Escherichia coli, Pyricularia oryzae (G4NHF4), Pyricularia oryzae
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