Information on EC 3.1.3.12 - trehalose-phosphatase

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.
Specify your search results
Select one or more organisms in this record:


The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea

EC NUMBER
COMMENTARY hide
3.1.3.12
-
RECOMMENDED NAME
GeneOntology No.
trehalose-phosphatase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-trehalose + phosphate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis of phosphoric ester
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
glycogen biosynthesis III (from alpha-maltose 1-phosphate)
-
-
mycolate biosynthesis
-
-
trehalose biosynthesis I
-
-
trehalose biosynthesis II
-
-
trehalose biosynthesis III
-
-
metabolism of disaccharids
-
-
Starch and sucrose metabolism
-
-
Metabolic pathways
-
-
SYSTEMATIC NAME
IUBMB Comments
alpha,alpha-trehalose-6-phosphate phosphohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY hide
9025-72-3
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene AFUB_043350
-
-
Manually annotated by BRENDA team
gene AFUB_043350
-
-
Manually annotated by BRENDA team
in symbiosis with Glycine max, strain USDA 110 - a low trehalose accumulator, and strain USDA 61A76 - a high trehalose accumulator
-
-
Manually annotated by BRENDA team
gene gob-1, several strains
-
-
Manually annotated by BRENDA team
juveniles
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
cultivar Yukihikari
UniProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
inbred lines RIL115 and RIL147
-
-
Manually annotated by BRENDA team
fragment
UniProt
Manually annotated by BRENDA team
; bifunctional trehalose-6-phosphate synthase/phosphatase, EC 2.4.1.15 and EC 3.1.3.12
SwissProt
Manually annotated by BRENDA team
bifunctional trehalose-6-phosphate synthase/phosphatase, EC 2.4.1.15 and EC 3.1.3.12
SwissProt
Manually annotated by BRENDA team
gene otsB
SwissProt
Manually annotated by BRENDA team
gene otsB
SwissProt
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
malfunction
metabolism
physiological function
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
2-Deoxy-D-glucose 6-phosphate + H2O
2-Deoxy-D-glucose + phosphate
show the reaction diagram
-
-
-
-
?
alpha,alpha-1,1-trehalose 6-phosphate
alpha,alpha-1,1-trehalose + phosphate
show the reaction diagram
alpha,alpha-trehalose 6-phosphate + H2O
alpha,alpha-trehalose + phosphate
show the reaction diagram
D-fructose 6-phosphate + H2O
D-fructose + phosphate
show the reaction diagram
D-glucose 6-phosphate + H2O
D-glucose + phosphate
show the reaction diagram
D-mannose 6-phosphate + H2O
D-mannose + phosphate
show the reaction diagram
-
16% of the activity with trehalose 6-phosphate
-
-
?
glucose 6-phosphate + H2O
?
show the reaction diagram
trehalose 6-phosphate + H2O
trehalose + phosphate
show the reaction diagram
trehalose-6-phosphate + H2O
trehalose + phosphate
show the reaction diagram
UDP-alpha-D-glucose + D-glucose 6-phosphate
UDP + alpha,alpha-trehalose 6-phosphate
show the reaction diagram
additional information
?
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
trehalose 6-phosphate + H2O
trehalose + phosphate
show the reaction diagram
trehalose-6-phosphate + H2O
trehalose + phosphate
show the reaction diagram
additional information
?
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
has significant positive effect on enzyme activity
K+
in the present of K+, the enzyme is less active than in the presence of Mg2+ and Co2+
Na+
-
NaCl has a slightly negative effect on OtsB activity in the range of 0-250 mM, but is clearly inhibitory (over 30%) at higher concentrations
additional information
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
acetate
-
no activity in Tris-citrate and only minimal activity in acetate buffer
arsenate
-
10 mM, 10% inhibition
CDTA
-
strong inhibition
citrate
D-glucose 6-sulfate
-
-
deoxycholate
-
even 0.025%
Diumycin
-
EGTA
-
strong inhibition
glucose
-
competitive inhibition of hydrolysis of glucose 6-phosphate, ineffective against hydrolysis of trehalose 6-phosphate
Moenomycin
NaF
-
strongly inhibited (70%) by 10 mM NaF
phosphate
-
-
Sarkosyl
-
even 0.025%
trehalose
-
-
trehalose 6-sulfate
-
competitive inhibitor
additional information
-
not: 10 mM sodium fluoride, 10 mM sodium orthovanadate, Nonident P-40, Triton X-100, octyl glucoside
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ADP-glucose
activates 4.5% at 5 mM
GDP-glucose
activates 3.6% at 5 mM
phosphate
-
increases activity
TDP-glucose
activates 4.6% at 5 mM
trehalose
-
activates hydrolysis of glucose 6-phosphate, no activation of trehalose 6-phosphate
UDP-glucose
activates 10% at 5 mM
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.25 - 0.5
glucose 6-phosphate
-
-
0.04 - 6.1
Trehalose 6-phosphate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03 - 24
Trehalose 6-phosphate
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.11 - 450
Trehalose 6-phosphate
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.6
Cu2+
-
in presence of 5 mM Mg2+
10
D-glucose 6-sulfate
-
Ki above 10 mM, wild type enzyme, at pH 7.5 and 22°C
10
trehalose
-
Ki above 10 mM, wild type enzyme, at pH 7.5 and 22°C
0.082
trehalose 6-sulfate
-
wild type enzyme, at pH 7.5 and 22°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.01033
-
cell lysate, at pH 8.5 and 30°C
0.4505
-
after 43.6fold purification, at pH 8.5 and 30°C
0.631
-
trehalose activated hydrolysis of glucose 6-phosphate
2.9
pH 7.0, 80°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6 - 6.5
-
hydrolysis of trehalose 6-phosphate
6
-
hydrolysis of glucose 6-phosphate in presence of trehalose
7.2
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.5 - 7.5
the enzyme activity remains nearly constant from pH 5.0 to 7.0 in Mes/NaOH buffer and 7.0 to 7.5 in Tris/HCl buffer, whereas the enzyme shows almost no activity at pH 9.0 (Tris/HCl buffer) and half activity at pH 4.0 (acetate buffer)
5.5 - 9
5.8 - 8.2
-
pH 5.8: about 20% of maximal activity, pH 8.2: about 75% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
assay at room temperature
30 - 40
-
both the chimeric enzyme and the equimolar mixture of trehalose 6-phosphate synthetase/trehalose 6-phosphate phosphatase
60
-
assay at and optimal activity
70
recombinant enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 30
the enzyme exhibits full activity at 30°C, about 92% of the maximal activity at 20°C, about 85% of the maximal activity at 12°C, and still 75% of the maximal activity at 4°C
25 - 60
-
activity range
30 - 58
-
30°C: about 45% of maximal activity, 58°C: about 85% of mmaximal activity
40 - 90
recombinant enzyme, 45% of maximal activity at 90°C, about 15% at 40°C
pI VALUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.1
calculated from amino acid sequence
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
gene expression in
Manually annotated by BRENDA team
-
isoforms TPPA and TPPG are preferentially expressed in atrichoblast cells
Manually annotated by BRENDA team
gene expression in
Manually annotated by BRENDA team
gene expression in
Manually annotated by BRENDA team
i.e. Y-organ, gene expression in
Manually annotated by BRENDA team
gene expression in
Manually annotated by BRENDA team
gene expression in
Manually annotated by BRENDA team
-
lethal gut-obstructed-gene 1, gob-1
Manually annotated by BRENDA team
gene expression in
Manually annotated by BRENDA team
gene expression in
Manually annotated by BRENDA team
gene expression in
Manually annotated by BRENDA team
gene expression in
Manually annotated by BRENDA team
-
accumulates mostly in young inflorescences at the stage of axillary meristem primordia initiation
Manually annotated by BRENDA team
-
moderate activty
Manually annotated by BRENDA team
-
lowest activity
Manually annotated by BRENDA team
gene expression in
Manually annotated by BRENDA team
-
highest activity in lower length of the uterus, lower activity in central and upper uterus
Manually annotated by BRENDA team
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25000 - 26000
-
gel filtration, sucrose density gradient centrifugation
26360
-
x * 26360, calculation from nucleotide sequence
27000
-
gel filtration
27873
1 * 27873, calculated from amino acid sequence
28000
1 * 28000, SDS-PAGE
29400
-
deduced from cDNA
33000
x * 81000, TPSP holoenzyme, x * 50000, isolated trehalose-6-phosphate synthase domain, x * 33000, isolated trehalose-6-phosphate phophatase domain
37400
-
SDS-PAGE
42600
deduced from the nucleotide sequence
46228
-
x * 46228, MALDI-TOF mass spectrometry
46236
-
x * 46236, calculated from amino acid sequence
50000
x * 81000, TPSP holoenzyme, x * 50000, isolated trehalose-6-phosphate synthase domain, x * 33000, isolated trehalose-6-phosphate phophatase domain
53610
-
deduced from cDNA
60000
-
x * 60000, recombinant His6-tagged SDS-PAGE
81000
x * 81000, TPSP holoenzyme, x * 50000, isolated trehalose-6-phosphate synthase domain, x * 33000, isolated trehalose-6-phosphate phophatase domain
82000
-
x * 82000, SDS-PAGE
82108
-
x * 82108, MALDI-TOF mass spectrometry
88300
-
chimeric enzyme which contains trehalose 6-phosphate synthetase and trehalose 6-phosphate phosphatase, SDS-PAGE
104000
calculation from amino acid sequence
973000
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
additional information
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
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapor diffusion method, using 33% (w/v) PEG 300, 0.1 M sodium citrate pH 5.0, 13% ethylene glycol and 10 mM CoCl2
-
sitting drop vapour diffusion method with 30% PEG 4000, 0.2 M MgCl2, and 0.1 M Tris-HCl (pH 8.5)
-
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
4 - 12
-
the enzyme retains almost 60% activity in highly alkaline condition (pH 10.0) or moderately acidic condition (pH 6.0). Almost 40% activity still remains in pH as low as 4.0 or as high as 12.0
730106
5.5 - 9
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30 - 60
-
the enzyme is most stable up to 30°C. The enzyme is also able to show almost 50% activity at temperatures as high as 60°C
40 - 60
-
enzyme is stable to heating or 6 min
53
-
5 min, 25% loss of activity
57
-
15 min, 15% loss of activity
80
half-life of the recombinant enzyme is 161 min
90
half-life of the recombinant enzyme is 120 min
100
half-life of the recombinant enzyme is 40 min
additional information
-
-
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
trehalose can have a positive effect in preventing recombinant protein aggregation
-
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
the enzyme is solubilized in presence of 0.2% sarkosyl
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-12°C, completely stable for at least 2 months
-
-20°C, stable at least several weeks
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
ammonium sulfate precipitation, Protein-Pak DEAE column chromatography and Biosuite 125 gel filtration
-
gel filtration
glutathione-Sepharose 4B affinity column chromatography
HiTrap Q column chromatography
-
Ni-NTA affinity chromatography
-
Ni-NTA affinity column chromatography and S200 gel filtration
-
Ni-NTA agarose column chromatography
Ni-NTA resin column chromatography and S200 gel filtration
-
recombinant GST-tagged enzyme from Escherichia coli by glutathione affinity chromatography, gel filtration, and ion exchange chromatography, to homogeneity, the GST-tag is cleaved off by thrombin
recombinant GST-tagged enzyme from Escherichia coli strain BL21(DE3)
-
recombinant His6-tagged enzyme from Escherichia coli by nickel affinity chromatography
-
the chimeric gene
-
trehalose-6-phosphate synthase/phosphatase complex
-
using Ni-NTA chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cloned as an operon and expressed in Escherichia coli M15(pREP4)
-
commentary
construction of homozygous and heterozygous deletion mutants, the homozygous deletion mutants has little or no enzyme activity, the complete inactivation of enzyme results in 50fold hyperaccumulation of trehalose 6-phosphate, thermosensitivity, and rapid death of the cells after a few hours at 44°C
-
DNA and amino acid sequence determination and analysis, expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3) and release into the soluble fraction with a natively folded conformation
-
expressed in Arabidopsis thaliana
-
expressed in Escherichia coli
expressed in Escherichia coli as a His-tagged fusion protein
-
expressed in Escherichia coli BL21 cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli strain JM107
-
expressed in Escherichia coli T7 Express cells
-
expressed in Escherichia coli, pBluescript SK vector, pHB expression vector
expressed in Saccharomyces cerevisiae
expressed in Saccharomyces cerevisiae mutants tps1 (encoding a synthase domain) and tps2 (encoding synthase and phosphatase domains)
-
expression in a yeast tps2 mutant strain with functional complementation and rescue of the mutant phenotype at high temperature
-
expression in Escherichia coli
expression of the enzyme as single transcript in transgenic Solanum tuberosum cv. Sumi plants using the Ti plasmid and the Agrobacterium tumefaciens, strain LBA4404, infection system leading to drought-resistance of the transgenic plants
-
gene AFUB_043350, DNA and amino acid sequence determination and analysis
-
gene gob-1, DNA and amino acid sequence determination and analysis, expression pattern, expression of GST-tagged enzyme in Escherichia coli strain BL21(DE3)
-
gene otsB, DNA and amino acid sequence determination and analysis, overexpression of GST-tagged enzyme in Eschrichia coli strains XL1-Blue and BL21
gene Rv3372, expression of His-tagged enzyme in Escherichia coli strains DH5alpha and HMS-F
-
gene TPP1, expression analysis in rice, low level expression under normal conditions, induction under chilling stress, transient expression in and functional complementation of a yeast enzyme-deficient mutant strain
-
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
-
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
-
the disruption of gene leads to aggregation of the cells in stationary phase and greatly decreases infectivity of Candida albicans in mice
the expression of mRNA under saline condition, heat shock and cold shock is studied by Nothern blot analysis: salt stress and heat stress reduce the expression of gene
transcriptional coexpression networks developed
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
almost 1.8fold increase in activity is observed when the concentration of S-adenosyl-L-methionine is increased from 0 to 2 mM
-
AtTPS5 expression is strongly induced 6 h after sucrose feeding; AtTPS6 expression is slightly induced upon cytokinin treatment; expression is clearly induced after cytokinin treatment; expression is slightly induced upon cytokinin treatment
-
expression is down-regulated by cytokinin-treatment; expression is repressed upon sucrose feeding
-
expression is induced transiently by cold, salt and drought stress
-
under phosphorus deficiency, trehalose 6-phosphate phosphatase transcript is increased by about 35%
-
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D213A
-
inactive
D215A
-
inactive
D336A
-
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
D378A
-
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
DELTA59
-
the mutant shows increased catalytic efficiency compared to the wild type enzyme
E384A
-
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
E386A
-
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
K334A
-
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
N228A
-
the mutant shows increased catalytic efficiency compared to the wild type enzyme
Q332A
-
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
R337A
-
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
S329A
-
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
T339A
-
the mutant shows increased catalytic efficiency compared to the wild type enzyme
W280A
-
the mutant shows increased catalytic efficiency compared to the wild type enzyme
Y221A
-
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
Y225A
-
the mutant shows decreased catalytic efficiency compared to the wild type enzyme
additional information
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
agriculture
possible use of OsTPP1 in abiotic stress engineering of crops
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.
drug development
-
Bm-TPP bodes well as a rational drug target against lymphatic filariasis
medicine
Show AA Sequence (7190 entries)
Longer loading times are possible. Please use the Sequence Search for a specific query.