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Enzyme Nomenclature
Information on EC 3.2.1.153 - fructan beta-(2,1)-fructosidase
for references in articles please use BRENDA:EC3.2.1.153
Word Map on EC 3.2.1.153
- 3.2.1.153
-
fructans
- 1-fehs
-
winter
- wheat
- invertases
-
season
-
pichia
-
sprouting
- pastoris
- chicory
- aestivum
-
triticum
- inulin
- levan
-
cerrado
-
defoliation
- intybus
-
fructosyl
-
snow
-
inulin-type
-
cichorium
-
brazilian
-
autumn
-
1-fructosyltransferase
- herbacea
-
underground
-
iso-electric
-
2.4.1.99
-
jerusalem
-
sucrose:sucrose
-
crown
-
convincingly
-
anthesis
-
hardened
-
regrowth
- asteraceae
-
remobilization
- artichoke
-
phenological
-
helianthus
- tuberosus
-
vernonia
- diagnostics
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The enzyme appears in viruses and cellular organisms
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EC NUMBER 
COMMENTARY 
3.2.1.153
-
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RECOMMENDED NAME
GeneOntology No.
fructan beta-(2,1)-fructosidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Hydrolysis of terminal, non-reducing (2->1)-linked beta-D-fructofuranose residues in fructans
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis
hydrolysis
hydrolytic cleavage of terminal fructosyl residues off inulin
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SYSTEMATIC NAME
IUBMB Comments
beta-(2->1)-D-fructan fructohydrolase
Possesses one of the activities of EC 3.2.1.80, fructan beta-fructosidase. While the best substrates are the inulin-type fructans, such as 1-kestose [beta-D-fructofuranosyl-(2->1)-beta-D-fructofuranosyl alpha-D-glucopyranoside] and 1,1-nystose [beta-D-fructofuranosyl-(2->1)-beta-D-fructofuranosyl-(2->1)-beta-D-fructofuranosyl alpha-D-glucopyranoside], some (but not all) levan-type fructans can also be hydrolysed, but more slowly [see EC 3.2.1.154, fructan beta-(2,6)-fructosidase]. Sucrose, while being a very poor substrate, can substantially inhibit enzyme activity in some cases.
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CAS REGISTRY NUMBER
COMMENTARY
1000593-08-7
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37288-56-5
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
enzyme contains three activities that hydrolyze beta-2,6-glycosidic linkages faster than beta-2,1-glycosidic linkages and two activities hydrolyze beta-2,1-glycosidic linkages faster than beta-2,6-glycosidic linkages
-
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a cold tolerant, graminean decaploid species from the Patagonian region of Argentina, gene Bp1-FEHa
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cultivars PI 173438 (snow mold-resistant) and Valuevskaya (snow mold-susceptible), gene Wfh-sm3
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drought-resistant varieties Kauz and Westonia; varieties Kauz and Westonia
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18 months old plants, natural outdoor condition (control), excised natural conditions, excised and intact plants at 5°C for 21 days
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fragment, full-length cDNA of FEH gene of Vernonia herbacea, 2,074 bp, 582 amino acids; samples of sprouting induced plants taken at day 0 and 20, and of defoliated plants stored for one week at 5 degrees Celsius
UniProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
-
snow molds consume carbon sources contained in the inoculated wheat tissues but cannot effectively use wheat polysaccharide including fructans compared with mono- and disaccharides. Therefore, in snow mold inoculated wheat tissues, fructans are rapidly degraded, mainly by wheat enzymes, FEHs, to maintain necessary levels of mono- and disaccharides for metabolic demands under snow cover
physiological function
fructan 1-exohydrolase enzymes are involved in inulin degradation in the roots of chicory. Higher enzyme expression in cold temperatures can decrease the quality and the quantity of the inulin; fructan 1-exohydrolase enzymes are involved in inulin degradation in the roots of chicory. Higher enzyme expression in cold temperatures can decrease the quality and the quantity of the inulin; fructan 1-exohydrolase enzymes are involved in inulin degradation in the roots of chicory. Higher enzyme expression in cold temperatures can decrease the quality and the quantity of the inulin
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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
1-kestose + H2O
D-fructose
from Vernonia herbacea and Vernonia discolor, but levans from Gomphrena macrocephala and Phleum pratense are poorly hydrolyzed, hydrolytic cleavage of terminal fructosyl residues off inulin, sucrose is not hydrolyzed
-
-
?
6G,6-kestotetraose + H2O
?
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4% of the activity with 6G,1-kestotetraose
-
-
?
inulin + H2O
D-fructose
5% inulin from Vernonia herbacea and Vernonia discolor, but levans from Gomphrena macrocephala and Phleum pratense are poorly hydrolyzed, hydrolytic cleavage of terminal fructosyl residues off inulin, sucrose is not hydrolyzed
-
-
?
1,1,1-kestopentaose + H2O
D-fructose + ?
-
1.2 mM in 50 mM Na-acetate buffer, pH 5.2, 0.02% Na-azide, 60 min, 30°C
-
-
?
1,1-kestotetraose + H2O
?
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85% of the activity with 6G,1-kestotetraose
-
-
?
1,1-nystose + H2O
?
-
72% of the activity with 1-kestose, isoenzyme 1-FEH w1
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-
?
1,1-nystose + H2O
?
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83% of the activity with 1-kestose, isoenzyme 1-FEH w2
-
-
?
1-kestotriose + H2O
?
1-FEHa is a fructan exohydrolase with predominant activity towards beta-(2-1) linkages
-
-
?
1-kestotriose + H2O
?
58% of the activity with 1,1-kestotetraose
-
-
?
6-kestose + H2O
?
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0.7% of the activity with 1-kestose, isoenzyme 1-FEH w1
-
-
?
6-kestose + H2O
?
-
1% of the activity with 1-kestose, isoenzyme 1-FEH w2
-
-
?
inulin + H2O
?
-
22% of the activity with 1-kestose, isoenzyme 1-FEH w2
-
-
?
inulin + H2O
?
-
39% of the activity with 1-kestose, isoenzyme 1-FEH w1
-
-
?
inulin + H2O
fructose + fructo-oligosaccharide + fructo-polysaccharide
-
5% inulin from chicory, 30 degrees Celsius
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-
?
inulin + H2O
fructose + fructo-oligosaccharide + fructo-polysaccharide
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5% inulin from Helianthus tuberosus, McIlvaine buffer, pH 4.5, 30°C, 4 h
-
-
?
levan + H2O
?
-
3% of the activity with 1-kestose, isoenzyme 1-FEH w2
-
-
?
levan + H2O
?
-
4% of the activity with 1-kestose, isoenzyme 1-FEH w1
-
-
?
neokestose + H2O
?
-
3% of the activity with 1-kestose, isoenzyme 1-FEH w2
-
-
?
neokestose + H2O
?
-
4% of the activity with 1-kestose, isoenzyme 1-FEH w1
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
3% of the activity with 6G,1-kestotetraose
-
-
?
additional information
?
-
-
Bp1-FEHa is a fructan exohydrolase with predominant activity towards beta-2,1-linkages
-
-
-
additional information
?
-
Bp1-FEHa is a fructan exohydrolase with predominant activity towards beta-2,1-linkages
-
-
-
additional information
?
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-
the enzyme is involved in fructan breakdown
-
-
-
additional information
?
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isoform 1-FEH II is expressed when young chicory plants are defoliated, suggesting that this enzyme can be induced at any developmental stage when large energy supplies are necessary
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-
-
additional information
?
-
-
the enzyme is involved in fructan degradation
-
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-
additional information
?
-
-
the enzyme hydrolyzes the beta(2-1) linkage in inulin, 1-kestose and 1,1-nystose at rates at least 5fold faster than the beta(2-6) linkages in levan oligosaccharides and levanbiose
-
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-
additional information
?
-
-
hydrolytic cleavage of terminal fructosyl residues off inulin
-
-
-
additional information
?
-
-
the enzyme hydrolyzes terminal beta-(2-1)-fructosylfructose-linkages in linear and branched fructan oligomers. beta-(2-6)-linkages are hardly hydrolyzed
-
-
-
additional information
?
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high expression level in conditions of active fructan synthesis, low expression level when fructan contents are low. The enzyme might play a role as a beta-(2,1) trimming enzyme acting during fructan synthesis in concert with fructan synthesis enzymes
-
-
-
additional information
?
-
high expression level in conditions of active fructan synthesis, low expression level when fructan contents are low. The enzyme might play a role as a beta-(2,1) trimming enzyme acting during fructan synthesis in concert with fructan synthesis enzymes
-
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-
additional information
?
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low activity against 6-kestotriose and levan. No hydrolase activity can be detected towards sucrose
-
-
-
additional information
?
-
low activity against 6-kestotriose and levan. No hydrolase activity can be detected towards sucrose
-
-
-
additional information
?
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-
isoenzyme 1-FEH w2 might play a role as a beta-(2,1)-trimmer throughout the period of active graminan biosynthesis
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-
additional information
?
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-
isozyme Wfh-sm3m hydrolyzes beta-(2,6)-linkages of fructans (6-kestotriose) more efficiently than beta-(2,1)-linkages of fructans (1-kestotriose and 1,1-kestotetraose). On the other hand, Wfh-sm3m cannot hydrolyze long-chain fructans such as inulin and bacterial levan
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additional information
?
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wheat graminan degradation by Wfh-sm3 recombinant protein Wfh-sm3m. The recombinant protein Wfh-sm3m preferentially degrades 6-kestotriose and possesses minor hydrolase activity to 1-kestotriose and 1,1-kestotetraose, poor activity with sucrose, and no activity with inulin and levan
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-
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additional information
?
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hydrolytic cleavage of terminal fructosyl residues off inulin
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-
additional information
?
-
a set of fructan 1-exohydrolase proteins acts in two different ways during fructan mobilization: (1) by hydrolyzing fructo-oligosaccharides and -polysaccharides in sprouting plants (naturally or induced) for carbon supply and (2) by hydrolyzing preferably fructo-polysaccharides under low temperature to maintain the oligosaccharide pool for plant cold acclimation
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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
additional information
?
-
-
Bp1-FEHa is a fructan exohydrolase with predominant activity towards beta-2,1-linkages
-
-
-
additional information
?
-
D2IGW7
Bp1-FEHa is a fructan exohydrolase with predominant activity towards beta-2,1-linkages
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-
-
additional information
?
-
-
the enzyme is involved in fructan breakdown
-
-
-
additional information
?
-
-
isoform 1-FEH II is expressed when young chicory plants are defoliated, suggesting that this enzyme can be induced at any developmental stage when large energy supplies are necessary
-
-
-
additional information
?
-
-
the enzyme is involved in fructan degradation
-
-
-
additional information
?
-
-
hydrolytic cleavage of terminal fructosyl residues off inulin
-
-
-
additional information
?
-
-
high expression level in conditions of active fructan synthesis, low expression level when fructan contents are low. The enzyme might play a role as a beta-(2,1) trimming enzyme acting during fructan synthesis in concert with fructan synthesis enzymes
-
-
-
additional information
?
-
Q64GB3
high expression level in conditions of active fructan synthesis, low expression level when fructan contents are low. The enzyme might play a role as a beta-(2,1) trimming enzyme acting during fructan synthesis in concert with fructan synthesis enzymes
-
-
-
additional information
?
-
-
isoenzyme 1-FEH w2 might play a role as a beta-(2,1)-trimmer throughout the period of active graminan biosynthesis
-
-
-
additional information
?
-
-
isozyme Wfh-sm3m hydrolyzes beta-(2,6)-linkages of fructans (6-kestotriose) more efficiently than beta-(2,1)-linkages of fructans (1-kestotriose and 1,1-kestotetraose). On the other hand, Wfh-sm3m cannot hydrolyze long-chain fructans such as inulin and bacterial levan
-
-
-
additional information
?
-
-
hydrolytic cleavage of terminal fructosyl residues off inulin
-
-
-
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Sucrose
-
inhibitor for wild-type 1-FEH IIa, weak hydrolysation product in S101L mutant
Sucrose
-
inhibition by sucrose is a mechanism for controlling fructan degradation in plants
Sucrose
range 0.5-10 mM, 1 mM inhibits 1-FEH by 8%, 5 mM by about 50%, 10 mM by 81%
additional information
-
about 50% decreased enzyme activity in the first leaf section after 7 days of cold treatment, fructan accumulation profile along with cold treatment, overview
-
additional information
about 50% decreased enzyme activity in the first leaf section after 7 days of cold treatment, fructan accumulation profile along with cold treatment, overview
-
additional information
-
proteinaceous inhibitors of acid invertases (structurally related to fructan 1-exohydrolase) do not inhibit fructan 1-exohydrolase
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
1-kestose
-
5 mM substrate: wild-type enzyme about 23 mol fructose/mol enzyme, mutant about 8 mol fructose/mol enzyme
additional information
inulin
-
5 mM substrate: wild-type 1-FEH IIa 10 mol fructose/mol enzyme, S101L mutant about 2 mol fructose/mol enzyme
additional information
Sucrose
-
5 mM substrate: about zero activity in both enzyme variants, only at higher substrate concentrations (500-1000 mM) strongly raised activity: 10 mol fructose/mol enzyme
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.0122
-
of 1-FEH I with 0.0083 micomol/min/mg background activity in Nicotiana benthamiana leaves
0.0205
-
of 1-FEH IIa with 0.0083 micomol/min/mg background activity in Nicotiana benthamiana leaves
additional information
additional information
-
highest activities in proximal rhizophores, increased in low temperature and excised plants, and low temperature + excised plants, overall highest activities in low temperature + excised plant rhizophores, overall high fructan content in all treatments, higher fructo-oligosaccharide/fructo-polysaccharide ratios in low temperature treatments, chain size lowest in distal region
additional information
activity increase gradually from 1% up to 8% inulin, however solubility above 5% incomplete
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 6.5
0.05M citrate phosphate buffer, 30°C, at pH 5.5 maximal activity of more than 300 microgram fructose per mg protein and hour, at pH 4.5-5.0 about 90% activity, at pH 4.25 and 6.0 about 75% activity, at pH 4.0 and 6.5 about 60% activity
4.3 - 6.3
pH 4.3: about 60% of maximal activity, pH 6.3: about 50% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 50
at pH 5.5, maximal activity of slightly more than 400 microgram fructose per mg protein and h at 40°C, about 95% of maximal activity at 50°C, about 90% of maximal activity at 30°C, about 50% at 20°C, about 25% of maximal activity at 20°C
30 - 50
30°C: about 70% of maximal activity, 50°C: about 30% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
activity is low in growing tubers but increases during dormancy and sprouting
; meature leaves, highest Bp1-FEHa expression levels in the second section of the sheath and the tip of the blade
-
enzyme expression analysis of isozymes under different water conditions, overview
transcripts detected in proximal region of sprouting induced plant, in proximal, medium, and distal regions of sprouting induced + 5°C plants
variable levels of FEHI expression in different phenotypes of the chicory cultivars. Roots from all cultivars show different expression level after five weeks storage time, but they are not significantly different; variable levels of FEHII expression in different phenotypes of the chicory cultivars. Roots from all cultivars show different expression level after five weeks storage time, but they are not significantly different; variable levels of FEHII expression in different phenotypes of the chicory cultivars. Roots from all cultivars show different expression level after five weeks storage time, but they are not significantly different
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PDB
SCOP
CATH
UNIPROT
ORGANISM
Cichorium intybus;
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70000
-
x * 70000, isoenzyme 1-FEH w1, SDS-PAGE; x * 70000, isoenzyme 1-FEH w2, SDS-PAGE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 70000, isoenzyme 1-FEH w1, SDS-PAGE; x * 70000, isoenzyme 1-FEH w2, SDS-PAGE
monomer
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
-
glycosylation on at least two of four potential N-glycosylation sites, isoenzyme 1-FEH w1; glycosylation on at least two of four potential N-glycosylation sites, isoenzyme 1-FEH w2
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Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
hanging drop vapour diffusion method of recombinant enzyme heterologously expressed in Pichia pastoris. The structure of the isoenzyme 1-FEH IIa is determined at a resolution of 2.35 A. The structure consists of an N-terminal fivefold beta-propeller domain
-
hanging-drop vapour-diffusion method at 4°C. The crystals are tetragonal belonging to space group P4(1)2(1)2 or P4(3)2(1)2, with unit-cell parameters a = 139.83, b = 139.83, c = 181.94 A
-
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
during storage at 15°C, 1-FEH in onion bulbs is low but peaks abruptly after 12 and 16 weeks, respectively, after which it decreases to levels higher to that observed at the beginning of the storage
-
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
during storage at 15°C, 1-FEH in onion bulbs is low but peaks abruptly after 12 and 16 weeks, respectively, after which it decreases to levels higher to that observed at the beginning of the storage
-
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
leaf material frozen, ground, soluble proteins extracted, precipitated, dialyzed, cell-wall associated proteins in pellets incubated in 1 M CaCl, supernatant precipitated, dialysed
-
partial, enzyme contains three activities that hydrolyze beta-2,6-glycosidic linkages faster than beta-2,1-glycosidic linkages and two activities hydrolyze beta-2,1-glycosidic linkages faster than beta-2,6-glycosidic linkages
-
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
48 h in Nicotiana benthamiana leaves infiltrated by Agrobacterium tumefaciens C58C1 with entry vector pDONR(TM)Zeo and destination vector pMDC32
-
enzyme expression analysis of isozymes under different water conditions, overview
-
expressed in Pichia pastoris; single copy gene Bp1-FEHa, DNA and amino acid sequence determination and analysis, phylogenetic tree, functional expression in Pichia pastoris
heterologous expression in Pichia pastoris strain X-33 after culturing of plasmids in Escherichia coli, expression vector pPICZalphaA
quantitative real time PCR analysis of the FEH mRNAs (including FEHI and FEHII) in cold stored roots of three chicory cultivars, overview. Variable levels of FEHII and FEHI expression in different phenotypes of the chicory cultivars; quantitative real time PCR analysis of the FEH mRNAs (including FEHI and FEHII) in cold stored roots of three chicory cultivars, overview. Variable levels of FEHII and FEHI expression in different phenotypes of the chicory cultivars; quantitative real time PCR analysis of the FEH mRNAs (including FEHI and FEHII) in cold stored roots of three chicory cultivars, overview. Variable levels of FEHII and FEHI expression in different phenotypes of the chicory cultivars
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
expression of isozyme 1-FEH IIa is induced by cold stress (12 h at 4°C); expression of isozyme 1-FEH I is induced by cold stress (12 h at 4°C)
Q93X60;, Q9FNS9;
storage at low temperature (5°C) enhances enzyme gene expression and activity
the profile of water-soluble carbohydrate accumulation and loss is negatively correlated with the mRNA concentration of 1-FEH, especially 1-FEH w3 (1-FEH-6B)
-
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
S101L
-
neighbouring amino acid exchange influences the orientation of Trp82, thus switches the function of sucrose as inhibitor towards hydrolysation substrate, but only when present in high concentrations because substrate binding is inefficient
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
diagnostics
-
expression of 1-FEH w3 may be a good indicator to identify potential grain yield in wheat exposed to water deficits during grain filling, when linked to osmotic potential and green leaf retention
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LINKS TO OTHER DATABASES (specific for EC-Number 3.2.1.153)
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