Any feedback?
Information on EC 3.2.1.153 - fructan beta-(2,1)-fructosidase
for references in articles please use BRENDA:EC3.2.1.153Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.2.1.153 fructan beta-(2,1)-fructosidaseIUBMB Comments
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.
Specify your search results
Word Map
- 3.2.1.153
- fructans
- 1-fehs
-
winter
- inulin
- chicory
-
inulin-type
- invertases
- aestivum
-
triticum
- intybus
- levan
-
cichorium
-
fructosyl
-
2.4.1.99
-
snow
-
defoliation
-
convincingly
- 1,1-kestotetraose
-
cerrado
-
exohydrolases
-
6-exohydrolase
-
remobilization
-
anthesis
-
underground
-
iso-electric
- herbacea
-
taproot
-
vernonia
-
jerusalem
-
1-fructosyltransferase
-
sucrose:sucrose
-
phenological
- artichoke
- 1-kestotriose
-
hardened
- asteraceae
- diagnostics
The enzyme appears in viruses and cellular organisms
Synonyms
ci1-feh iia, lp1-feha, 1-feh w1, 1-feh w2, 1-fructan exohydrolase, fructan 1-exohydrolase w2, wfh-sm3m, 1-feh2a, 1-feh2b, 
more
topPlease wait a moment until the data is sorted. This message will disappear when the data is sorted.
SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
1-FEH
1-FEH I
1-FEH IIa
1-FEH w1
1-FEHa
1-fructan exohydrolase
FEH
fructan 1-exohydrolase
fructan 1-exohydrolase w1
fructan exohydrolase
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
1,1,1,1-kestohexaose + H2O = 1,1,1-kestopentaose + beta-D-fructofuranose
-
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis
hydrolysis
hydrolytic cleavage of terminal fructosyl residues off inulin
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CAS REGISTRY NUMBER
COMMENTARY
1000593-08-7
-
37288-56-5
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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 + sucrose
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
?
-
4% of the activity with 6G,1-kestotetraose
-
-
?
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
?
-
85% of the activity with 6G,1-kestotetraose
-
-
?
1,1-nystose + H2O
?
-
72% of the activity with 1-kestose, isoenzyme 1-FEH w1
-
-
?
1,1-nystose + H2O
?
-
83% of the activity with 1-kestose, isoenzyme 1-FEH w2
-
-
?
1-kestose + H2O
beta-D-fructose + sucrose
best substrate
-
-
?
1-kestotriose + H2O
?
1-FEHa is a fructan exohydrolase with predominant activity towards beta-(2-1) linkages
-
-
?
6-kestose + H2O
?
-
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
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
-
-
?
inulin + H2O
fructose + fructo-oligosaccharide + fructo-polysaccharide
-
5% inulin from chicory, 30 degrees Celsius
-
-
?
inulin + H2O
fructose + fructo-oligosaccharide + fructo-polysaccharide
-
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
?
-
-
Agave tequilana fructans are a polydisperse mixture of long degree of polymerization (DP) polymers and fructooligosaccharides (FOSs) with both b(2-1) and b(2-6) linkages. This mixture also contains highly branched agavins and graminans, and agavins are the most abundant of all. Agave tequilana fructans exhibit fluctuation of their total reducing sugar content and DP according to the plant age
-
-
?
additional information
?
-
-
hydrolysis of terminal, non-reducing 2,1-linked beta-D-fructofuranose residues in fructans
-
-
?
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
?
-
-
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
?
-
-
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
-
-
?
additional information
?
-
-
hydrolytic cleavage of terminal fructosyl residues off inulin
-
-
?
additional information
?
-
hydrolysis of Jerusalem artichoke tuber by immobilized isozyme Ci1-FEH IIa and analysis of carbohydrate profile. The fructan in the tuber is rapidly degraded to fructose by immobilized recombinant Ci1-FEH IIa. Substrate specificity, overview. No activity with sucrose and levan. Isozyme Ci1-FEH IIa has much higher activity than all other investigated FEH isozymes from Cichorium intybus and Helianthus tuberosus
-
-
?
additional information
?
-
hydrolysis of Jerusalem artichoke tuber by immobilized isozyme Ci1-FEH IIa and analysis of carbohydrate profile. The fructan in the tuber is rapidly degraded to fructose by immobilized recombinant Ci1-FEH IIa. Substrate specificity, overview. No activity with sucrose and levan. Isozyme Ci1-FEH IIa has much higher activity than all other investigated FEH isozymes from Cichorium intybus and Helianthus tuberosus
-
-
?
additional information
?
-
hydrolysis of Jerusalem artichoke tuber by immobilized isozyme Ci1-FEH IIa and analysis of carbohydrate profile. The fructan in the tuber is rapidly degraded to fructose by immobilized recombinant Ci1-FEH IIa. Substrate specificity, overview. No activity with sucrose and levan. Isozyme Ci1-FEH IIa has much higher activity than all other investigated FEH isozymes from Cichorium intybus and Helianthus tuberosus
-
-
?
additional information
?
-
-
hydrolysis of Jerusalem artichoke tuber by immobilized isozyme Ci1-FEH IIa and analysis of carbohydrate profile. The fructan in the tuber is rapidly degraded to fructose by immobilized recombinant Ci1-FEH IIa. Substrate specificity, overview. No activity with sucrose and levan. Isozyme Ci1-FEH IIa has much higher activity than all other investigated FEH isozymes from Cichorium intybus and Helianthus tuberosus
-
-
?
additional information
?
-
substrate specificity, overview. No activity with sucrose and levan
-
-
?
additional information
?
-
substrate specificity, overview. No activity with sucrose and levan
-
-
?
additional information
?
-
substrate specificity, overview. No activity with sucrose and levan
-
-
?
additional information
?
-
-
substrate specificity, overview. No activity with sucrose and levan
-
-
?
additional information
?
-
substrate specificity, overview. No activity with sucrose and levan. Isozyme Ci1-FEH I shows quite low activity compared to other FEH isozymes analyzed from Cichorium intybus and Helianthus
-
-
?
additional information
?
-
substrate specificity, overview. No activity with sucrose and levan. Isozyme Ci1-FEH I shows quite low activity compared to other FEH isozymes analyzed from Cichorium intybus and Helianthus
-
-
?
additional information
?
-
substrate specificity, overview. No activity with sucrose and levan. Isozyme Ci1-FEH I shows quite low activity compared to other FEH isozymes analyzed from Cichorium intybus and Helianthus
-
-
?
additional information
?
-
-
substrate specificity, overview. No activity with sucrose and levan. Isozyme Ci1-FEH I shows quite low activity compared to other FEH isozymes analyzed from Cichorium intybus and Helianthus
-
-
?
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
?
-
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
-
-
?
additional information
?
-
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
?
-
-
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
?
-
-
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
-
-
?
additional information
?
-
-
hydrolytic cleavage of terminal fructosyl residues off inulin
-
-
?
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
additional information
?
-
-
Agave tequilana fructans are a polydisperse mixture of long degree of polymerization (DP) polymers and fructooligosaccharides (FOSs) with both b(2-1) and b(2-6) linkages. This mixture also contains highly branched agavins and graminans, and agavins are the most abundant of all. Agave tequilana fructans exhibit fluctuation of their total reducing sugar content and DP according to the plant age
-
-
?
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
?
-
-
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
?
-
-
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
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
activity increase gradually from 1% up to 8% inulin, however solubility above 5% incomplete
additional information
-
activity increase gradually from 1% up to 8% inulin, however solubility above 5% incomplete
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.5
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 6.5
4.3 - 6.3
pH 4.3: about 60% of maximal activity, pH 6.3: about 50% of maximal activity
4 - 6.5
over 50% of maximal activity within this range
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
40
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 50
20 - 70
over 60% of maximal activity within this range
25 - 45
over 50% of maximal activity within this range
30 - 50
30°C: about 70% of maximal activity, 50°C: about 30% of maximal activity
20 - 50
over 60% of maximal activity within this range
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
-
brenda
a cold tolerant, graminean decaploid species from the Patagonian region of Argentina, gene Bp1-FEHa
-
-
brenda
subspecies Cichorium intybus foliosum, variant Zoom
SwissProt
brenda
cultivars PI 173438 (snow mold-resistant) and Valuevskaya (snow mold-susceptible), gene Wfh-sm3
-
-
brenda
isozyme fructan 1-exohydrolase w1, encoded by gene 1-FEHw1; different cultivars
UniProt
brenda
isozyme fructan 1-exohydrolase w1, encoded by gene 1-FEHw1; doubled haploid lines DH 307 and DH 338 selected from a population of 225 lines derived from a var. Westonia/Kauz cross
UniProt
brenda
18 months old plants, natural outdoor condition (control), excised natural conditions, excised and intact plants at 5°C for 21 days
-
-
brenda
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
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
activity is low in growing tubers but increases during dormancy and sprouting
brenda
additional information
meature leaves, highest Bp1-FEHa expression levels in the second section of the sheath and the tip of the blade
brenda
-
enzyme expression analysis of isozymes under different water conditions, overview
brenda
transcripts detected in proximal region of sprouting induced plant, in proximal, medium, and distal regions of sprouting induced + 5°C plants
brenda
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
brenda
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
brenda
additional information
1-FEH activities are higher in all DH 338 stem segments under drought, as compared to irrigated plants after 10 days after anthesis (DAA), although in the sheath the difference disappears during the later stages. Under drought, 1-FEH activity tends to increase in the peduncle and the penultimate internode after 14 DAA, while it remains similar between treatments in the lower parts and sheath in DH 307. The combined 1-FEH and 6-FEH activities are particularly important during the later stages in drought treated DH 338
brenda
additional information
seasonal changes in mRNA levels of FEH genes (1-FEH, 6-KEH, 6&1-FEH, 6-FEH, Wfh-sm3) in crown and leaf tissues of winter wheat sampled in the field from autumn to spring (2009/2010), overview. Transcript levels of 1-FEH w1 is constant in leaves and changes according to plant growth rate in crown tissues. The transcript levels of 1-FEH w1 both in crown and leaf tissues of the freezing-tolerant cultivars, Valuevskaya and Norstar, are higher than those of cv. PI 173438
brenda
additional information
-
seasonal changes in mRNA levels of FEH genes (1-FEH, 6-KEH, 6&1-FEH, 6-FEH, Wfh-sm3) in crown and leaf tissues of winter wheat sampled in the field from autumn to spring (2009/2010), overview. Transcript levels of 1-FEH w1 is constant in leaves and changes according to plant growth rate in crown tissues. The transcript levels of 1-FEH w1 both in crown and leaf tissues of the freezing-tolerant cultivars, Valuevskaya and Norstar, are higher than those of cv. PI 173438
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
physiological function
evolution
the enzyme belongs to the glycoside hydrolase family 32, GH32
evolution
phylogenetic analysis of deduced amino acid sequences of plant fructan metabolism genes
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
metabolism
in chicory hairy root cultures, transcription factor CiMYB5 displays co-expression with its target genes in response to different abiotic stress and phytohormone treatments, whereas correlations with CiMYB3 expression are less consistent. Oligofructan levels indicate that the metabolic response, while depending on the balance of the relative expression levels of fructan exohydrolases and fructosyltransferases, can be also affected by differential subcellular localization of different FEH isoforms. In chicory hairy root cultures CiMYB5 and CiMYB3 act as positive regulators of the fructan degradation pathway
metabolism
model for fructan and primary carbohydrate metabolism in sink cells of perennial ryegrass, overview
metabolism
-
proposed model for the biosynthesis of fructooligosaccharides (FOSs) in Agave tequilana Weber Blue variety, overview
metabolism
regulation of the expression of FEH genes is a crucial factor for overwintering ability of fructan-accumulating cereals and grasses. The coordinated expression of FEH genes in wheat is related to the regulation of water-soluble carbohydrate accumulation from autumn to early winter and fructan consumption under snow cover as well as energy supply. Wheat FEHs also play an important role in the varietal difference in freezing tolerance and snow mold resistance. Cooperative expression of 6-FEH and 1-FEH genes might be related to the seasonal changes and varietal difference in mono- and disaccharide contents
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
physiological function
1-FEH activities are higher in all DH 338 stem segments under drought, as compared to irrigated plants after 10 days after anthesis (DAA), although in the sheath the difference disappears during the later stages. Under drought, 1-FEH activity tends to increase in the peduncle and the penultimate internode after 14 DAA, while it remains similar between treatments in the lower parts and sheath in DH 307. The combined 1-FEH and 6-FEH activities are particularly important during the later stages in drought treated DH 338. FEH dynamics under drought may play a more essential role in var. DH 307 than in var. DH 338
physiological function
fructan exohydrolase, FEH, gene plays a key role in fructan metabolism associated with wintering ability, especially for snow mold resistance. Gene 1-FEH w1 is thought to code a trimming enzyme
physiological function
-
fructan metabolism in Agave tequilana exhibits changes in fructan content, type, degree of polymerization (DP), and molecular structure, overview. Analysis of the specific activities of involved vacuolar fructan active enzymes (FAZY) in Agave tequilana plants of different age and the biosynthesis of fructooligosaccharides (FOSs). Fructan hydrolysis is carried out by FEH enzymes, that remove terminal fructosyl units from fructan chains, to fulfill a diverse set of functions in the plant, such as energy supply during plant growth, maintenance of the osmotic pressure in the vacuoles, and modulation of the oligofructans amounts under oxidative stress and freezing tolerance
physiological function
fructans are polymers of fructose and one of the main constituents of water-soluble carbohydrates in forage grasses and cereal crops of temperate climates. Fructans are involved in cold and drought resistance, regrowth following defoliation and early spring growth, seed filling, they have beneficial effects on human health and are used for industrial processes. Fructan metabolism is under the control of both synthesis by fructosyltransferases (FTs)and breakdown through fructan exohydrolases (FEHs). The accumulation of fructans can be triggered by high sucrose levels and abiotic stress conditions such as drought and cold stress. The activities of enzymes involved in fructan synthesis and breakdown, the expression levels for the corresponding genes and levels for water-soluble carbohydrates are determined following pulse treatments with abscisic acid (ABA), auxin (AUX), ethylene (ET), gibberellic acid (GA), or kinetin (KIN)
physiological function
in hairy root cultures with induced fructan accumulation, co-expression of transcription factor CiMYB5 and FEH genes is correlated with changes in oligofructan profiles upon stress and hormone treatments
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). 1FEH_LEYCH
600
1
67194
Swiss-Prot
Secretory Pathway (Reliability: 1)
1FEH_TRIUA
597
1
66677
Swiss-Prot
Secretory Pathway (Reliability: 1)
1FEH1_WHEAT
597
1
66645
Swiss-Prot
Secretory Pathway (Reliability: 1)
1FEH2_WHEAT
596
1
66603
Swiss-Prot
Secretory Pathway (Reliability: 1)
1FEH3_WHEAT
596
1
66296
Swiss-Prot
Secretory Pathway (Reliability: 1)
1FEH_AEGSP
595
1
66492
Swiss-Prot
Secretory Pathway (Reliability: 1)
1FEH_AEGTA
596
1
66505
Swiss-Prot
Secretory Pathway (Reliability: 1)
1FEH_BROPI
602
0
67078
Swiss-Prot
Secretory Pathway (Reliability: 4)
1FEH_HORVU
599
1
66628
Swiss-Prot
Secretory Pathway (Reliability: 1)
A0A2G9H6T1_9LAMI
524
1
59763
TrEMBL
Secretory Pathway (Reliability: 1)
Q9FNS9_CICIN
568
0
63981
TrEMBL
other Location (Reliability: 2)
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PDB
SCOP
CATH
UNIPROT
ORGANISM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70000
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
glycoprotein
-
glycosylation on at least two of four potential N-glycosylation sites, isoenzyme 1-FEH w1
glycoprotein
-
glycosylation on at least two of four potential N-glycosylation sites, isoenzyme 1-FEH w2
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
PROTEIN VARIANTS
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
additional information
additional information
immobilization of purified recombinant isozyme Ci1-FEH IIa
additional information
immobilization of purified recombinant isozyme Ci1-FEH IIa
additional information
immobilization of purified recombinant isozyme Ci1-FEH IIa
additional information
-
immobilization of purified recombinant isozyme Ci1-FEH IIa
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
recombinant His-tagged enzyme from Pichia pastoris strain X-33 by nickel affinity chromatography and ultrafiltration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
-
gene 1-FEH1, cloning from var. Zoom, cloning of transcription factors and target gene promoters using Phusion DNA polymerase, yeast-one-hybrid analysis, transcript levels for CiMYB1, CiMYB3, CiMYB4, and CiMYBa are strongly upregulated, being coinduced with 1-FEH1 and 1-FEH2, overview
gene 1-FEH2a, cloning from var. Zoom, cloning of transcription factors and target gene promoters using Phusion DNA polymerase, yeast-one-hybrid analysis, transcript levels for CiMYB1, CiMYB3, CiMYB4, and CiMYBa are strongly upregulated, being coinduced with 1-FEH1 and 1-FEH2, overview
gene 1-FEH2b, cloning from var. Zoom, cloning of transcription factors and target gene promoters using Phusion DNA polymerase, yeast-one-hybrid analysis, transcript levels for CiMYB1, CiMYB3, CiMYB4, and CiMYBa are strongly upregulated, being coinduced with 1-FEH1 and 1-FEH2, overview
gene FEH-I, FEH isozyme sequences comparisons, phylogenetic analysis, recombinant expression of His-tagged enzyme in Pichia pastoris strain X-33
gene FEH-IIa, FEH isozyme sequences comparisons, phylogenetic analysis, recombinant expression of His-tagged enzyme in Pichia pastoris strain X-33
gene FEH-IIb, FEH isozyme sequences comparisons, phylogenetic analysis, recombinant expression of His-tagged enzyme in Pichia pastoris strain X-33
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
single copy gene Bp1-FEHa, DNA and amino acid sequence determination and analysis, phylogenetic tree, functional expression in Pichia pastoris
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
CiMYB3 and CiMYB5 selectively enhance promoter activities of 1-FEH1, 1-FEH2a, and 1-FEH2b genes, without affecting promoter activities of fructosyltransferase genes. Both factors recognize the MYB-core motifs (C/TNGTTA/G) that are abundantly present in 1-FEH promoters. In chicory hairy root cultures CiMYB5 and CiMYB3 act as positive regulators of the fructan degradation pathway. Expression of 1-FEH1 is potently induced by abscisic acid, iodoacetic acid, and jasmonic acid. Cold exposure caused a substantial upregulation of transcript levels of 1-FEH1 across different plant organs
CiMYB3 and CiMYB5 selectively enhance promoter activities of 1-FEH1, 1-FEH2a, and 1-FEH2b genes, without affecting promoter activities of fructosyltransferase genes. Both factors recognize the MYB-core motifs (C/TNGTTA/G) that are abundantly present in 1-FEH promoters. In chicory hairy root cultures CiMYB5 and CiMYB3 act as positive regulators of the fructan degradation pathway. Expression of 1-FEH2a is slightly induced by abscisic acid and iodoacetic acid, and more potently induced by jasmonic acid. Cold exposure causes a substantial upregulation of transcript levels of 1-FEH1 across different plant organs
CiMYB3 and CiMYB5 selectively enhance promoter activities of 1-FEH1, 1-FEH2a, and 1-FEH2b genes, without affecting promoter activities of fructosyltransferase genes. Both factors recognize the MYB-core motifs (C/TNGTTA/G) that are abundantly present in 1-FEH promoters. In chicory hairy root cultures CiMYB5 and CiMYB3 act as positive regulators of the fructan degradation pathway. Expression of 1-FEH2b is slightly induced by abscisic acid and iodoacetic acid, and more potently induced by jasmonic acid. Cold exposure causes a substantial upregulation of transcript levels of 1-FEH1 across different plant organs
expression of FEHs following phytohormone treatments, overview. Expression levels of the enzymes involved in fructan breakdown, are determined following pulse treatments with abscisic acid (ABA), auxin (AUX), ethylene (ET), gibberellic acid (GA), or kinetin (KIN) reveals a minor is effect evident for 1-FEH activity with an increased activity in response to KIN and a decrease by GA. LpFEH expression levels are increased 48 h following ET treatment, but this increase is significant only for Lp6-FEH
expression of isozyme 1-FEH I is induced by cold stress (12 h at 4°C)
expression of isozyme 1-FEH IIa is induced by cold stress (12 h at 4°C)
several R2R3-MYB transcriptional regulators are analysed for their possible involvement in 1-FEH regulation via transient transactivation of 1-FEH target promoters and for in vivo co-expression with target genes under different stress and hormone treatments, overview
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)
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Henson, C.A.; Livingston III, D.P.
Characterization of a fructan exohydrolase purified from barley stems that hydrolyzes multiple fructofuranosidic linkages
Plant Physiol. Biochem.
36
715-720
1998
Hordeum vulgare
-
brenda
De Roover, J.; Van Laere, A.; De Winter, M.; Timmermanns, J.W.; Van den Ende, W.
Purification and properties of a second fructan exohydrolase from the roots of Chicorium intybus
Physiol. Plant.
106
28-34
1999
Cichorium intybus
-
brenda
Verhaest, M.; Van den Ende, W.; Yoshida, M.; Le Roy, K.; Peeraer, Y.; Sansen, S.; De Ranter, C.J.; Van Laere, A.; Rabijns, A.
Crystallization and preliminary X-ray diffraction study of fructan 1-exohydrolase IIa from Cichorium intybus
Acta Crystallogr. Sect. D
60
553-554
2004
Cichorium intybus
brenda
Van den Ende, W.; Michiels, A.; Van Wonterghem, D.; Clerens, S.P.; De Roover, J.; Van Laere, A.J.
Defoliation induces fructan 1-exohydrolase II in witloof chicory roots. Cloning and purification of two isoforms, fructan 1-exohydrolase IIa and fructan 1-exohydrolase IIb. Mass fingerprint of the fructan 1-exohydrolase II enzymes
Plant Physiol.
126
1186-1195
2001
Cichorium intybus
brenda
Van Den Ende, W.; Clerens, S.; Vergauwen, R.; Van Riet, L.; Van Laere, A.; Yoshida, M.; Kawakami, A.
Fructan 1-exohydrolases. beta-(2,1)-trimmers during graminan biosynthesis in stems of wheat? Purification, characterization, mass mapping, and cloning of two fructan 1-exohydrolase isoforms
Plant Physiol.
131
621-631
2003
Triticum aestivum
brenda
Bonnett, G.D.; Simpson, R.J.
Fructan exohydrolase activities from Lolium rigidum that hydrolyze ??2, 1? and ??2, 6?glycosidic linkages at different rates
New Phytol.
131
199-209
1995
Lolium rigidum
brenda
Marx, S.P.; Nosberger, J.; Frehner, M.
Seasonal variation of fructan-beta-fructosidase (FEH) activity and characterization of a beta-(2-1)-linkage specific FEH from tubers of Jerusalem artichoke (Helianthus tuberosus)
New Phytol.
135
267-277
1997
Helianthus tuberosus
brenda
Verhaest, M.; Ende, W.V.; Roy, K.L.; De Ranter, C.J.; Laere, A.V.; Rabijns, A.
X-ray diffraction structure of a plant glycosyl hydrolase family 32 protein: fructan 1-exohydrolase IIa of Cichorium intybus
Plant J.
41
400-411
2005
Cichorium intybus
brenda
Benkeblia, N.; Ueno, K.; Onodera, S.; Shiomi, N.
Variation of fructooligosaccharides and their metabolizing enzymes in onion bulb (Allium cepa L. cv. Tenshin) during long-term storage
J. Food Sci.
70
S208-S214
2005
Allium cepa
brenda
Lothier, J.; Lasseur, B.; Le Roy, K.; Van Laere, A.; Prudhomme, M.P.; Barre, P.; Van den Ende, W.; Morvan-Bertrand, A.
Cloning, gene mapping, and functional analysis of a fructan 1-exohydrolase (1-FEH) from Lolium perenne implicated in fructan synthesis rather than in fructan mobilization
J. Exp. Bot.
58
1969-1983
2007
Lolium perenne (Q64GB3), Lolium perenne
brenda
Le Roy, K.; Lammens, W.; Van Laere, A.; Van den Ende, W.
Influencing the binding configuration of sucrose in the active sites of chicory fructan 1-exohydrolase and sugar beet fructan 6-exohydrolase
New Phytol.
178
572-580
2008
Cichorium intybus
brenda
Portes, M.T.; Figueiredo-Ribeiro, R.d.e..C.; de Carvalho, M.A.
Low temperature and defoliation affect fructan-metabolizing enzymes in different regions of the rhizophores of Vernonia herbacea
J. Plant Physiol.
165
1572-1581
2008
Vernonia herbacea
brenda
Kusch, U.; Harms, K.; Rausch, T.; Greiner, S.
Inhibitors of plant invertases do not affect the structurally related enzymes of fructan metabolism
New Phytol.
181
601-612
2009
Cichorium intybus
brenda
Asega, A.F.; do Nascimento, J.R.; Schroeven, L.; Van den Ende, W.; Carvalho, M.A.
Cloning, characterization and functional analysis of a 1-FEH cDNA from Vernonia herbacea (Vell.) Rusby
Plant Cell Physiol.
49
1185-1195
2008
Vernonia herbacea (A9JIF3), Vernonia herbacea
brenda
Zhang, J.; Dell, B.; Conocono, E.; Waters, I.; Setter, T.; Appels, R.
Water deficits in wheat: Fructan exohydrolase (1-FEH) mRNA expression and relationship to soluble carbohydrate concentrations in two varieties
New Phytol.
181
843-850
2009
Triticum aestivum
brenda
Kusch, U.; Greiner, S.; Steininger, H.; Meyer, A.D.; Corbiere-Divialle, H.; Harms, K.; Rausch, T.
Dissecting the regulation of fructan metabolism in chicory (Cichorium intybus) hairy roots
New Phytol.
184
127-140
2009
Cichorium intybus (Q93X60), Cichorium intybus (Q9FNS9)
brenda
Del Viso, F.; Puebla, A.; Hopp, H.; Heinz, R.
Cloning and functional characterization of a fructan 1-exohydrolase (1-FEH) in the cold tolerant Patagonian species Bromus pictus
Planta
231
13-25
2009
Bromus pictus, Bromus pictus (D2IGW7)
brenda
Asega, A.F.; do Nascimento, J.R.; Carvalho, M.A.
Increased expression of fructan 1-exohydrolase in rhizophores of Vernonia herbacea during sprouting and exposure to low temperature
J. Plant Physiol.
168
558-565
2011
Vernonia herbacea (A9JIF3)
brenda
Kawakami, A.; Yoshida, M.
Graminan breakdown by fructan exohydrolase induced in winter wheat inoculated with snow mold
J. Plant Physiol.
169
294-302
2012
Triticum aestivum
brenda
Maroufi, A.; Van Bockstaele, E.; De Loose, M.
Differential expression of fructan 1-exohydrolase genes involved in inulin biodegradation in chicory (Cichorium intybus) cultivars
Aust. J. Crop Sci.
6
1362-1368
2012
Cichorium intybus (Q93X60), Cichorium intybus (Q9FNS9), Cichorium intybus (V9LTH3)
-
brenda
Gasperl, A.; Morvan-Bertrand, A.; Prudhomme, M.P.; van der Graaff, E.; Roitsch, T.
Exogenous classic phytohormones have limited regulatory effects on fructan and primary carbohydrate metabolism in perennial ryegrass (Lolium perenne L.)
Front. Plant Sci.
6
1251
2015
Lolium perenne (Q108T5)
brenda
Zhang, J.; Chen, W.; Dell, B.; Vergauwen, R.; Zhang, X.; Mayer, J.E.; Van den Ende, W.
Wheat genotypic variation in dynamic fluxes of WSC components in different stem segments under drought during grain filling
Front. Plant Sci.
6
624
2015
Triticum aestivum (Q84PN8)
brenda
Zhan, W.; Jin, L.; Jiao, J.; Zhang, X.; Zhang, Y.; Zhao, H.; Liang, M.
Expression and purification of plant fructan exohydrolases and their potential applications in fructose production
Int. J. Biol. Macromol.
108
9-17
2018
Cichorium intybus (Q93X59), Cichorium intybus (Q93X60), Cichorium intybus (Q9FNS9), Cichorium intybus
brenda
Wei, H.; Zhao, H.; Su, T.; Bausewein, A.; Greiner, S.; Harms, K.; Rausch, T.
Chicory R2R3-MYB transcription factors CiMYB5 and CiMYB3 regulate fructan 1-exohydrolase expression in response to abiotic stress and hormonal cues
J. Exp. Bot.
68
4323-4338
2017
Cichorium intybus (Q93X59), Cichorium intybus (Q93X60), Cichorium intybus (Q9FNS9), Cichorium intybus
brenda
Meguro-Maoka, A.; Yoshida, M.
Analysis of seasonal expression levels of wheat fructan exohydrolase (FEH) genes regulating fructan metabolism involved in wintering ability
J. Plant Physiol.
191
54-62
2016
Triticum aestivum (Q84PN8), Triticum aestivum
brenda
Mellado-Mojica, E.; Gonzalez de la Vara, L.E.; Lopez, M.G.
Fructan active enzymes (FAZY) activities and biosynthesis of fructooligosaccharides in the vacuoles of Agave tequilana c variety plants of different age
Planta
245
265-281
2017
Agave tequilana
brenda
Select items on the left to see more content.
EXTERNAL LINKS (specific for EC-Number 3.2.1.153)
html completed
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
About BRENDA
Social media
Help
Survey
Download
Contribution
Legal
Curated at
Member of
