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1,1,1-kestopentaose + H2O
?
1,1,1-kestopentaose + H2O
D-fructose + ?
1,1-kestotetraose + H2O
?
1-kestose + H2O
beta-D-fructose + sucrose
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
-
-
?
1G-kestotetraose + H2O
?
-
96% of the activity with 6G,1-kestotetraose
-
-
?
6G,1-kestotetraose + H2O
?
-
-
-
-
?
6G,6-kestotetraose + H2O
?
-
4% of the activity with 6G,1-kestotetraose
-
-
?
6G-kestotetraose + H2O
?
-
-
-
-
?
6G-kestotriose + H2O
?
-
5% of the activity with 6G,1-kestotetraose
-
-
?
fructan + H2O
D-fructose + ?
-
Agave tequilana fructans
-
-
?
fructofuranosylnystose + H2O
?
inulin + H2O
D-fructose + ?
inulin + H2O
fructose + ?
inulin + H2O
fructose + fructo-oligosaccharide + fructo-polysaccharide
sucrose + H2O
D-fructose + D-glucose
wheat graminan + H2O
?
-
-
-
-
?
additional information
?
-
1,1,1-kestopentaose + H2O
?
-
-
-
-
?
1,1,1-kestopentaose + H2O
?
-
-
-
-
?
1,1,1-kestopentaose + H2O
D-fructose + ?
-
-
-
?
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
?
-
-
-
-
?
1,1-kestotetraose + H2O
?
-
85% of the activity with 6G,1-kestotetraose
-
-
?
1,1-kestotetraose + H2O
?
-
-
-
?
1,1-kestotetraose + H2O
?
-
-
-
-
?
1,1-nystose + H2O
?
-
-
-
-
?
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
?
-
-
-
-
?
1-kestose + H2O
?
-
-
-
-
?
1-kestose + H2O
beta-D-fructose + sucrose
-
-
-
?
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
-
-
?
1-kestotriose + H2O
?
-
88% of the activity with 6G,1-kestotetraose
-
-
?
1-kestotriose + H2O
?
58% of the activity with 1,1-kestotetraose
-
-
?
1-kestotriose + H2O
?
-
-
-
-
?
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
-
-
?
6-kestotriose + H2O
?
lower activity compared to 1-kestotriose
-
-
?
6-kestotriose + H2O
?
-
-
-
-
?
fructofuranosylnystose + H2O
?
-
-
-
?
fructofuranosylnystose + H2O
?
best substrate
-
-
?
fructofuranosylnystose + H2O
?
high activity
-
-
?
inulin + H2O
?
best substrate
-
-
?
inulin + H2O
?
high activity
-
-
?
inulin + H2O
?
24 of the activity with 1,1-kestotetraose
-
-
?
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 + ?
-
-
-
-
?
inulin + H2O
D-fructose + ?
-
-
-
?
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 + ?
-
-
-
-
?
inulin + H2O
fructose + ?
-
multichain mechanism
-
-
?
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
-
-
?
nystose + H2O
?
-
-
-
?
nystose + H2O
?
best substrate
-
-
?
nystose + H2O
?
high activity
-
-
?
sucrose + H2O
D-fructose + D-glucose
-
-
-
-
?
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
-
-
?
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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
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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
expression in Pichia pastoris
fructan 1-exohydrolase IIa and fructan 1-exohydrolase IIb
-
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 1-FEHa, quantitative RT-PCR expression analysis
gene FEH-1, real-time PCR quantitative expression analysis
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
gene Wfh-sm3, recombinant expression in Pichia pastoris
-
heterologous expression in Pichia pastoris strain X-33 after culturing of plasmids in Escherichia coli, expression vector pPICZalphaA
heterologous expression in Pichia pastoris, pPICZalphaA vector
-
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
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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 1-FEH1 is reduced by zeatin
expression of 1-FEH2a is reduced by zeatin
expression of 1-FEH2b is reduced by zeatin
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)
-
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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
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Agave tequilana
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