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Information on EC 2.4.1.243 - 6G-fructosyltransferase and Organism(s) Allium cepa and UniProt Accession P92916

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     2 Transferases
         2.4 Glycosyltransferases
             2.4.1 Hexosyltransferases
                2.4.1.243 6G-fructosyltransferase
IUBMB Comments
Inulins are polysaccharides consisting of linear or branched D-fructofuranosyl chains attached to the fructosyl residue of sucrose by a beta(2->1) linkage. This enzyme catalyses the transfer of the terminal (2->1)-linked -D-fructosyl group of an inulin chain onto O-6 position of the glucose residue of another inulin molecule . For example, if 1-kestose [1F-(beta-D-fructofuranosyl)sucrose] is both the donor and recipient in the reaction shown above, i.e., if m = 1 and n = 1, then the products will be sucrose and 6G-di-beta-D-fructofuranosylsucrose. In this notation, the superscripts F and G are used to specify whether the fructose or glucose residue of the sucrose carries the substituent. Alternatively, this may be indicated by the presence and/or absence of primes (see {iupac/2carb/36#362::http://www.chem.qmul.ac.uk/iupac/2carb/36.html#362}). Sucrose cannot be a donor substrate in the reaction (i.e. m cannot be zero) and inulin cannot act as an acceptor. Side reactions catalysed are transfer of a beta-D-fructosyl group between compounds of the structure 1F-(1-beta-D-fructofuranosyl)m-6G-(1-beta-D-fructofuranosyl)n sucrose, where m >= 0 and n = 1 for the donor, and m >= 0 and n >= 0 for the acceptor.
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Allium cepa
UNIPROT: P92916
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The taxonomic range for the selected organisms is: Allium cepa
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Synonyms
6g-fft, fructan:fructan 6g-fructosyltransferase, 6g-fructosyltransferase, fructan-fructan 6g-fructosyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6(G)-fructosyltransferase/2,1-fructan:2,1-fructan 1-fructosyltransferase
bifunctional enzyme
fructan:fructan 6G-fructosyltransferase
-
6G-FFT
-
-
SYSTEMATIC NAME
IUBMB Comments
1F-oligo[beta-D-fructofuranosyl-(2->1)-]sucrose 6G-beta-D-fructotransferase
Inulins are polysaccharides consisting of linear or branched D-fructofuranosyl chains attached to the fructosyl residue of sucrose by a beta(2->1) linkage. This enzyme catalyses the transfer of the terminal (2->1)-linked -D-fructosyl group of an inulin chain onto O-6 position of the glucose residue of another inulin molecule [1]. For example, if 1-kestose [1F-(beta-D-fructofuranosyl)sucrose] is both the donor and recipient in the reaction shown above, i.e., if m = 1 and n = 1, then the products will be sucrose and 6G-di-beta-D-fructofuranosylsucrose. In this notation, the superscripts F and G are used to specify whether the fructose or glucose residue of the sucrose carries the substituent. Alternatively, this may be indicated by the presence and/or absence of primes (see {iupac/2carb/36#362::http://www.chem.qmul.ac.uk/iupac/2carb/36.html#362}). Sucrose cannot be a donor substrate in the reaction (i.e. m cannot be zero) and inulin cannot act as an acceptor. Side reactions catalysed are transfer of a beta-D-fructosyl group between compounds of the structure 1F-(1-beta-D-fructofuranosyl)m-6G-(1-beta-D-fructofuranosyl)n sucrose, where m >= 0 and n = 1 for the donor, and m >= 0 and n >= 0 for the acceptor.
CAS REGISTRY NUMBER
COMMENTARY hide
79633-28-6
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
1-kestose + 3 sucrose
3 neokestose + H2O
show the reaction diagram
1-kestose + sucrose
1,1-kestotetraose + 1G-kestotetraose + 6G-kestotetraose
show the reaction diagram
-
-
prolonged incubation produces a complex fructan series with a higher degree of polymerization
-
?
1F(1-beta-D-fructofuranosyl)2 sucrose + sucrose
1F,6G-di-beta-D-fructofuranosylsucrose + ?
show the reaction diagram
-
i.e. nystose
-
-
?
1F(1-beta-D-fructofuranosyl)3 sucrose + sucrose
1F,6G-di-beta-D-fructofuranosylsucrose + ?
show the reaction diagram
-
i.e. fructosyl nystose
-
-
?
1F(1-beta-D-fructofuranosyl)sucrose + sucrose
1F,6G-di-beta-D-fructofuranosylsucrose + ?
show the reaction diagram
-
i.e. 1-kestose
-
-
?
neokestose + sucrose
1F,6G-di-beta-D-fructofuranosylsucrose + ?
show the reaction diagram
-
-
-
-
?
sucrose + sucrose
1F,6G-di-beta-D-fructofuranosylsucrose + ?
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
plays an important role in the synthesis of inulin and inulinneo-series fructo-oligosaccharides
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
plays an important role in the synthesis of inulin and inulinneo-series fructo-oligosaccharides
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ag+
-
1 mM, no residual activity
Hg2+
-
1 mM, no residual activity
p-chloromercuribenzoate
-
0.1 mM, 2.5% residual activity
Sodium dodecyl sulfate
-
1 mM, 48% residual activity
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
sodium deoxycholate
-
1 mM, 209% of initial activity
Triton X-100
-
1 mM, 160% of initial activity
Tween-80
-
1mM, 171% of initial activity
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
310
1F(1-beta-D-fructofuranosyl)2 sucrose
-
pH 5.7, 30°C
88
1F(1-beta-D-fructofuranosyl)sucrose
-
pH 5.7, 30°C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
26.54
-
pH 5.68, 30°C
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.4 - 6.3
-
more than 80% of maximum activity within this range
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
induction by light
Manually annotated by BRENDA team
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GFT_ALLCE
612
1
68631
Swiss-Prot
Mitochondrion (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25000
-
x * 52000, x * 25000, SDS-PAGE
52000
-
x * 52000, x * 25000, SDS-PAGE
66000
-
gel filtration
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 52000, x * 25000, SDS-PAGE
additional information
-
N-terminal amino acid sequence of 52000 Da polypeptide and of 25000 Da polypeptide
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
N84A
preferred addition of fructose to a terminal fructose instead of terminal glucose, producing inulin-type fructans
N84A/S87N
prefers synthesis of beta(2-1) linkages
N84G
no enzymic activity
N84Q
preferred addition of fructose to a terminal fructose instead of terminal glucose, producing inulin-type fructans
N84S
preferred addition of fructose to a terminal fructose instead of terminal glucose, producing inulin-type fructans
N84Y
no enzymic activity
S87D
no change in substrate or product specificity
additional information
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.3 - 6.3
-
30°C, stable for 30 min
660021
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
20 - 40
-
stable for at least 15 min
50
-
inactivation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Lolium perenne genotypes N2 and F6
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Benkeblia, N.; Onodera, S.; Shiomi, N.
Effect of temperature and storage time on fructosyltransferase activities (1-FFT and 6G-FFT) in onion bulb tissues
Acta Agric. Scand. Sect. B
53
211-214
2003
Allium cepa
-
Manually annotated by BRENDA team
Fujishima, M.; Sakai, H.; Ueno, K.; Takahashi, N.; Onodera, S.; Benkeblia, N.; Shiomi, N.
Purification and characterization of a fructosyltransferase from onion bulbs and its key role in the synthesis of fructo-oligosaccharides in vivo
New Phytol.
165
513-524
2005
Allium cepa
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Ritsema, T.; Joling, J.; Smeekens, S.
Patterns of fructan synthesized by onion fructan:fructan 6G-fructosyltransferase expressed in tobacco BY2 cells. Is fructan:fructan 1-fructosyltransferase needed in onion?
New Phytol.
160
61-67
2003
Allium cepa
Manually annotated by BRENDA team
Vijn, I.; van Dijken, A.; Sprenger, N.; van Dun, K.; Weisbeek, P.; Wiemken, A.; Smeekens, S.
Fructan of the inulin neoseries is synthesized in transgenic chicory plants (Cichorium intybus L.) harbouring onion (Allium cepa L.) fructan:fructan 6G-fructosyltransferase
Plant J.
11
387-398
1997
Allium cepa (P92916), Allium cepa
Manually annotated by BRENDA team
Ritsema, T.; Verhaar, A.; Vijin, I.; Smeekens, S.
Fructosyltransferase mutants specify a function for the beta-fructosidase motif of the sucrose-binding box in specifying the fructan type synthesized
Plant Mol. Biol.
54
853-863
2004
Allium cepa (P92916), Allium cepa
Manually annotated by BRENDA team
Ritsema, T.; Verhaar, A.; Vijn, I.; Smeekens, S.
Using natural variation to investigate the function of individual amino acids in the sucrose-binding box of fructan:fructan 6G-fructosyltransferase (6G-FFT) in product formation
Plant Mol. Biol.
58
597-607
2005
Allium cepa (P92916), Allium cepa
Manually annotated by BRENDA team
Gadegaard, G.; Didion, T.; Folling, M.; Storgaard, M.; Andersen, C.H.; Nielsen, K.K.
Improved fructan accumulation in perennial ryegrass transformed with the onion fructosyltransferase genes 1-SST and 6G-FFT
J. Plant Physiol.
165
1214-1225
2008
Allium cepa (P92916), Allium cepa
Manually annotated by BRENDA team