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* Residue conservation analysis
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Enzyme class:
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E.C.3.2.1.80
- Fructan beta-fructosidase.
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Pathway:
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Fructosidase
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Reaction:
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Hydrolysis of terminal, non-reducing 2,1- and 2,6-linked beta-D-fructofuranose residues in fructans.
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Gene Ontology (GO) functional annotation
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Biological process
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metabolic process
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2 terms
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Biochemical function
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hydrolase activity
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4 terms
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DOI no:
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New Phytol
174:90
(2007)
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PubMed id:
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Insights into the fine architecture of the active site of chicory fructan 1-exohydrolase: 1-kestose as substrate vs sucrose as inhibitor.
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M.Verhaest,
W.Lammens,
K.Le Roy,
C.J.De Ranter,
A.Van Laere,
A.Rabijns,
W.Van den Ende.
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ABSTRACT
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* Invertases and fructan exohydrolases (FEHs) fulfil important physiological
functions in plants. Sucrose is the typical substrate for invertases and
bacterial levansucrases but not for plant FEHs, which are usually inhibited by
sucrose. * Here we report on complexes between chicory (Cichorium intybus) 1-FEH
IIa with the substrate 1-kestose and the inhibitors sucrose, fructose and 2,5
dideoxy-2,5-imino-D-mannitol. Comparisons with other family GH32 and 68
enzyme-substrate complexes revealed that sucrose can bind as a substrate
(invertase/levansucrase) or as an inhibitor (1-FEH IIa). * Sucrose acts as
inhibitor because the O2 of the glucose moiety forms an H-linkage with the
acid-base catalyst E201, inhibiting catalysis. By contrast, the homologous O3 of
the internal fructose in the substrate 1-kestose forms an intramolecular
H-linkage and does not interfere with the catalytic process. Mutagenesis showed
that W82 and S101 are important for binding sucrose as inhibitor. * The
physiological implications of the essential differences in the active sites of
FEHs and invertases/levansucrases are discussed. Sucrose-inhibited FEHs show a
K(i) (inhibition constant) well below physiological sucrose concentrations and
could be rapidly activated under carbon deprivation.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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A.Bujacz,
M.Jedrzejczak-Krzepkowska,
S.Bielecki,
I.Redzynia,
and
G.Bujacz
(2011).
Crystal structures of the apo form of β-fructofuranosidase from Bifidobacterium longum and its complex with fructose.
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FEBS J, 278,
1728-1744.
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PDB codes:
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D.Altenbach,
E.Rudiño-Pinera,
C.Olvera,
T.Boller,
A.Wiemken,
and
T.Ritsema
(2009).
An acceptor-substrate binding site determining glycosyl transfer emerges from mutant analysis of a plant vacuolar invertase and a fructosyltransferase.
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Plant Mol Biol, 69,
47-56.
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D.P.Livingston,
D.K.Hincha,
and
A.G.Heyer
(2009).
Fructan and its relationship to abiotic stress tolerance in plants.
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Cell Mol Life Sci, 66,
2007-2023.
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L.Schroeven,
W.Lammens,
A.Kawakami,
M.Yoshida,
A.Van Laere,
and
W.Van den Ende
(2009).
Creating S-type characteristics in the F-type enzyme fructan:fructan 1-fructosyltransferase of Triticum aestivum L.
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J Exp Bot, 60,
3687-3696.
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U.Kusch,
S.Greiner,
H.Steininger,
A.D.Meyer,
H.Corbière-Divialle,
K.Harms,
and
T.Rausch
(2009).
Dissecting the regulation of fructan metabolism in chicory (Cichorium intybus) hairy roots.
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New Phytol, 184,
127-140.
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W.Lammens,
K.Le Roy,
L.Schroeven,
A.Van Laere,
A.Rabijns,
and
W.Van den Ende
(2009).
Structural insights into glycoside hydrolase family 32 and 68 enzymes: functional implications.
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J Exp Bot, 60,
727-740.
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W.Van den Ende,
W.Lammens,
A.Van Laere,
L.Schroeven,
and
K.Le Roy
(2009).
Donor and acceptor substrate selectivity among plant glycoside hydrolase family 32 enzymes.
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FEBS J, 276,
5788-5798.
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A.F.Asega,
J.R.do Nascimento,
L.Schroeven,
W.Van den Ende,
and
M.A.Carvalho
(2008).
Cloning, characterization and functional analysis of a 1-FEH cDNA from Vernonia herbacea (Vell.) Rusby.
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Plant Cell Physiol, 49,
1185-1195.
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J.Mátrai,
W.Lammens,
A.Jonckheer,
K.Le Roy,
A.Rabijns,
W.Van den Ende,
and
M.De Maeyer
(2008).
An alternate sucrose binding mode in the E203Q Arabidopsis invertase mutant: an X-ray crystallography and docking study.
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Proteins, 71,
552-564.
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PDB code:
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K.Le Roy,
W.Lammens,
A.Van Laere,
and
W.Van den Ende
(2008).
Influencing the binding configuration of sucrose in the active sites of chicory fructan 1-exohydrolase and sugar beet fructan 6-exohydrolase.
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New Phytol, 178,
572-580.
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K.Le Roy,
M.Verhaest,
A.Rabijns,
S.Clerens,
A.Van Laere,
and
W.Van den Ende
(2007).
N-glycosylation affects substrate specificity of chicory fructan 1-exohydrolase: evidence for the presence of an inulin binding cleft.
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New Phytol, 176,
317-324.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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Links
