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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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Plant J
41:400-411
(2005)
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PubMed id:
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X-ray diffraction structure of a plant glycosyl hydrolase family 32 protein: fructan 1-exohydrolase IIa of Cichorium intybus.
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M.Verhaest,
W.V.Ende,
K.L.Roy,
C.J.De Ranter,
A.V.Laere,
A.Rabijns.
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ABSTRACT
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Fructan 1-exohydrolase, an enzyme involved in fructan degradation, belongs to
the glycosyl hydrolase family 32. The structure of isoenzyme 1-FEH IIa from
Cichorium intybus is described at a resolution of 2.35 A. The structure consists
of an N-terminal fivefold beta-propeller domain connected to two C-terminal
beta-sheets. The putative active site is located entirely in the beta-propeller
domain and is formed by amino acids which are highly conserved within glycosyl
hydrolase family 32. The fructan-binding site is thought to be in the cleft
formed between the two domains. The 1-FEH IIa structure is compared with the
structures of two homologous but functionally different enzymes: a levansucrase
from Bacillus subtilis (glycosyl hydrolase family 68) and an invertase from
Thermotoga maritima (glycosyl hydrolase family 32).
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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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B.Lasseur,
J.Lothier,
A.Wiemken,
A.Van Laere,
A.Morvan-Bertrand,
W.V.Ende,
and
M.P.Prud'homme
(2011).
Towards a better understanding of the generation of fructan structure diversity in plants: molecular and functional characterization of a sucrose:fructan 6-fructosyltransferase (6-SFT) cDNA from perennial ryegrass (Lolium perenne).
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J Exp Bot, 62,
1871-1885.
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A.Homann,
and
J.Seibel
(2009).
Chemo-enzymatic synthesis and functional analysis of natural and modified glycostructures.
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Nat Prod Rep, 26,
1555-1571.
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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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F.del Viso,
A.F.Puebla,
H.E.Hopp,
and
R.A.Heinz
(2009).
Cloning and functional characterization of a fructan 1-exohydrolase (1-FEH) in the cold tolerant Patagonian species Bromus pictus.
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Planta, 231,
13-25.
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K.Tamura,
A.Kawakami,
Y.Sanada,
K.Tase,
T.Komatsu,
and
M.Yoshida
(2009).
Cloning and functional analysis of a fructosyltransferase cDNA for synthesis of highly polymerized levans in timothy (Phleum pratense L.).
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J Exp Bot, 60,
893-905.
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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,
K.Harms,
T.Rausch,
and
S.Greiner
(2009).
Inhibitors of plant invertases do not affect the structurally related enzymes of fructan metabolism.
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New Phytol, 181,
601-612.
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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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G.Meng,
and
K.Fütterer
(2008).
Donor substrate recognition in the raffinose-bound E342A mutant of fructosyltransferase Bacillus subtilis levansucrase.
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BMC Struct Biol, 8,
16.
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PDB codes:
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H.Hisano,
A.Kanazawa,
M.Yoshida,
M.O.Humphreys,
M.Iizuka,
K.Kitamura,
and
T.Yamada
(2008).
Coordinated expression of functionally diverse fructosyltransferase genes is associated with fructan accumulation in response to low temperature in perennial ryegrass.
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New Phytol, 178,
766-780.
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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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C.Goosen,
X.L.Yuan,
J.M.van Munster,
A.F.Ram,
M.J.van der Maarel,
and
L.Dijkhuizen
(2007).
Molecular and biochemical characterization of a novel intracellular invertase from Aspergillus niger with transfructosylating activity.
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Eukaryot Cell, 6,
674-681.
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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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M.Verhaest,
W.Lammens,
K.Le Roy,
C.J.De Ranter,
A.Van Laere,
A.Rabijns,
and
W.Van den Ende
(2007).
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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New Phytol, 174,
90.
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PDB codes:
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W.S.Jung,
C.K.Hong,
S.Lee,
C.S.Kim,
S.J.Kim,
S.I.Kim,
and
S.Rhee
(2007).
Structural and functional insights into intramolecular fructosyl transfer by inulin fructotransferase.
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J Biol Chem, 282,
8414-8423.
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PDB codes:
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L.K.Ozimek,
S.Kralj,
T.Kaper,
M.J.van der Maarel,
and
L.Dijkhuizen
(2006).
Single amino acid residue changes in subsite -1 of inulosucrase from Lactobacillus reuteri 121 strongly influence the size of products synthesized.
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FEBS J, 273,
4104-4113.
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M.Verhaest,
W.Lammens,
K.Le Roy,
B.De Coninck,
C.J.De Ranter,
A.Van Laere,
W.Van den Ende,
and
A.Rabijns
(2006).
X-ray diffraction structure of a cell-wall invertase from Arabidopsis thaliana.
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Acta Crystallogr D Biol Crystallogr, 62,
1555-1563.
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PDB code:
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T.Ritsema,
L.Hernández,
A.Verhaar,
D.Altenbach,
T.Boller,
A.Wiemken,
and
S.Smeekens
(2006).
Developing fructan-synthesizing capability in a plant invertase via mutations in the sucrose-binding box.
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Plant J, 48,
228-237.
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J.Chalmers,
A.Lidgett,
N.Cummings,
Y.Cao,
J.Forster,
and
G.Spangenberg
(2005).
Molecular genetics of fructan metabolism in perennial ryegrass.
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Plant Biotechnol J, 3,
459-474.
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M.Verhaest,
K.Le Roy,
S.Sansen,
B.De Coninck,
W.Lammens,
C.J.De Ranter,
A.Van Laere,
W.Van den Ende,
and
A.Rabijns
(2005).
Crystallization and preliminary X-ray diffraction study of a cell-wall invertase from Arabidopsis thaliana.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 61,
766-768.
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T.Ritsema,
A.Verhaar,
I.Vijn,
and
S.Smeekens
(2005).
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.
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Plant Mol Biol, 58,
597-607.
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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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