Information on EC 4.2.2.17 - inulin fructotransferase (DFA-I-forming)

for references in articles please use BRENDA:EC4.2.2.17
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The enzyme appears in viruses and cellular organisms

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EC NUMBER
COMMENTARY hide
4.2.2.17
-
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RECOMMENDED NAME
GeneOntology No.
inulin fructotransferase (DFA-I-forming)
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REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
Produces alpha-D-fructofuranose beta-D-fructofuranose 1,2':2,1'-dianhydride (DFA I) by successively eliminating the diminishing (2->1)-beta-D-fructan (inulin) chain from the terminal D-fructosyl-D-fructosyl disaccharide.
show the reaction diagram
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D-fructosyl-D-fructofuranosyl group transfer
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
(2->1)-beta-D-fructan lyase (alpha-D-fructofuranose-beta-D-fructofuranose-1,2':2,1'-dianhydride-forming)
This enzyme, like EC 4.2.2.16 [levan fructotransferase (DFA-IV-forming)] and EC 4.2.2.18 [inulin fructotransferase (DFA-III-forming)] eliminates the fructan chain from the terminal disaccharide leaving a difructose dianhydride. These enzymes have long been known as fructotransferases, so this is retained in the accepted name. Since the transfer is intramolecular, the reaction is an elimination and, hence, the enzyme is a lyase, belonging in EC 4.
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CAS REGISTRY NUMBER
COMMENTARY hide
125008-19-7
-
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MC12493
-
-
Manually annotated by BRENDA team
MC12493
-
-
Manually annotated by BRENDA team
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SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
inulin
3 di-D-fructofuranose-1,2':2,1'-dianhydride + H2O
show the reaction diagram
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NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
inulin
3 di-D-fructofuranose-1,2':2,1'-dianhydride + H2O
show the reaction diagram
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Fe3+
-
1 mM, strong
Hg2+
-
1 mM, strong
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
-
slight stimulation
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4
inulin
-
pH 5.5, 45°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3.5 - 8
-
10% of maximal activity at pH 3.5, 25% of maximal activity at pH 8.0
4.5 - 7
-
pH 4.5: about 50% of maximal activity, pH 7.0: about 50% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
80% of maximal activity at 30°C, 20% of maximal activity at 65°C
30 - 60
-
30°C: about 70% of maximal activity, 60°C: about 45% of maximal activity
30 - 65
-
30°C: about 80% of maximal activity
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37000
-
2 * 37000, SDS-PAGE
38000
-
2 * 38000, SDS-PAGE
39000
-
SDS-PAGE
40000
-
SDS-PAGE and gel filtration
41600
-
amino acid analysis
46000
-
gel filtration
60000
-
gel filtration
61000
-
gel filtration
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3
-
stable at 25°C
644467
4
-
30°C, 30 min., stable
644466
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
-
stable, rapid inactivation above 80°C
70
-
pH 6, 30 min., 80% activity
85
-
pH 5.5, 1 h, complete inactivation
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli MV1184
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nutrition
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LINKS TO OTHER DATABASES (specific for EC-Number 4.2.2.17)
ExplorEnz
ExPASy
KEGG
MetaCyc
SABIO-RK
NCBI: PubMed, Protein, Nucleotide, Structure, Genome, OMIM
IUBMB Enzyme Nomenclature
PROSITE Database of protein families and domains
InterPro (database of protein families, domains and functional sites)