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

for references in articles please use BRENDA:EC4.2.2.17
Word Map on EC 4.2.2.17
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Select one or more organisms in this record:

The enzyme appears in viruses and cellular organisms

top print hide
EC NUMBER
COMMENTARY hide
4.2.2.17
-
top print hide
RECOMMENDED NAME
GeneOntology No.
inulin fructotransferase (DFA-I-forming)
top print hide
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
-
-
-
-
top print hide
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D-fructosyl-D-fructofuranosyl group transfer
-
-
-
-
top print hide
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.
top
top print hide
CAS REGISTRY NUMBER
COMMENTARY hide
125008-19-7
-
top print hide
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
MC12493
-
-
Manually annotated by BRENDA team
MC12493
-
-
Manually annotated by BRENDA team
top print hide
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
top print hide
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
top print hide
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Fe3+
-
1 mM, strong
Hg2+
-
1 mM, strong
top print hide
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EDTA
-
slight stimulation
top print hide
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4
inulin
-
pH 5.5, 45°C
top print hide
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide
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
top print hide
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
top print hide
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
top print hide
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
top print hide
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
top print hide
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
top print hide
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
top print hide
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
3
-
stable at 25°C
644467
4
-
30°C, 30 min., stable
644466
top print hide
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
top print hide
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
top print hide
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli MV1184
-
top print hide
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
nutrition
top
top
top
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)