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Information on EC 4.2.2.16 - levan fructotransferase (DFA-IV-forming)
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4.2.2.16 levan fructotransferase (DFA-IV-forming)IUBMB Comments
This enzyme, like EC 4.2.2.17 [inulin fructotransferase (DFA-I-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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Word Map
- 4.2.2.16
- arthrobacter
- difructose
- ureafaciens
- levanbiose
- inulin
- nicotinovorans
- disaccharide
- microbacterium
- oligosaccharides
- fructans
- synthesis
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gel-filtration
-
tetraose
-
non-reducing
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transfructosylation
- oligofructans
-
sweetener
- iptg
- monosaccharide
- fructooligosaccharides
- levanase
- biotechnology
- medicine
The enzyme appears in viruses and cellular organisms
Synonyms
lftase, levan fructotransferase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
2,6-beta-D-fructan D-fructosyl-D-fructosyltransferase (forming di-beta-D-fructofuranose 2,6':2',6-dianhydride)
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FTF
levan fructotransferase
levan fructotransferase (DFA-IV-forming)
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LFTase
LftM
levan fructotransferase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
[levan]n = di-beta-D-fructofuranose 2,6':2',6-dianhydride + [Levan]n-2
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SYSTEMATIC NAME
IUBMB Comments
(2->6)-beta-D-fructan lyase (di-beta-D-fructofuranose-2,6':2',6-dianhydride-forming)
This enzyme, like EC 4.2.2.17 [inulin fructotransferase (DFA-I-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
88593-15-1
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
ascorbic acid + levan
ascorbic acid 2-fructoside + ?
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transfructosylation. When 35% of ascorbic acid and 2% of levan are incubated with LFTase of 0.5 unit/g levan at 37°C for 85 h, a maximum 52 g/l of ascorbic acid 2-fructoside is produced
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?
phlein
di-D-fructose-2,6':2',6 dianhydride
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while it degrades Phleum pratense phlein more than 90%, formation of 6% reducing sugars as D-fructose
and two or three minor fructooligosaccharides
?
levan
5 di-D-fructose-2,6':2',6 dianhydride + ?
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levan from Zymomonas mobilis: conversion yield 28.4% after 24 h. Levan from Serratia: conversion yield: 28.4% after 24 h
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?
levan
5 di-D-fructose-2,6':2',6 dianhydride + ?
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levan from Zymomonas mobilis: conversion yield 28.4% after 24 h. Levan from Serratia: conversion yield: 28.4% after 24 h
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?
levan
5 di-D-fructose-2,6':2',6 dianhydride + ?
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?
levan
5 di-D-fructose-2,6':2',6 dianhydride + ?
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?
levan
5 di-D-fructose-2,6':2',6 dianhydride + ?
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?
levan
5 di-D-fructose-2,6':2',6 dianhydride + ?
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di-D-fructose-2,6':2',6 dianhydride is the main product, 75%. Fructose, levanbiose, and two unidentified oligosaccharides are minor products
?
levan
5 di-D-fructose-2,6':2',6 dianhydride + ?
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the enzyme is specifically induced by levan
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?
levan
5 di-D-fructose-2,6':2',6 dianhydride + ?
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di-D-fructose-2,6':2',6 dianhydride is the main product, 75%. Fructose, levanbiose, and two unidentified oligosaccharides are minor products
?
levan
5 di-D-fructose-2,6':2',6 dianhydride + ?
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the enzyme is specifically induced by levan
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?
levan
5 di-D-fructose-2,6':2',6 dianhydride + ?
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?
levan
5 di-D-fructose-2,6':2',6 dianhydride + ?
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?
levan
5 di-D-fructose-2,6':2',6 dianhydride + ?
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?
levan
5 di-D-fructose-2,6':2',6 dianhydride + ?
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the enzyme degrades Bacillus mesentericus levan up to 40% leaving the levan fragment at the limit of the enzymatic degradation, formation of 5% reducing sugars as D-fructose
and two or three minor fructooligosaccharides
?
levan
5 di-D-fructose-2,6':2',6 dianhydride + ?
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?
levan
5 di-D-fructose-2,6':2',6 dianhydride + ?
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levan from Zymomonas mobilis, conversion yield is 35%
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?
levan
5 di-D-fructose-2,6':2',6 dianhydride + ?
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levan from Zymomonas mobilis, conversion yield is 35%
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?
levan
5 di-D-fructose-2,6':2',6 dianhydride + ?
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?
levan
5 di-D-fructose-2,6':2',6 dianhydride + ?
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?
levan
di-D-fructofuranose-2,6':2',6 dianhydride + ?
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and small amounts of several oligosaccharides and free fructose
?
levan
di-D-fructofuranose-2,6':2',6 dianhydride + ?
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and small amounts of several oligosaccharides and free fructose
?
levan
di-D-fructose-2,6':2',6 dianhydride + fructose + limited levan
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di-D-fructose-2,6':2',6 dianhydride (49.1%) + fructose (3.5%) + limited levan (16.2%)
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?
levan
di-D-fructose-2,6':2',6 dianhydride + fructose + limited levan
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di-D-fructose-2,6':2',6 dianhydride (49.1%) + fructose (3.5%) + limited levan (16.2%)
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?
raffinose + D-galactopyranose
?
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transfer of the beta-fructofuranosyl residue from donor substrate to the 1-C of the acceptor galactopyranose, equilibrium towards galactosyl-fructoside
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r
raffinose + D-galactopyranose
?
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transfer of the beta-fructofuranosyl residue from donor substrate to the 1-C of the acceptor galactopyranose, equilibrium towards galactosyl-fructoside
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r
stachyose + D-galactopyranose
?
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transfer of the beta-fructofuranosyl residue from donor substrate to the 1-C of the acceptor galactopyranose, equilibrium towards galactosyl-fructoside
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r
stachyose + D-galactopyranose
?
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transfer of the beta-fructofuranosyl residue from donor substrate to the 1-C of the acceptor galactopyranose, equilibrium towards galactosyl-fructoside
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r
sucrose + D-galactopyranose
?
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transfer of the beta-fructofuranosyl residue from donor substrate to the 1-C of the acceptor galactopyranose, equilibrium towards galactosyl-fructoside
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r
sucrose + D-galactopyranose
?
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transfer of the beta-fructofuranosyl residue from donor substrate to the 1-C of the acceptor galactopyranose, equilibrium towards galactosyl-fructoside
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r
additional information
?
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no activity with dextran, soluble starch, inulin, maltose, sucrose, raffinose, 1-kestose, nystose and 1F-fructofuranosyl nystose
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?
additional information
?
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the enzyme never hydrolyzes beta-2,1-fructosyl-linked fructans, such as inulin, as well as oligosaccharides such as 1-kestose and nystose
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?
additional information
?
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no activity with dextran, soluble starch, inulin, maltose, sucrose, raffinose, 1-kestose, nystose and 1F-fructofuranosyl nystose
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?
additional information
?
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the enzyme never hydrolyzes beta-2,1-fructosyl-linked fructans, such as inulin, as well as oligosaccharides such as 1-kestose and nystose
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?
additional information
?
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no formation of fructose, levanbiose, nor difructose anhydride IV from bifurcose and [O-beta-D-Fru(f)-(2-1)]-O-[beta-D-Fru(f)-(2-6)]2-O-beta-D-Fru(f)-(2-1)-alpha-D-G(p)
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?
additional information
?
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no activity with inulin, levanbiose, sucrose, dextran or starch
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?
additional information
?
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no activity with inulin, levanbiose, sucrose, dextran or starch
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?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
levan
5 di-D-fructose-2,6':2',6 dianhydride + ?
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the enzyme is specifically induced by levan
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?
levan
5 di-D-fructose-2,6':2',6 dianhydride + ?
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the enzyme is specifically induced by levan
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?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CaCl2
NaCl
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1 mM, activation to 125% of control. 10 mM, activation to 142% of control
CaCl2
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1 mM, activation to 156% of control. 10 mM, activation to 181% of control
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
Km for levan: 2 mg/ml at pH 7.0 and 40°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 7.5
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pH 5.0: about 35% of maximal activity, pH 7.5: about 40% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
50
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 50
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30°C: about 35% of maximal activity, 50°C: about 80% of maximal activity, 60°C: about 15% of maximal activity
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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recombinant enzyme expressed in Escherichia coli
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brenda
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recombinant enzyme expressed in Escherichia coli
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brenda
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Q9EVQ9_9MICO
530
0
57458
TrEMBL
Secretory Pathway (Reliability: 1)
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
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