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Information on EC 2.4.1.10 - levansucrase and Organism(s) Priestia megaterium and UniProt Accession D5DC07
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2.4.1.10 levansucraseIUBMB Comments
Some other sugars can act as D-fructosyl acceptors.
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Word Map
- 2.4.1.10
-
fructosylation
- fructooligosaccharides
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transfructosylation
- mobilis
-
zymomonas
- exopolysaccharide
- erwinia
- raffinose
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prebiotics
- inulin
-
levan-type
- diazotrophicus
- fructosyltransferases
- leuconostoc
- reuteri
- inulosucrase
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gluconacetobacter
- mesenteroides
- dextransucrase
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sucrose:sucrose
- synthesis
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gluconobacter
- 6-kestose
- aquatilis
-
rahnella
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exocellular
- invertases
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hpaec-pad
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sourdough
-
amylovoran
-
antitermination
- oxydans
- food industry
- agriculture
The taxonomic range for the selected organisms is: Priestia megaterium
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea
Synonyms
levansucrase, 6-sft, sucrose:fructan 6-fructosyltransferase, fructansucrase, lsc-3, t2-ls, t1-ls, sucrose 6-fructosyltransferase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
beta-2,6-fructan:D-glucose 1-fructosyltransferase
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beta-2,6-fructosyltransferase
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fructosyltransferase, sucrose 6-
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sucrose 6-fructosyltransferase
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hexosyl group transfer
hexosyl group transfer
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SYSTEMATIC NAME
IUBMB Comments
sucrose:[6)-beta-D-fructofuranosyl-(2->]n alpha-D-glucopyranoside 6-beta-D-fructosyltransferase
Some other sugars can act as D-fructosyl acceptors.
CAS REGISTRY NUMBER
COMMENTARY
9030-17-5
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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
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
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-
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?
sucrose + (2,6-beta-D-fructosyl)n
D-glucose + (2,6-beta-D-fructosyl)n+1
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polyfructan produced by the levansucrase from Bacillus megaterium has a molecular mass of 2711 kDa and consisted mainly of beta(2,6) linkages. Besides the polyfructan formation, the wild-type levansucrase of Bacillus megaterium also synthesizes five different detectable oligosaccharides. Three products are identified: 1-kestose (isokestose), 6-kestose and nystose which are known acceptors for the transfer of fructosyl units
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-
?
sucrose + ?
blastose + ?
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two-dimensional COSY, TOCSY, HMBC and HSQC experiments
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?
sucrose + ?
polyfructan + ?
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polyfructan, molecular mass of 2711 kDa and consisted mainly of beta(2-6) linkages
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?
sucrose + sucrose
D-glucose + neokestose
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identified by one-dimensional and correlation spectroscopy (i.e. COSY, TOCSY, HMBC, DEPT and HSQC)
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?
additional information
?
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levan synthesis, the first reaction of levan synthesis is formation of 6-kestose from two molecules of sucrose, one acting as a fructosyl donor and the other as an acceptor. 6-Kestose is further extended through numerous transfructosylation reactions
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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
sucrose + [beta-D-fructofuranosyl-(2->6)]n alpha-D-glucopyranoside
D-glucose + [beta-D-fructofuranosyl-(2->6)]n+1 alpha-D-glucopyranoside
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-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
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2.3 mM (sucrose) total, mutant enzyme S173A
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additional information
additional information
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29.2 mM (sucrose) total, mutant enzyme R370A, a 4fold KM value decrease compared with the wild-type enzyme supported the interactions of Arg 370 with the 2-OH and 3-OH of the glucosyl residue in the active site
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additional information
additional information
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31.9 mM (sucrose) total, mutant enzyme W94A, 9% of the catalytic efficiency of the wild-type
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additional information
additional information
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35.1 mM (sucrose) total, mutant enzyme N252H
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additional information
additional information
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4.1 mM (sucrose) total, mutant enzyme N252A
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additional information
additional information
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480.4 mM (sucrose) total, mutant enzyme W172A, 72fold increase of the KM of the wild-type
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additional information
additional information
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51.9 mM (sucrose) total, mutant enzyme Y421A, 3%of the wild-type activity
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additional information
additional information
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6.6 mM (sucrose) total, wild-type, pH 6.6, 37°C, 50 mM Sorensens phosphate buffer, 7.36 mg/l enzyme concentration, reaction time 60 min
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additional information
additional information
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66.6 mM (sucrose), mutant enzyme L118A
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additional information
additional information
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7.5 mM (sucrose) total, mutant enzyme N252G
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additional information
additional information
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8.4 mM (sucrose) total, mutant enzyme N252D
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additional information
additional information
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mutant enzyme D257A, no activity
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additional information
additional information
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mutant enzyme D95A, no activity
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additional information
additional information
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mutant enzyme E350A, nearly inactive
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additional information
additional information
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mutant enzyme E352A, no measureable activity
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additional information
additional information
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mutant enzyme R256A, nearly inactive
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
6 - 7
6 - 7
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wild-type, 50 mM Sorensens phosphate buffer at 37°C, containing 500 mM sucrose using an enzyme concentration of 7.36 mg/l
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.6 - 7.6
5.6 - 7.6
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the enzyme activity significantly decreases at pH values below 5.6 and above 7.6
5.6 - 7.6
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wild-type, 50 mM Sorensens phosphate buffer at 37°C, containing 500 mM sucrose using an enzyme concentration of 7.36 mg/l
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
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in addition to fructooligosaccharides, levansucrases produce polymeric levan, degree of polymerization of which can be very high
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
52000
52000
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FPLC, proteins are identified by peptide mass fingerprinting, as well as by using postsource decay fragmentation data recorded with an Ultraflex MALDI-TOF (matrix-assisted laser desorption ionization-time of flight) mass spectrometer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
K373A
the mutant shows 2fold decrease in catalytic efficiency compared to the wild type enzyme
K373R
the mutant shows 2fold decrease in catalytic efficiency compared to the wild type enzyme
N252H
the mutant shows 8fold decrease in catalytic efficiency compared to the wild type enzyme
R370A
the mutant shows 57fold decrease in catalytic efficiency compared to the wild type enzyme
S173A
the mutant shows 19fold decrease in catalytic efficiency compared to the wild type enzyme
S173G
the mutant shows 59fold decrease in catalytic efficiency compared to the wild type enzyme
S173T
the mutant shows 7fold decrease in catalytic efficiency compared to the wild type enzyme
S422A
the mutant shows 4fold decrease in catalytic efficiency compared to the wild type enzyme
W172A
the mutant shows 69fold decrease in catalytic efficiency compared to the wild type enzyme
W94A
the mutant shows 11fold decrease in catalytic efficiency compared to the wild type enzyme
Y247A
the mutant shows 2fold decrease in catalytic efficiency compared to the wild type enzyme
Y247I
the mutant shows 2fold decrease in catalytic efficiency compared to the wild type enzyme
Y247W
the mutant shows 0.2fold decrease in catalytic efficiency compared to the wild type enzyme
Y421A
the mutant shows 520fold decrease in catalytic efficiency compared to the wild type enzyme
Y421F
the mutant shows 33fold decrease in catalytic efficiency compared to the wild type enzyme
Y421M
the mutant shows 302fold decrease in catalytic efficiency compared to the wild type enzyme
Y421W
the mutant shows 101fold decrease in catalytic efficiency compared to the wild type enzyme
Y439A
the mutant shows 2130fold decrease in catalytic efficiency compared to the wild type enzyme
Y439F
the mutant shows 9fold decrease in catalytic efficiency compared to the wild type enzyme
Y439M
the mutant shows 131fold decrease in catalytic efficiency compared to the wild type enzyme
Y439W
the mutant shows 41fold decrease in catalytic efficiency compared to the wild type enzyme
D257A
E350A
L118A
N252A
R256A
R370A
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site-directed mutagenesis, after a reaction time of 60 min an accumulation of neokestose (2,6-beta-Fru-betaGlc-1,2-beta-Fru, 32.7 mM) is determined, whereas after 19 h, blastose (2,6-beta-Fru-alpha,betaGlc) is the main reaction product (69.7 mM)
S173A
W172A
W94A
Y421A
W172A
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site-directed mutagenesis, 72fold increase of the KM of the wild-type
W94A
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site-directed mutagenesis, 9% of the catalytic efficiency of the wild-type
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
in standard reactions, long-term temperature treatment revealed a high protein stability at 37°C for at least 24h
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Homann, A.; Biedendieck, R.; Gtze, S.; Jahn, D.; Seibel, J.
Insights into polymer versus oligosaccharide synthesis: mutagenesis and mechanistic studies of a novel levansucrase from Bacillus megaterium
Biochem. J.
407
189-198
2007
Priestia megaterium, Priestia megaterium DSM 319
Visnapuu, T.; Mardo, K.; Alamaee, T.
Levansucrases of a Pseudomonas syringae pathovar as catalysts for the synthesis of potentially prebiotic oligo- and polysaccharides
New Biotechnol.
32
597-605
2015
Priestia megaterium, Bacillus subtilis, Burkholderia cepacia, Dactylis glomerata, Erwinia amylovora, Lactobacillus gasseri, Limosilactobacillus reuteri, Fructilactobacillus sanfranciscensis, Zymomonas mobilis, Limosilactobacillus panis, Phleum pratense, Pseudomonas syringae (O68609), Gluconacetobacter diazotrophicus (Q43998), Pseudomonas syringae pv. tomato (Q883P5), Pseudomonas syringae pv. tomato (Q88BN6), Pseudomonas chlororaphis subsp. aurantiaca (Q93FU9), Bacillus licheniformis (W8GV60), Pseudomonas syringae pv. tomato DC3000 (Q883P5), Pseudomonas syringae pv. tomato DC3000 (Q88BN6)
Ortiz-Soto, M.E.; Porras-Dominguez, J.R.; Seibel, J.; Lopez-Munguia, A.
A close look at the structural features and reaction conditions that modulate the synthesis of low and high molecular weight fructans by levansucrases
Carbohydr. Polym.
219
130-142
2019
Pseudomonas syringae, Zymomonas mobilis, Priestia megaterium (D5DC07), Bacillus subtilis (P05655), Bacillus subtilis 168 (P05655), Priestia megaterium DSM 319 (D5DC07)
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