Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Visnapuu, T.; Mardo, K.; Alamaee, T.
    Levansucrases of a Pseudomonas syringae pathovar as catalysts for the synthesis of potentially prebiotic oligo- and polysaccharides (2015), New Biotechnol., 32, 597-605.
    View publication on PubMed

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.4.1.10 catalytic center of levansucrase LsdA, PDB ID 1W18, with raffinose molecule, from PDB ID 3BYN, in the substrate-binding pocket Zymomonas mobilis
2.4.1.10 catalytic center of levansucrase LsdA, PDB ID 1W18, with raffinose molecule, from PDB ID 3BYN, in the substrate-binding pocket Gluconacetobacter diazotrophicus

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.10 D219A site-directed mutagenesis, inactive mutant Pseudomonas syringae pv. tomato
2.4.1.10 D225A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Pseudomonas syringae pv. tomato
2.4.1.10 D225N site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Pseudomonas syringae pv. tomato
2.4.1.10 D300A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Pseudomonas syringae pv. tomato
2.4.1.10 D31N site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Pseudomonas syringae pv. tomato
2.4.1.10 D333A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Pseudomonas syringae pv. tomato
2.4.1.10 D333N site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme Pseudomonas syringae pv. tomato
2.4.1.10 D62A site-directed mutagenesis, inactive mutant Pseudomonas syringae pv. tomato
2.4.1.10 E110D site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme Pseudomonas syringae pv. tomato
2.4.1.10 E146Q site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme Pseudomonas syringae pv. tomato
2.4.1.10 E236Q site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Pseudomonas syringae pv. tomato
2.4.1.10 E303A site-directed mutagenesis, inactive mutant Pseudomonas syringae pv. tomato
2.4.1.10 E303Q site-directed mutagenesis, inactive mutant Pseudomonas syringae pv. tomato
2.4.1.10 H113A site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Pseudomonas syringae pv. tomato
2.4.1.10 H113Q site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Pseudomonas syringae pv. tomato
2.4.1.10 H306A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Pseudomonas syringae pv. tomato
2.4.1.10 H321K site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Pseudomonas syringae pv. tomato
2.4.1.10 H321L site-directed mutagenesis, almost inactive mutant Pseudomonas syringae pv. tomato
2.4.1.10 H321R site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Pseudomonas syringae pv. tomato
2.4.1.10 H321S site-directed mutagenesis, almost inactive mutant Pseudomonas syringae pv. tomato
2.4.1.10 L66A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Pseudomonas syringae pv. tomato
2.4.1.10 P220A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Pseudomonas syringae pv. tomato
2.4.1.10 Q301A site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Pseudomonas syringae pv. tomato
2.4.1.10 Q301E site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Pseudomonas syringae pv. tomato
2.4.1.10 R304A site-directed mutagenesis, almost inactive mutant Pseudomonas syringae pv. tomato
2.4.1.10 R304C site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Pseudomonas syringae pv. tomato
2.4.1.10 T302M site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme Pseudomonas syringae pv. tomato
2.4.1.10 T302P site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Pseudomonas syringae pv. tomato
2.4.1.10 V248A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Pseudomonas syringae pv. tomato
2.4.1.10 W109A site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Pseudomonas syringae pv. tomato
2.4.1.10 W109F site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Pseudomonas syringae pv. tomato
2.4.1.10 W109R site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Pseudomonas syringae pv. tomato
2.4.1.10 W61A site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme Pseudomonas syringae pv. tomato
2.4.1.10 W61N site-directed mutagenesis, almost inactive mutant Pseudomonas syringae pv. tomato
2.4.1.10 W63A site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme Pseudomonas syringae pv. tomato

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.4.1.10 raffinose
-
Pseudomonas chlororaphis subsp. aurantiaca
2.4.1.10 raffinose
-
Pseudomonas syringae pv. tomato

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.4.1.10 17.1
-
sucrose sucrose hydrolysis, pH 6.0-6.6, 60°C Pseudomonas syringae pv. tomato
2.4.1.10 18.5
-
sucrose sucrose hydrolysis, pH 6.0-6.6, 60°C Pseudomonas syringae pv. tomato
2.4.1.10 24.1
-
sucrose sucrose hydrolysis, pH 6.0-6.6, 60°C Pseudomonas chlororaphis subsp. aurantiaca
2.4.1.10 160
-
sucrose sucrose hydrolysis, pH 5.8-6.6, 60°C Pseudomonas syringae

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.4.1.10 extracellular
-
Bacillus subtilis
-
-
2.4.1.10 extracellular
-
Priestia megaterium
-
-
2.4.1.10 extracellular
-
Zymomonas mobilis
-
-
2.4.1.10 extracellular
-
Burkholderia cepacia
-
-
2.4.1.10 extracellular
-
Dactylis glomerata
-
-
2.4.1.10 extracellular
-
Limosilactobacillus reuteri
-
-
2.4.1.10 extracellular
-
Erwinia amylovora
-
-
2.4.1.10 extracellular
-
Lactobacillus gasseri
-
-
2.4.1.10 extracellular
-
Fructilactobacillus sanfranciscensis
-
-
2.4.1.10 extracellular
-
Gluconacetobacter diazotrophicus
-
-
2.4.1.10 extracellular
-
Limosilactobacillus panis
-
-
2.4.1.10 extracellular
-
Pseudomonas syringae pv. tomato
-
-
2.4.1.10 extracellular
-
Phleum pratense
-
-
2.4.1.10 extracellular
-
Pseudomonas chlororaphis subsp. aurantiaca
-
-
2.4.1.10 extracellular
-
Pseudomonas syringae
-
-
2.4.1.10 intracellular
-
Bacillus licheniformis 5622
-

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.10 Bacillus licheniformis W8GV60
-
-
2.4.1.10 Bacillus subtilis
-
-
-
2.4.1.10 Burkholderia cepacia
-
-
-
2.4.1.10 Dactylis glomerata
-
-
-
2.4.1.10 Erwinia amylovora
-
-
-
2.4.1.10 Fructilactobacillus sanfranciscensis
-
-
-
2.4.1.10 Gluconacetobacter diazotrophicus Q43998
-
-
2.4.1.10 Lactobacillus gasseri
-
-
-
2.4.1.10 Limosilactobacillus panis
-
-
-
2.4.1.10 Limosilactobacillus reuteri
-
-
-
2.4.1.10 Phleum pratense
-
-
-
2.4.1.10 Priestia megaterium
-
-
-
2.4.1.10 Pseudomonas chlororaphis subsp. aurantiaca Q93FU9 gene lscA
-
2.4.1.10 Pseudomonas syringae O68609 pv. phaseolicola, gene lsc
-
2.4.1.10 Pseudomonas syringae pv. tomato Q883P5 pv. tomato, gene lsc2
-
2.4.1.10 Pseudomonas syringae pv. tomato Q88BN6 pv. tomato, gene lsc3
-
2.4.1.10 Pseudomonas syringae pv. tomato DC3000 Q883P5 pv. tomato, gene lsc2
-
2.4.1.10 Pseudomonas syringae pv. tomato DC3000 Q88BN6 pv. tomato, gene lsc3
-
2.4.1.10 Zymomonas mobilis
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.10 2 sucrose
-
Bacillus subtilis 6-kestose + D-glucose
-
?
2.4.1.10 2 sucrose
-
Priestia megaterium 6-kestose + D-glucose
-
?
2.4.1.10 2 sucrose
-
Zymomonas mobilis 6-kestose + D-glucose
-
?
2.4.1.10 2 sucrose
-
Burkholderia cepacia 6-kestose + D-glucose
-
?
2.4.1.10 2 sucrose
-
Dactylis glomerata 6-kestose + D-glucose
-
?
2.4.1.10 2 sucrose
-
Limosilactobacillus reuteri 6-kestose + D-glucose
-
?
2.4.1.10 2 sucrose
-
Erwinia amylovora 6-kestose + D-glucose
-
?
2.4.1.10 2 sucrose
-
Lactobacillus gasseri 6-kestose + D-glucose
-
?
2.4.1.10 2 sucrose
-
Fructilactobacillus sanfranciscensis 6-kestose + D-glucose
-
?
2.4.1.10 2 sucrose
-
Gluconacetobacter diazotrophicus 6-kestose + D-glucose
-
?
2.4.1.10 2 sucrose
-
Limosilactobacillus panis 6-kestose + D-glucose
-
?
2.4.1.10 2 sucrose
-
Pseudomonas syringae pv. tomato 6-kestose + D-glucose
-
?
2.4.1.10 2 sucrose
-
Phleum pratense 6-kestose + D-glucose
-
?
2.4.1.10 2 sucrose
-
Bacillus licheniformis 6-kestose + D-glucose
-
?
2.4.1.10 2 sucrose
-
Pseudomonas chlororaphis subsp. aurantiaca 6-kestose + D-glucose
-
?
2.4.1.10 2 sucrose
-
Pseudomonas syringae 6-kestose + D-glucose
-
?
2.4.1.10 2 sucrose
-
Pseudomonas syringae pv. tomato DC3000 6-kestose + D-glucose
-
?
2.4.1.10 additional information 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 Bacillus subtilis ?
-
?
2.4.1.10 additional information 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 Priestia megaterium ?
-
?
2.4.1.10 additional information 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 Zymomonas mobilis ?
-
?
2.4.1.10 additional information 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 Burkholderia cepacia ?
-
?
2.4.1.10 additional information 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 Dactylis glomerata ?
-
?
2.4.1.10 additional information 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 Limosilactobacillus reuteri ?
-
?
2.4.1.10 additional information 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 Erwinia amylovora ?
-
?
2.4.1.10 additional information 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 Lactobacillus gasseri ?
-
?
2.4.1.10 additional information 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 Fructilactobacillus sanfranciscensis ?
-
?
2.4.1.10 additional information 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 Gluconacetobacter diazotrophicus ?
-
?
2.4.1.10 additional information 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 Limosilactobacillus panis ?
-
?
2.4.1.10 additional information 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 Phleum pratense ?
-
?
2.4.1.10 additional information 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 Bacillus licheniformis ?
-
?
2.4.1.10 additional information 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. No activity with raffinose or stachyose Pseudomonas syringae ?
-
?
2.4.1.10 additional information 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. The enzyme cleaves raffinose and stachyose Pseudomonas syringae pv. tomato ?
-
?
2.4.1.10 additional information 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. The enzyme cleaves raffinose and stachyose Pseudomonas chlororaphis subsp. aurantiaca ?
-
?
2.4.1.10 additional information 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. The enzyme cleaves raffinose and stachyose Pseudomonas syringae pv. tomato DC3000 ?
-
?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.10 endolevanase
-
Bacillus licheniformis
2.4.1.10 LevB1
-
Bacillus licheniformis
2.4.1.10 LevU
-
Zymomonas mobilis
2.4.1.10 Lsc
-
Pseudomonas syringae
2.4.1.10 Lsc2
-
Pseudomonas syringae pv. tomato
2.4.1.10 Lsc3
-
Pseudomonas syringae pv. tomato
2.4.1.10 LscA
-
Pseudomonas chlororaphis subsp. aurantiaca
2.4.1.10 LSD
-
Burkholderia cepacia
2.4.1.10 LsdA
-
Gluconacetobacter diazotrophicus
2.4.1.10 SacB
-
Gluconacetobacter diazotrophicus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
2.4.1.10 20
-
transfructosylation Pseudomonas syringae pv. tomato
2.4.1.10 20
-
transfructosylation Pseudomonas chlororaphis subsp. aurantiaca
2.4.1.10 50
-
sucrose hydrolysis Pseudomonas syringae pv. tomato
2.4.1.10 60
-
sucrose hydrolysis Pseudomonas syringae pv. tomato
2.4.1.10 60
-
sucrose hydrolysis Pseudomonas chlororaphis subsp. aurantiaca
2.4.1.10 60
-
sucrose hydrolysis Pseudomonas syringae

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.4.1.10 7.2
-
sucrose sucrose hydrolysis, pH 6.0-6.6, 60°C Pseudomonas chlororaphis subsp. aurantiaca
2.4.1.10 328.3
-
sucrose sucrose hydrolysis, pH 6.0-6.6, 60°C Pseudomonas syringae pv. tomato
2.4.1.10 504.4
-
sucrose sucrose hydrolysis, pH 6.0-6.6, 60°C Pseudomonas syringae pv. tomato

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
2.4.1.10 5.8 6.6 sucrose hydrolysis Pseudomonas syringae
2.4.1.10 6
-
sucrose hydrolysis Pseudomonas syringae pv. tomato
2.4.1.10 6 6.6 sucrose hydrolysis Pseudomonas chlororaphis subsp. aurantiaca

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.4.1.10 39.9
-
raffinose inhibition of sucrose hydrolysis, pH 6.0, 60°C Pseudomonas syringae pv. tomato
2.4.1.10 49
-
raffinose inhibition of sucrose hydrolysis, pH 6.0, 60°C Pseudomonas syringae pv. tomato
2.4.1.10 80.8
-
raffinose inhibition of sucrose hydrolysis, pH 6.0-6.6, 60°C Pseudomonas chlororaphis subsp. aurantiaca

General Information

EC Number General Information Comment Organism
2.4.1.10 additional information the catalytic triad is formed by residues Asp135, Asp309 and Glu401 Zymomonas mobilis
2.4.1.10 additional information the catalytic triad is formed by residues Asp135, Asp309 and Glu401 Gluconacetobacter diazotrophicus
2.4.1.10 additional information the three-dimensional structure of enzyme Lsc2 of Pseudomonas syringae pv. tomato is modeled on the basis of crystal structures of either LsdA of Gluconacetobacter diazotrophicus or beta-fructofuranosidase of Arthrobacter sp. K-1 Pseudomonas syringae pv. tomato
2.4.1.10 additional information the three-dimensional structure of enzyme Lsc3 of Pseudomonas syringae pv. tomato is modeled on the basis of crystal structures of either LsdA of Gluconacetobacter diazotrophicus or beta-fructofuranosidase of Arthrobacter sp. K-1 Pseudomonas syringae pv. tomato
2.4.1.10 physiological function in addition to fructooligosaccharides, levansucrases produce polymeric levan, degree of polymerization of which can be very high Bacillus subtilis
2.4.1.10 physiological function in addition to fructooligosaccharides, levansucrases produce polymeric levan, degree of polymerization of which can be very high Priestia megaterium
2.4.1.10 physiological function in addition to fructooligosaccharides, levansucrases produce polymeric levan, degree of polymerization of which can be very high Zymomonas mobilis
2.4.1.10 physiological function in addition to fructooligosaccharides, levansucrases produce polymeric levan, degree of polymerization of which can be very high Burkholderia cepacia
2.4.1.10 physiological function in addition to fructooligosaccharides, levansucrases produce polymeric levan, degree of polymerization of which can be very high Limosilactobacillus reuteri
2.4.1.10 physiological function in addition to fructooligosaccharides, levansucrases produce polymeric levan, degree of polymerization of which can be very high Erwinia amylovora
2.4.1.10 physiological function in addition to fructooligosaccharides, levansucrases produce polymeric levan, degree of polymerization of which can be very high Lactobacillus gasseri
2.4.1.10 physiological function in addition to fructooligosaccharides, levansucrases produce polymeric levan, degree of polymerization of which can be very high Fructilactobacillus sanfranciscensis
2.4.1.10 physiological function in addition to fructooligosaccharides, levansucrases produce polymeric levan, degree of polymerization of which can be very high Limosilactobacillus panis
2.4.1.10 physiological function in addition to fructooligosaccharides, levansucrases produce polymeric levan, degree of polymerization of which can be very high Pseudomonas syringae pv. tomato
2.4.1.10 physiological function in addition to fructooligosaccharides, levansucrases produce polymeric levan, degree of polymerization of which can be very high Bacillus licheniformis
2.4.1.10 physiological function in addition to fructooligosaccharides, levansucrases produce polymeric levan, degree of polymerization of which can be very high Pseudomonas chlororaphis subsp. aurantiaca
2.4.1.10 physiological function in addition to fructooligosaccharides, levansucrases produce polymeric levan, degree of polymerization of which can be very high Pseudomonas syringae
2.4.1.10 physiological function in addition to fructooligosaccharides, levansucrases produce polymeric levan, degree of polymerization of which can be very high. Enzyme LsdA is specifically prone for fructooligosaccharide synthesis, producing inulin-type fructooligosaccharides and only a small amount of levan Gluconacetobacter diazotrophicus
2.4.1.10 physiological function in addition to fructooligosaccharides, levansucrases produce polymeric levan, degree of polymerization of which can be very high. The plant enzyme synthesizes linear beta-2,6-linked fructans which are referred to as plant levans or phleins. Phleins have lower degree of polymerization than bacterial levans which usually have polymers of DP over 100 Dactylis glomerata
2.4.1.10 physiological function in addition to fructooligosaccharides, levansucrases produce polymeric levan, degree of polymerization of which can be very high. The plant enzyme synthesizes linear beta-2,6-linked fructans which are referred to as plant levans or phleins. Phleins have lower degree of polymerization than bacterial levans which usually have polymers of DP over 100 Phleum pratense