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Literature summary for 2.4.1.10 extracted from
- Levansucrases of a Pseudomonas syringae pathovar as catalysts for the synthesis of potentially prebiotic oligo- and polysaccharides (2015), New Biotechnol., 32, 597-605.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| catalytic center of levansucrase LsdA, PDB ID 1W18, with raffinose molecule, from PDB ID 3BYN, in the substrate-binding pocket | Zymomonas mobilis |
| catalytic center of levansucrase LsdA, PDB ID 1W18, with raffinose molecule, from PDB ID 3BYN, in the substrate-binding pocket | Gluconacetobacter diazotrophicus |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D219A | site-directed mutagenesis, inactive mutant | Pseudomonas syringae pv. tomato |
| D225A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Pseudomonas syringae pv. tomato |
| D225N | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Pseudomonas syringae pv. tomato |
| D300A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Pseudomonas syringae pv. tomato |
| D31N | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Pseudomonas syringae pv. tomato |
| D333A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Pseudomonas syringae pv. tomato |
| D333N | site-directed mutagenesis, the mutant shows similar activity as the wild-type enzyme | Pseudomonas syringae pv. tomato |
| D62A | site-directed mutagenesis, inactive mutant | Pseudomonas syringae pv. tomato |
| E110D | site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme | Pseudomonas syringae pv. tomato |
| E146Q | site-directed mutagenesis, the mutant shows slightly increased activity compared to the wild-type enzyme | Pseudomonas syringae pv. tomato |
| E236Q | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Pseudomonas syringae pv. tomato |
| E303A | site-directed mutagenesis, inactive mutant | Pseudomonas syringae pv. tomato |
| E303Q | site-directed mutagenesis, inactive mutant | Pseudomonas syringae pv. tomato |
| H113A | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Pseudomonas syringae pv. tomato |
| H113Q | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Pseudomonas syringae pv. tomato |
| H306A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Pseudomonas syringae pv. tomato |
| H321K | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Pseudomonas syringae pv. tomato |
| H321L | site-directed mutagenesis, almost inactive mutant | Pseudomonas syringae pv. tomato |
| H321R | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Pseudomonas syringae pv. tomato |
| H321S | site-directed mutagenesis, almost inactive mutant | Pseudomonas syringae pv. tomato |
| L66A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Pseudomonas syringae pv. tomato |
| P220A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Pseudomonas syringae pv. tomato |
| Q301A | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Pseudomonas syringae pv. tomato |
| Q301E | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Pseudomonas syringae pv. tomato |
| R304A | site-directed mutagenesis, almost inactive mutant | Pseudomonas syringae pv. tomato |
| R304C | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Pseudomonas syringae pv. tomato |
| T302M | site-directed mutagenesis, the mutant shows slightly reduced activity compared to the wild-type enzyme | Pseudomonas syringae pv. tomato |
| T302P | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Pseudomonas syringae pv. tomato |
| V248A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Pseudomonas syringae pv. tomato |
| W109A | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Pseudomonas syringae pv. tomato |
| W109F | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Pseudomonas syringae pv. tomato |
| W109R | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Pseudomonas syringae pv. tomato |
| W61A | site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme | Pseudomonas syringae pv. tomato |
| W61N | site-directed mutagenesis, almost inactive mutant | Pseudomonas syringae pv. tomato |
| W63A | site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme | Pseudomonas syringae pv. tomato |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| raffinose | - |
Pseudomonas chlororaphis subsp. aurantiaca |  |
| raffinose | - |
Pseudomonas syringae pv. tomato | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 17.1 | - |
sucrose | sucrose hydrolysis, pH 6.0-6.6, 60°C | Pseudomonas syringae pv. tomato | |
| 18.5 | - |
sucrose | sucrose hydrolysis, pH 6.0-6.6, 60°C | Pseudomonas syringae pv. tomato | |
| 24.1 | - |
sucrose | sucrose hydrolysis, pH 6.0-6.6, 60°C | Pseudomonas chlororaphis subsp. aurantiaca | |
| 160 | - |
sucrose | sucrose hydrolysis, pH 5.8-6.6, 60°C | Pseudomonas syringae | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | - |
Bacillus subtilis | - |
- |
| extracellular | - |
Priestia megaterium | - |
- |
| extracellular | - |
Zymomonas mobilis | - |
- |
| extracellular | - |
Burkholderia cepacia | - |
- |
| extracellular | - |
Dactylis glomerata | - |
- |
| extracellular | - |
Limosilactobacillus reuteri | - |
- |
| extracellular | - |
Erwinia amylovora | - |
- |
| extracellular | - |
Lactobacillus gasseri | - |
- |
| extracellular | - |
Fructilactobacillus sanfranciscensis | - |
- |
| extracellular | - |
Gluconacetobacter diazotrophicus | - |
- |
| extracellular | - |
Limosilactobacillus panis | - |
- |
| extracellular | - |
Pseudomonas syringae pv. tomato | - |
- |
| extracellular | - |
Phleum pratense | - |
- |
| extracellular | - |
Pseudomonas chlororaphis subsp. aurantiaca | - |
- |
| extracellular | - |
Pseudomonas syringae | - |
- |
| intracellular | - |
Bacillus licheniformis | 5622 | - |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus licheniformis | W8GV60 | - |
- |
| Bacillus subtilis | - |
- |
- |
| Burkholderia cepacia | - |
- |
- |
| Dactylis glomerata | - |
- |
- |
| Erwinia amylovora | - |
- |
- |
| Fructilactobacillus sanfranciscensis | - |
- |
- |
| Gluconacetobacter diazotrophicus | Q43998 | - |
- |
| Lactobacillus gasseri | - |
- |
- |
| Limosilactobacillus panis | - |
- |
- |
| Limosilactobacillus reuteri | - |
- |
- |
| Phleum pratense | - |
- |
- |
| Priestia megaterium | - |
- |
- |
| Pseudomonas chlororaphis subsp. aurantiaca | Q93FU9 | gene lscA | - |
| Pseudomonas syringae | O68609 | pv. phaseolicola, gene lsc | - |
| Pseudomonas syringae pv. tomato | Q883P5 | pv. tomato, gene lsc2 | - |
| Pseudomonas syringae pv. tomato | Q88BN6 | pv. tomato, gene lsc3 | - |
| Pseudomonas syringae pv. tomato DC3000 | Q883P5 | pv. tomato, gene lsc2 | - |
| Pseudomonas syringae pv. tomato DC3000 | Q88BN6 | pv. tomato, gene lsc3 | - |
| Zymomonas mobilis | - |
- |
- |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 2 sucrose | - |
Bacillus subtilis | 6-kestose + D-glucose | - |
? | |
| 2 sucrose | - |
Priestia megaterium | 6-kestose + D-glucose | - |
? | |
| 2 sucrose | - |
Zymomonas mobilis | 6-kestose + D-glucose | - |
? | |
| 2 sucrose | - |
Burkholderia cepacia | 6-kestose + D-glucose | - |
? | |
| 2 sucrose | - |
Dactylis glomerata | 6-kestose + D-glucose | - |
? | |
| 2 sucrose | - |
Limosilactobacillus reuteri | 6-kestose + D-glucose | - |
? | |
| 2 sucrose | - |
Erwinia amylovora | 6-kestose + D-glucose | - |
? | |
| 2 sucrose | - |
Lactobacillus gasseri | 6-kestose + D-glucose | - |
? | |
| 2 sucrose | - |
Fructilactobacillus sanfranciscensis | 6-kestose + D-glucose | - |
? | |
| 2 sucrose | - |
Gluconacetobacter diazotrophicus | 6-kestose + D-glucose | - |
? | |
| 2 sucrose | - |
Limosilactobacillus panis | 6-kestose + D-glucose | - |
? | |
| 2 sucrose | - |
Pseudomonas syringae pv. tomato | 6-kestose + D-glucose | - |
? | |
| 2 sucrose | - |
Phleum pratense | 6-kestose + D-glucose | - |
? | |
| 2 sucrose | - |
Bacillus licheniformis | 6-kestose + D-glucose | - |
? | |
| 2 sucrose | - |
Pseudomonas chlororaphis subsp. aurantiaca | 6-kestose + D-glucose | - |
? | |
| 2 sucrose | - |
Pseudomonas syringae | 6-kestose + D-glucose | - |
? | |
| 2 sucrose | - |
Pseudomonas syringae pv. tomato DC3000 | 6-kestose + D-glucose | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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 | ? | - |
? | |
| 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
| Synonyms | Comment | Organism |
|---|---|---|
| endolevanase | - |
Bacillus licheniformis |
| LevB1 | - |
Bacillus licheniformis |
| LevU | - |
Zymomonas mobilis |
| Lsc | - |
Pseudomonas syringae |
| Lsc2 | - |
Pseudomonas syringae pv. tomato |
| Lsc3 | - |
Pseudomonas syringae pv. tomato |
| LscA | - |
Pseudomonas chlororaphis subsp. aurantiaca |
| LSD | - |
Burkholderia cepacia |
| LsdA | - |
Gluconacetobacter diazotrophicus |
| SacB | - |
Gluconacetobacter diazotrophicus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 20 | - |
transfructosylation | Pseudomonas syringae pv. tomato |
| 20 | - |
transfructosylation | Pseudomonas chlororaphis subsp. aurantiaca |
| 50 | - |
sucrose hydrolysis | Pseudomonas syringae pv. tomato |
| 60 | - |
sucrose hydrolysis | Pseudomonas syringae pv. tomato |
| 60 | - |
sucrose hydrolysis | Pseudomonas chlororaphis subsp. aurantiaca |
| 60 | - |
sucrose hydrolysis | Pseudomonas syringae |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 7.2 | - |
sucrose | sucrose hydrolysis, pH 6.0-6.6, 60°C | Pseudomonas chlororaphis subsp. aurantiaca | |
| 328.3 | - |
sucrose | sucrose hydrolysis, pH 6.0-6.6, 60°C | Pseudomonas syringae pv. tomato | |
| 504.4 | - |
sucrose | sucrose hydrolysis, pH 6.0-6.6, 60°C | Pseudomonas syringae pv. tomato | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5.8 | 6.6 | sucrose hydrolysis | Pseudomonas syringae |
| 6 | - |
sucrose hydrolysis | Pseudomonas syringae pv. tomato |
| 6 | 6.6 | sucrose hydrolysis | Pseudomonas chlororaphis subsp. aurantiaca |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 39.9 | - |
raffinose | inhibition of sucrose hydrolysis, pH 6.0, 60°C | Pseudomonas syringae pv. tomato | |
| 49 | - |
raffinose | inhibition of sucrose hydrolysis, pH 6.0, 60°C | Pseudomonas syringae pv. tomato | |
| 80.8 | - |
raffinose | inhibition of sucrose hydrolysis, pH 6.0-6.6, 60°C | Pseudomonas chlororaphis subsp. aurantiaca | |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | the catalytic triad is formed by residues Asp135, Asp309 and Glu401 | Zymomonas mobilis |
| additional information | the catalytic triad is formed by residues Asp135, Asp309 and Glu401 | Gluconacetobacter diazotrophicus |
| 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 |
| 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 |
| physiological function | in addition to fructooligosaccharides, levansucrases produce polymeric levan, degree of polymerization of which can be very high | Bacillus subtilis |
| physiological function | in addition to fructooligosaccharides, levansucrases produce polymeric levan, degree of polymerization of which can be very high | Priestia megaterium |
| physiological function | in addition to fructooligosaccharides, levansucrases produce polymeric levan, degree of polymerization of which can be very high | Zymomonas mobilis |
| physiological function | in addition to fructooligosaccharides, levansucrases produce polymeric levan, degree of polymerization of which can be very high | Burkholderia cepacia |
| physiological function | in addition to fructooligosaccharides, levansucrases produce polymeric levan, degree of polymerization of which can be very high | Limosilactobacillus reuteri |
| physiological function | in addition to fructooligosaccharides, levansucrases produce polymeric levan, degree of polymerization of which can be very high | Erwinia amylovora |
| physiological function | in addition to fructooligosaccharides, levansucrases produce polymeric levan, degree of polymerization of which can be very high | Lactobacillus gasseri |
| physiological function | in addition to fructooligosaccharides, levansucrases produce polymeric levan, degree of polymerization of which can be very high | Fructilactobacillus sanfranciscensis |
| physiological function | in addition to fructooligosaccharides, levansucrases produce polymeric levan, degree of polymerization of which can be very high | Limosilactobacillus panis |
| physiological function | in addition to fructooligosaccharides, levansucrases produce polymeric levan, degree of polymerization of which can be very high | Pseudomonas syringae pv. tomato |
| physiological function | in addition to fructooligosaccharides, levansucrases produce polymeric levan, degree of polymerization of which can be very high | Bacillus licheniformis |
| physiological function | in addition to fructooligosaccharides, levansucrases produce polymeric levan, degree of polymerization of which can be very high | Pseudomonas chlororaphis subsp. aurantiaca |
| physiological function | in addition to fructooligosaccharides, levansucrases produce polymeric levan, degree of polymerization of which can be very high | Pseudomonas syringae |
| 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 |
| 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 |
| 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 |
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