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Literature summary for 2.4.1.10 extracted from
- A recombinant levansucrase from Bacillus licheniformis 8-37-0-1 catalyzes versatile transfructosylation reactions (2014), Process Biochem., 49, 1503-1510.
No PubMed abstract available
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene sacB, DNA and amino acid sequence determination and analysis, recombinant expression in Escherichia coli | Bacillus licheniformis |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetics | Bacillus licheniformis |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | the enzyme has a putative signal peptide in the N-terminal region,with a predicted cleavage site between the 29th and 30th aminoacids | Bacillus licheniformis | - |
- |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 51000 | - |
native enzyme, gel filtration | Bacillus licheniformis |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus licheniformis | - |
gene sacB | - |
| Bacillus licheniformis 8-37-0-1 | - |
gene sacB | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| native enzyme from strain 8-37-0-1 by ammonium sulfate fractionation, anion-exchange chromatography, and ultrafiltration to homogeneity | Bacillus licheniformis |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| additional information | - |
maximum levan formation of 7.1 mg/mL at pH 6.5 | Bacillus licheniformis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | broad transglycosylation capability of the levansucrase from Bacillus licheniformis strain 8-37-0-1, substrate specificity, overview. When using sucrose as the donor, the enzyme displays a wide range of acceptor specificity and is able to transfer fructosyl to a series of sugar acceptors including hexose, pentose, beta- or alpha-disaccharides, along with the difficult branched alcohols. Product analysis by mass and NMR spectrometry | Bacillus licheniformis | ? | - |
? |  |
| additional information | broad transglycosylation capability of the levansucrase from Bacillus licheniformis strain 8-37-0-1, substrate specificity, overview. When using sucrose as the donor, the enzyme displays a wide range of acceptor specificity and is able to transfer fructosyl to a series of sugar acceptors including hexose, pentose, beta- or alpha-disaccharides, along with the difficult branched alcohols. Product analysis by mass and NMR spectrometry | Bacillus licheniformis 8-37-0-1 | ? | - |
? | |
| sucrose + cellobiose | - |
Bacillus licheniformis | D-glucose + beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->2)-beta-D-fructofuranoside | - |
? | |
| sucrose + cellobiose | - |
Bacillus licheniformis 8-37-0-1 | D-glucose + beta-D-glucopyranosyl-(1->4)-beta-D-glucopyranosyl-(1->2)-beta-D-fructofuranoside | - |
? | |
| sucrose + D-xylose | - |
Bacillus licheniformis | D-glucose + alpha-D-xylopyranosyl-(1->2)-beta-D-fructofuranoside | - |
? | |
| sucrose + D-xylose | - |
Bacillus licheniformis 8-37-0-1 | D-glucose + alpha-D-xylopyranosyl-(1->2)-beta-D-fructofuranoside | - |
? | |
| sucrose + lactose | - |
Bacillus licheniformis | D-glucose + beta-D-galactopyranosyl-(1->4)-alpha-D-glucopyranosyl-(1->2)-beta-D-fructofuranoside | - |
? | |
| sucrose + lactose | - |
Bacillus licheniformis 8-37-0-1 | D-glucose + beta-D-galactopyranosyl-(1->4)-alpha-D-glucopyranosyl-(1->2)-beta-D-fructofuranoside | - |
? | |
| sucrose + maltose | - |
Bacillus licheniformis | D-glucose + alpha-D-glucopyranosyl-(1->4)-alpha-D-glucopyranosyl-(1->2)-beta-D-fructofuranoside | - |
? | |
| sucrose + maltose | - |
Bacillus licheniformis 8-37-0-1 | D-glucose + alpha-D-glucopyranosyl-(1->4)-alpha-D-glucopyranosyl-(1->2)-beta-D-fructofuranoside | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 51000, SDS-PAGE | Bacillus licheniformis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
native and recombinant enzyme | Bacillus licheniformis |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 20 | 60 | native and recombinant enzymes lose 80% activities at temperatures below 20°C and are nearly inactive at above 60°C | Bacillus licheniformis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | - |
native and recombinant enzyme | Bacillus licheniformis |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 8.5 | native and recombinant enzymes, 50% of maximal activity at pH 4.0 and pH 8.5 | Bacillus licheniformis |
General Information
| General Information | Comment | Organism |
|---|---|---|
| additional information | the recombinant enzyme shows similar biochemical properties to the native one | Bacillus licheniformis |
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