| Cloned (Comment) | Organism |
|---|---|
| expression in Escherichia coli | Limosilactobacillus fermentum |
| Crystallization (Comment) | Organism |
|---|---|
| homology modeling of structure | Limosilactobacillus fermentum |
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | predicted by in silico analysis, protein contains the classical Gram-positive N-terminal signal peptide of 39 amino acids | Limosilactobacillus fermentum | - |
- |
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| amylose V | Limosilactobacillus fermentum | - |
alpha-glucans with alternating alpha (1 ->3)/alpha (1->4)-linkages and with alpha(1->3,4) branching points + D-glucose | - |
? | |
| maltoheptaose | Limosilactobacillus fermentum | - |
alpha-glucans with alternating alpha (1 ->3)/alpha (1->4)-linkages and with alpha(1->3,4) branching points + D-glucose | - |
? | |
| maltohexaose | Limosilactobacillus fermentum | - |
alpha-glucans with alternating alpha (1 ->3)/alpha (1->4)-linkages and with alpha(1->3,4) branching points + D-glucose | - |
? | |
| maltopentaose | Limosilactobacillus fermentum | - |
alpha-glucans with alternating alpha (1 ->3)/alpha (1->4)-linkages and with alpha(1->3,4) branching points + D-glucose | - |
? | |
| additional information | Limosilactobacillus fermentum | GtfB displays both hydrolysis and transglycosylase (disproportionation) activity on malto-oligosaccharides of DP 6 and 7. GtfB is not active on malto-oligosaccharides of DP below 4 and shows low disproportionating activity with maltopentaose. The enzyme fails to act on sucrose, panose, nigerose, and isomalto-oligosaccharides with DP2, DP3, and DP5 | ? | - |
? |
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Limosilactobacillus fermentum | A0A1D7ZV76 | cf. EC 2.4.1.5 | - |
| Purification (Comment) | Organism |
|---|---|
| recombinant protein, purification from soluble fraction by metal chelate chromatography and anion-exchange chromatography | Limosilactobacillus fermentum |
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| amylose V | - |
Limosilactobacillus fermentum | alpha-glucans with alternating alpha (1 ->3)/alpha (1->4)-linkages and with alpha(1->3,4) branching points + D-glucose | - |
? | |
| amylose V | - |
Limosilactobacillus fermentum | alpha-glucans with alternating alpha (1 ->3)/alpha (1->4)-linkages and with alpha(1->3,4) branching points + maltose | - |
? | |
| maltoheptaose | - |
Limosilactobacillus fermentum | alpha-glucans with alternating alpha (1 ->3)/alpha (1->4)-linkages and with alpha(1->3,4) branching points + D-glucose | - |
? | |
| maltoheptaose | - |
Limosilactobacillus fermentum | alpha-glucans with alternating alpha (1 ->3)/alpha (1->4)-linkages and with alpha(1->3,4) branching points + maltose | - |
? | |
| maltohexaose | - |
Limosilactobacillus fermentum | alpha-glucans with alternating alpha (1 ->3)/alpha (1->4)-linkages and with alpha(1->3,4) branching points + D-glucose | - |
? | |
| maltohexaose | - |
Limosilactobacillus fermentum | alpha-glucans with alternating alpha (1 ->3)/alpha (1->4)-linkages and with alpha(1->3,4) branching points + maltose | - |
? | |
| maltopentaose | - |
Limosilactobacillus fermentum | alpha-glucans with alternating alpha (1 ->3)/alpha (1->4)-linkages and with alpha(1->3,4) branching points + D-glucose | - |
? | |
| maltopentaose | - |
Limosilactobacillus fermentum | alpha-glucans with alternating alpha (1 ->3)/alpha (1->4)-linkages and with alpha(1->3,4) branching points + maltose | - |
? | |
| additional information | GtfB displays both hydrolysis and transglycosylase (disproportionation) activity on malto-oligosaccharides of DP 6 and 7. GtfB is not active on malto-oligosaccharides of DP below 4 and shows low disproportionating activity with maltopentaose. The enzyme fails to act on sucrose, panose, nigerose, and isomalto-oligosaccharides with DP2, DP3, and DP5 | Limosilactobacillus fermentum | ? | - |
? |
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 180000, calculated from sequence | Limosilactobacillus fermentum |
| Synonyms | Comment | Organism |
|---|---|---|
| GtfB | - |
Limosilactobacillus fermentum |
| LACFE_CDS0221 | - |
Limosilactobacillus fermentum |
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
- |
Limosilactobacillus fermentum |
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 60 | - |
Limosilactobacillus fermentum |
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 45 | - |
enzyme shows low stability at temperatures above 45°C in 20 mM Tris-HCl buffer pH 8.0 | Limosilactobacillus fermentum |
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5.5 | - |
- |
Limosilactobacillus fermentum |
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 6 | more than 80% of maximum activity | Limosilactobacillus fermentum |
| General Information | Comment | Organism |
|---|---|---|
| physiological function | enzyme acts as a 4,3-alpha-glucanotransferase, converting amylose into a new type of alpha-glucan with alternating alpha (1 ->3)/alpha (1->4)-linkages and with alpha(1->3,4) branching points | Limosilactobacillus fermentum |