Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | cell-associated | Limosilactobacillus reuteri | - |
- |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Limosilactobacillus reuteri | - |
- |
- |
Limosilactobacillus reuteri | A0A0U5F702 | - |
- |
Limosilactobacillus reuteri 121 | A0A0U5F702 | - |
- |
Limosilactobacillus reuteri DSM20016 | - |
- |
- |
Limosilactobacillus reuteri LMG 18388 | A0A0U5F702 | - |
- |
Limosilactobacillus reuteri ML1 | - |
- |
- |
Limosilactobacillus reuteri TMW1.106 | - |
- |
- |
no activity in Lactobacillus reuteri strain 180 | - |
- |
- |
no activity in Lactobacillus reuteri strain ATCC55730 | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
culture condition:maltodextrin-grown cell | - |
Limosilactobacillus reuteri | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | structure of the IMMP product of 4,6-alpha-GTase (e.g. GtfB) with maltodextrins, overview. NMR analysis of EPS samples produced by the GtfB enzyme in vitro and by Lactobacillus reuteri 121 cells in vivo. Enzyme reaction product analysis | Limosilactobacillus reuteri | ? | - |
- |
|
additional information | structure of the IMMP product of 4,6-alpha-GTase Gtf106b with maltodextrins, overview. Enzyme reaction product analysis | Limosilactobacillus reuteri | ? | - |
- |
|
additional information | structure of the IMMP product of 4,6-alpha-GTase GtfML4 with maltodextrins, overview. Enzyme reaction product analysis | Limosilactobacillus reuteri | ? | - |
- |
|
additional information | structure of the IMMP product of 4,6-alpha-GTase GtfW with maltodextrins, overview. Enzyme reaction product analysis | Limosilactobacillus reuteri | ? | - |
- |
|
additional information | structure of the IMMP product of 4,6-alpha-GTase Gtf106b with maltodextrins, overview. Enzyme reaction product analysis | Limosilactobacillus reuteri ML1 | ? | - |
- |
|
additional information | structure of the IMMP product of 4,6-alpha-GTase GtfML4 with maltodextrins, overview. Enzyme reaction product analysis | Limosilactobacillus reuteri ML1 | ? | - |
- |
|
additional information | structure of the IMMP product of 4,6-alpha-GTase GtfW with maltodextrins, overview. Enzyme reaction product analysis | Limosilactobacillus reuteri ML1 | ? | - |
- |
|
additional information | structure of the IMMP product of 4,6-alpha-GTase Gtf106b with maltodextrins, overview. Enzyme reaction product analysis | Limosilactobacillus reuteri DSM20016 | ? | - |
- |
|
additional information | structure of the IMMP product of 4,6-alpha-GTase GtfML4 with maltodextrins, overview. Enzyme reaction product analysis | Limosilactobacillus reuteri DSM20016 | ? | - |
- |
|
additional information | structure of the IMMP product of 4,6-alpha-GTase GtfW with maltodextrins, overview. Enzyme reaction product analysis | Limosilactobacillus reuteri DSM20016 | ? | - |
- |
|
additional information | structure of the IMMP product of 4,6-alpha-GTase (e.g. GtfB) with maltodextrins, overview. NMR analysis of EPS samples produced by the GtfB enzyme in vitro and by Lactobacillus reuteri 121 cells in vivo. Enzyme reaction product analysis | Limosilactobacillus reuteri 121 | ? | - |
- |
|
additional information | structure of the IMMP product of 4,6-alpha-GTase Gtf106b with maltodextrins, overview. Enzyme reaction product analysis | Limosilactobacillus reuteri TMW1.106 | ? | - |
- |
|
additional information | structure of the IMMP product of 4,6-alpha-GTase GtfML4 with maltodextrins, overview. Enzyme reaction product analysis | Limosilactobacillus reuteri TMW1.106 | ? | - |
- |
|
additional information | structure of the IMMP product of 4,6-alpha-GTase GtfW with maltodextrins, overview. Enzyme reaction product analysis | Limosilactobacillus reuteri TMW1.106 | ? | - |
- |
|
additional information | structure of the IMMP product of 4,6-alpha-GTase (e.g. GtfB) with maltodextrins, overview. NMR analysis of EPS samples produced by the GtfB enzyme in vitro and by Lactobacillus reuteri 121 cells in vivo. Enzyme reaction product analysis | Limosilactobacillus reuteri LMG 18388 | ? | - |
- |
Synonyms | Comment | Organism |
---|---|---|
4,6-alpha-GTase | - |
Limosilactobacillus reuteri |
Gtf106b | - |
Limosilactobacillus reuteri |
GtfB | - |
Limosilactobacillus reuteri |
GtfML4 | - |
Limosilactobacillus reuteri |
GtfW | - |
Limosilactobacillus reuteri |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
37 | - |
assay at | Limosilactobacillus reuteri |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
5 | - |
assay at | Limosilactobacillus reuteri |
General Information | Comment | Organism |
---|---|---|
evolution | the enzyme belongs to the GH70 family | Limosilactobacillus reuteri |
physiological function | Lactobacillus reuteri strain 121 possesses a 4,6-alpha-glucanotransferase (4,6-alpha-GTase) enzyme. Purified 4,6-alpha-GTase GtfB acts on starches (hydrolysates), cleaving alpha(1->4) linkages and synthesizing alpha(1->6) linkages, yielding isomalto-/maltopolysaccharides (IMMP). Lactobacillus reuteri cells with these extracellular, cell-associated 4,6-alpha-GTases synthesize homoexopolysaccharides (EPS, alpha-glucan) from starches (hydrolysates). NMR, SEC, and enzymatic hydrolysis of EPS synthesized by Lactobacillus reuteri srain 121 cells show that the EPS have similar linkage specificities but generally are much bigger in size than IMMP produced by the GtfB enzyme. 4,6-alpha-GTase enzymes are essential for EPS formation by Lactobacillus reuteri in vivo | Limosilactobacillus reuteri |
physiological function | Lactobacillus reuteri strain DSM20016 possesses a 4,6-alpha-glucanotransferase (4,6-alpha-GTase) enzyme. Purified 4,6-alpha-GTase Gtf106b acts on starches (hydrolysates), cleaving alpha(1->4) linkages and synthesizing alpha(1->6) linkages, yielding isomalto-/maltopolysaccharides (IMMP). Lactobacillus reuteri cells with extracellular, cell-associated 4,6-alpha-GTases synthesize homoexopolysaccharides (EPS, alpha-glucan) from starches (hydrolysates). 4,6-alpha-GTase enzymes are essential for EPS Fformation by Lactobacillus reuteri in vivo | Limosilactobacillus reuteri |
physiological function | Lactobacillus reuteri strain DSM20016 possesses a 4,6-alpha-glucanotransferase (4,6-alpha-GTase) enzyme. Purified 4,6-alpha-GTase GtfML4 acts on starches (hydrolysates), cleaving alpha(1->4) linkages and synthesizing alpha(1->6) linkages, yielding isomalto-/maltopolysaccharides (IMMP). Lactobacillus reuteri cells with extracellular, cell-associated 4,6-alpha-GTases synthesize homoexopolysaccharides (EPS, alpha-glucan) from starches (hydrolysates). 4,6-alpha-GTase enzymes are essential for EPS formation by Lactobacillus reuteri in vivo | Limosilactobacillus reuteri |
physiological function | Lactobacillus reuteri strain DSM20016 possesses a 4,6-alpha-glucanotransferase (4,6-alpha-GTase) enzyme. Purified 4,6-alpha-GTase GtfW acts on starches (hydrolysates), cleaving alpha(1->4) linkages and synthesizing alpha(1->6) linkages, yielding isomalto-/maltopolysaccharides (IMMP). Lactobacillus reuteri cells with extracellular, cell-associated 4,6-alpha-GTases synthesize homoexopolysaccharides (EPS, alpha-glucan) from starches (hydrolysates). 4,6-alpha-GTase enzymes are essential for EPS formation by Lactobacillus reuteri in vivo | Limosilactobacillus reuteri |