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Literature summary for 2.4.1.B34 extracted from
- 4,6-alpha-Glucanotransferase, a novel enzyme that structurally and functionally provides an evolutionary link between glycoside hydrolase enzyme families 13 and 70 (2011), Appl. Environ. Microbiol., 77, 8154-8163.
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression in Esdcherichia coli | Limosilactobacillus reuteri |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| D1015N | mutant enzyme shows no activity on maltooligosaccharides (maltose to maltoheptaose) | Limosilactobacillus reuteri |
| D1015N | mutation in putative nucleophile, mutant shows no activity on maltooligosaccharides | Limosilactobacillus reuteri |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Limosilactobacillus reuteri | - |
- |
- |
| Limosilactobacillus reuteri | Q5SBM0 | - |
- |
| Limosilactobacillus reuteri DSM 20016 | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
- |
Limosilactobacillus reuteri |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| amylose + maltose | the enzyme synthesizes larger saccharides with alpha1->4 and alpha1->6 glucosidic linkages | Limosilactobacillus reuteri | maltotriose + panose | panose i.e. Glc-alpha-(1->6)-maltose | ? |  |
| amylose + maltose | the enzyme synthesizes larger saccharides with alpha1->4 and alpha1->6 glucosidic linkages | Limosilactobacillus reuteri DSM 20016 | maltotriose + panose | panose i.e. Glc-alpha-(1->6)-maltose | ? | |
| Maltoheptaose | the enzyme synthesize oligosaccharides up to a degree of polymerization of at least 14. The enzyme introduces 1->6 glucosidic linkages (18%) into the final mixture of products | Limosilactobacillus reuteri | ? | - |
? | |
| Maltoheptaose | the enzyme synthesize oligosaccharides up to a degree of polymerization of at least 14. The enzyme introduces 1->6 glucosidic linkages (18%) into the final mixture of products | Limosilactobacillus reuteri DSM 20016 | ? | - |
? | |
| maltoheptaose + H2O | - |
Limosilactobacillus reuteri | ? | - |
? | |
| maltohexaose + H2O | - |
Limosilactobacillus reuteri | D-glucose + maltopentaose | first clear reaction products accumulating after 1 h, longer incubation leads to 4-substituted, 6-substituted, and terminal glucose residues at a molar ratio of 63, 17, and 20% | ? | |
| maltooligosaccharide | the enzyme uses maltooligosaccharides as donor and acceptor substrates. The enzyme disproportionates (cleaves 1->4 and synthesizes 1->6 and 1->4 glucosidic linkages) and 1->6 polymerizes maltotetraose and larger maltooligosaccharide substrates. Only linear products are made and that with increasing degrees of polymerization, more 1->6 glucosidic linkages are introduced into the final products | Limosilactobacillus reuteri | ? | - |
? | |
| maltooligosaccharide | the enzyme uses maltooligosaccharides as donor and acceptor substrates. The enzyme disproportionates (cleaves 1->4 and synthesizes 1->6 and 1->4 glucosidic linkages) and 1->6 polymerizes maltotetraose and larger maltooligosaccharide substrates. Only linear products are made and that with increasing degrees of polymerization, more 1->6 glucosidic linkages are introduced into the final products | Limosilactobacillus reuteri DSM 20016 | ? | - |
? | |
| maltopentaose + H2O | - |
Limosilactobacillus reuteri | D-glucose + maltotetraose | first clear reaction products accumulating after 1 h, longer incubation leads to 4-substituted, 6-substituted, and terminal glucose residues at a molar ratio of 63, 17, and 20% | ? | |
| Maltotetraose | - |
Limosilactobacillus reuteri | ? | - |
? | |
| additional information | the enzyme is unable to use sucrose as a donor substrate and is inactive with the sucrose analogs turanose and palatinose, with raffinose, with the DP5 and DP6 isomaltooligosaccharides and with panose | Limosilactobacillus reuteri | ? | - |
? | |
| additional information | enzyme is a alpha-glucanotransferase enzyme with disproportionating (cleaving alpha1->4 and synthesizing alpha1->6 and alpha1->4 glycosidic linkages) and alpha1->6 polymerizing types of activity on maltotetraose and larger maltooligosaccharide substrates. Only linear products are made and with increasing degrees of polymerization, more alpha1->6 glycosidic linkages are introduced into the final products, ranging from 18% in the incubation mixture to 33% in an enriched fraction. In view of its primary structure, GTFB is a member of the glycoside hydrolase 70 family. The GTFB enzyme reaction and product specificities, however, resemble those of the GH13 alpha-amylase type of enzymes | Limosilactobacillus reuteri | ? | - |
? | |
| additional information | no substrates: maltose, maltotriose, sucrose, turanose and palatinose, raffinose, panose, DP5 and DP6 isomaltooligosaccharides | Limosilactobacillus reuteri | ? | - |
? | |
| additional information | the enzyme is unable to use sucrose as a donor substrate and is inactive with the sucrose analogs turanose and palatinose, with raffinose, with the DP5 and DP6 isomaltooligosaccharides and with panose | Limosilactobacillus reuteri DSM 20016 | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| GTFB protein | - |
Limosilactobacillus reuteri |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 37 | substrate: maltotetraose | Limosilactobacillus reuteri |
| 37 | - |
- |
Limosilactobacillus reuteri |
| 37 | - |
assay at | Limosilactobacillus reuteri |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 5 | substrate: maltotetraose | Limosilactobacillus reuteri |
| 4.7 | - |
- |
Limosilactobacillus reuteri |
| 4.7 | - |
assay at | Limosilactobacillus reuteri |
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Release 2023.1 (January 2023)
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