Any feedback?
Literature summary for 2.4.1.25 extracted from
- Enzymatic synthesis of dimaltosyl-beta-cyclodextrin via a transglycosylation reaction using TreX, a Sulfolobus solfataricus P2 debranching enzyme (2008), Biochem. Biophys. Res. Commun., 366, 98-103.
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | the enzyme is useful in the enzymatic synthesis of dimaltosyl-beta-cyclodextrin via a transglycosylation reaction | Saccharolobus solfataricus |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| expression of His-tagged enzyme in Escherichia coli strain MC1061 | Saccharolobus solfataricus |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| beta-cyclodextrin | a mixed-type inhibitor | Saccharolobus solfataricus |  |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1.591 | - |
maltosyl-beta-cyclodextrin | pH 5.5, 75°C | Saccharolobus solfataricus | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Saccharolobus solfataricus | - |
gene treX | - |
| Saccharolobus solfataricus P2 | - |
gene treX | - |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged enzyme from Escherichia coli strain MC1061 by nickel affinity chromatography | Saccharolobus solfataricus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| maltose + beta-cyclodextrin | condensation reaction mechanism, overview | Saccharolobus solfataricus | 6-O-alpha-maltosyl-beta-cyclodextrin | mass spectrometric product identification | ? | |
| maltose + beta-cyclodextrin | condensation reaction mechanism, overview | Saccharolobus solfataricus P2 | 6-O-alpha-maltosyl-beta-cyclodextrin | mass spectrometric product identification | ? | |
| maltose + maltosyl-beta-cyclodextrin | - |
Saccharolobus solfataricus | ? | - |
? | |
| maltose + maltosyl-beta-cyclodextrin | - |
Saccharolobus solfataricus P2 | ? | - |
? | |
| additional information | synthesis of di-O-alpha-maltosyl-beta-cyclodextrin from 6-O-alpha-maltosyl-beta-cyclodextrin via a transglycosylation reaction, TreX transfers the maltosyl residue of a G2-beta-cyclodextrin to another molecule of G2-beta-cyclodextrin by forming an alpha-1,6-glucosidic linkage. TreX shows specificity for a branched glucosyl chain bigger than DP2 and no activity toward glucosyl-beta-cyclodextrin, transglycosylation reaction mechanism, overview | Saccharolobus solfataricus | ? | - |
? | |
| additional information | synthesis of di-O-alpha-maltosyl-beta-cyclodextrin from 6-O-alpha-maltosyl-beta-cyclodextrin via a transglycosylation reaction, TreX transfers the maltosyl residue of a G2-beta-cyclodextrin to another molecule of G2-beta-cyclodextrin by forming an alpha-1,6-glucosidic linkage. TreX shows specificity for a branched glucosyl chain bigger than DP2 and no activity toward glucosyl-beta-cyclodextrin, transglycosylation reaction mechanism, overview | Saccharolobus solfataricus P2 | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| debranching enzyme | - |
Saccharolobus solfataricus |
| TreX | - |
Saccharolobus solfataricus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 70 | 75 | assay at | Saccharolobus solfataricus |
Turnover Number [1/s]
| Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0113 | - |
maltosyl-beta-cyclodextrin | pH 5.5, 75°C | Saccharolobus solfataricus | |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5.5 | - |
assay at | Saccharolobus solfataricus |
Ki Value [mM]
| Ki Value [mM] | Ki Value maximum [mM] | Inhibitor | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 0.0556 | - |
beta-cyclodextrin | pH 5.5, 75°C, recombinant His-tagged enzyme | Saccharolobus solfataricus | |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2026.1 (March 2026)
Legal
Curated at
Member of
![DSMZ Digital Diversity]()
![Global Core Biodata Resource]()
![ELIXIR Core Data Resource]()
![German Network for Bioinformatics Infrastructure]()
