Any feedback?
Literature summary for 2.4.1.19 extracted from
- Altered product specificity of a cyclodextrin glycosyltransferase by molecular imprinting with cyclomaltododecaose (2010), J. Mol. Recognit., 23, 480-485.
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | manipulation of the enzyme by molecular imprinting to preferentially produce large-ring cyclodextrins, overview | Paenibacillus sp. |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| additional information | molecular imprinting of the CGTase with cyclomaltododecaose, CD12, as the template molecule followed by cross-linking of the derivatized protein stabilizes the enzyme, overview | Paenibacillus sp. |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Paenibacillus sp. | - |
- |
- |
| Paenibacillus sp. A11 | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| native enzyme by starch adsorption and anion exchange chromatography | Paenibacillus sp. |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| amylose | catalyzes the conversion of amylose to cyclodextrins, circular alpha-(1,4)-linked glucopyranose oligosaccharides of different ring sizes, the cyclodextrin containing 12 alpha-D-glucopyranose residues is preferentially synthesized by the enzyme. Interactions at oligosaccharide-binding subsites located close to the catalytic site apparently play a more important role in the determination of the size of the cyclodextrin formed | Paenibacillus sp. | alpha-cyclodextrin | product identification by amperometric detection, overview | ? |  |
| amylose | catalyzes the conversion of amylose to cyclodextrins, circular alpha-(1,4)-linked glucopyranose oligosaccharides of different ring sizes, the cyclodextrin containing 12 alpha-D-glucopyranose residues is preferentially synthesized by the enzyme. Interactions at oligosaccharide-binding subsites located close to the catalytic site apparently play a more important role in the determination of the size of the cyclodextrin formed | Paenibacillus sp. A11 | alpha-cyclodextrin | product identification by amperometric detection, overview | ? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CGTase | - |
Paenibacillus sp. |
| cyclodextrin glycosyltransferase | - |
Paenibacillus sp. |
| More | the enzyme belongs to the glycoside hydrolase family 13 | Paenibacillus sp. |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | - |
- |
Paenibacillus sp. |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 40 | 60 | activity measurement at | Paenibacillus sp. |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6 | - |
assay at | Paenibacillus sp. |
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
