Any feedback?
Literature summary extracted from
- Purification and characterization of a cyclomaltodextrin glucanotransferase from Paenibacillus campinasensis strain H69-3 (2007), Appl. Biochem. Biotechnol., 137-140, 41-55.
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 2.4.1.19 | DTT | slight activation | Paenibacillus campinasensis |  |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 2.4.1.19 | phylogenetic tree | Paenibacillus campinasensis |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 2.4.1.19 | alpha-cyclodextrin | - |
Paenibacillus campinasensis | |
| 2.4.1.19 | beta-cyclodextrin | complete inhibition | Paenibacillus campinasensis | |
| 2.4.1.19 | EDTA | - |
Paenibacillus campinasensis | |
| 2.4.1.19 | gamma-cyclodextrin | - |
Paenibacillus campinasensis | |
| 2.4.1.19 | additional information | no or poor inhibition by PMSF, sodium azide, sodium m-arsenite, and 2-mercaptoethanol | Paenibacillus campinasensis | |
| 2.4.1.19 | SDS | - |
Paenibacillus campinasensis | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 2.4.1.19 | 1.65 | - |
maltodextrin | pH 6.5, 60°C | Paenibacillus campinasensis | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 2.4.1.19 | extracellular | - |
Paenibacillus campinasensis | - |
- |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 2.4.1.19 | Ba2+ | activates | Paenibacillus campinasensis | |
| 2.4.1.19 | Co2+ | activates | Paenibacillus campinasensis | |
| 2.4.1.19 | Mn2+ | activates | Paenibacillus campinasensis | |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 2.4.1.19 | 70000 | - |
x * 70000, SDS-PAGE | Paenibacillus campinasensis |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 2.4.1.19 | additional information | Paenibacillus campinasensis | CGTase can hydrolyze glucan chains, e.g. starch, in a manner similar to alpha-amylases, but differs in its ability to form cyclodextrins as reaction products. Cyclodextrins are formed from starch molecules through intramolecular transglycosylation, i.e. cyclization, and can be made up of 6 to 8 glucan residues, alpha-, beta-, and gamma-cyclodextrin, respectively. The enzyme is multifunctional | ? | - |
? | |
| 2.4.1.19 | additional information | Paenibacillus campinasensis H69-3 | CGTase can hydrolyze glucan chains, e.g. starch, in a manner similar to alpha-amylases, but differs in its ability to form cyclodextrins as reaction products. Cyclodextrins are formed from starch molecules through intramolecular transglycosylation, i.e. cyclization, and can be made up of 6 to 8 glucan residues, alpha-, beta-, and gamma-cyclodextrin, respectively. The enzyme is multifunctional | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 2.4.1.19 | Paenibacillus campinasensis | - |
- |
- |
| 2.4.1.19 | Paenibacillus campinasensis H69-3 | - |
- |
- |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 2.4.1.19 | native enzyme about 200fold from strain H69-3 by gel filtration, and one or two different steps of anion exchange chromatography | Paenibacillus campinasensis |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 2.4.1.19 | 347.9 | - |
purified enzyme, substrate maltodextrin | Paenibacillus campinasensis |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 2.4.1.19 | maltodextrin + glycosyl acceptor | - |
Paenibacillus campinasensis | beta-cyclodextrin + alpha-cyclodextrin + gamma-cyclodextrin | - |
? | |
| 2.4.1.19 | maltodextrin + glycosyl acceptor | - |
Paenibacillus campinasensis H69-3 | beta-cyclodextrin + alpha-cyclodextrin + gamma-cyclodextrin | - |
? | |
| 2.4.1.19 | additional information | CGTase can hydrolyze glucan chains, e.g. starch, in a manner similar to alpha-amylases, but differs in its ability to form cyclodextrins as reaction products. Cyclodextrins are formed from starch molecules through intramolecular transglycosylation, i.e. cyclization, and can be made up of 6 to 8 glucan residues, alpha-, beta-, and gamma-cyclodextrin, respectively. The enzyme is multifunctional | Paenibacillus campinasensis | ? | - |
? | |
| 2.4.1.19 | additional information | cyclization with maltodextrin as substrate | Paenibacillus campinasensis | ? | - |
? | |
| 2.4.1.19 | additional information | CGTase can hydrolyze glucan chains, e.g. starch, in a manner similar to alpha-amylases, but differs in its ability to form cyclodextrins as reaction products. Cyclodextrins are formed from starch molecules through intramolecular transglycosylation, i.e. cyclization, and can be made up of 6 to 8 glucan residues, alpha-, beta-, and gamma-cyclodextrin, respectively. The enzyme is multifunctional | Paenibacillus campinasensis H69-3 | ? | - |
? | |
| 2.4.1.19 | additional information | cyclization with maltodextrin as substrate | Paenibacillus campinasensis H69-3 | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 2.4.1.19 | ? | x * 70000, SDS-PAGE | Paenibacillus campinasensis |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 2.4.1.19 | CGTase | - |
Paenibacillus campinasensis |
| 2.4.1.19 | More | the enzyme is a member of the alpha-amylase family, family 13, of glycosyl hydrolases | Paenibacillus campinasensis |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 2.4.1.19 | 65 | - |
- |
Paenibacillus campinasensis |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 2.4.1.19 | 60 | - |
the enzyme is thermally stable up to 60°C without substrate during 1 h in the presence of 10 mM CaCl2 | Paenibacillus campinasensis |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 2.4.1.19 | 6.5 | - |
- |
Paenibacillus campinasensis |
pH Stability
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 2.4.1.19 | 6 | 11.5 | purified enzyme, stable | Paenibacillus campinasensis |
pI Value
| EC Number | Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|---|
| 2.4.1.19 | Paenibacillus campinasensis | isoelectric focusing | - |
5.3 |
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
