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Literature summary for 2.4.1.19 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
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| DTT | slight activation | Paenibacillus campinasensis |  |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| phylogenetic tree | Paenibacillus campinasensis |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| alpha-cyclodextrin | - |
Paenibacillus campinasensis | |
| beta-cyclodextrin | complete inhibition | Paenibacillus campinasensis | |
| EDTA | - |
Paenibacillus campinasensis | |
| gamma-cyclodextrin | - |
Paenibacillus campinasensis | |
| additional information | no or poor inhibition by PMSF, sodium azide, sodium m-arsenite, and 2-mercaptoethanol | Paenibacillus campinasensis | |
| SDS | - |
Paenibacillus campinasensis | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| 1.65 | - |
maltodextrin | pH 6.5, 60°C | Paenibacillus campinasensis | |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | - |
Paenibacillus campinasensis | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ba2+ | activates | Paenibacillus campinasensis | |
| Co2+ | activates | Paenibacillus campinasensis | |
| Mn2+ | activates | Paenibacillus campinasensis | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 70000 | - |
x * 70000, SDS-PAGE | Paenibacillus campinasensis |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| 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 | ? | - |
? | |
| 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
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Paenibacillus campinasensis | - |
- |
- |
| Paenibacillus campinasensis H69-3 | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| 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]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 347.9 | - |
purified enzyme, substrate maltodextrin | Paenibacillus campinasensis |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| maltodextrin + glycosyl acceptor | - |
Paenibacillus campinasensis | beta-cyclodextrin + alpha-cyclodextrin + gamma-cyclodextrin | - |
? | |
| maltodextrin + glycosyl acceptor | - |
Paenibacillus campinasensis H69-3 | beta-cyclodextrin + alpha-cyclodextrin + gamma-cyclodextrin | - |
? | |
| 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 | ? | - |
? | |
| additional information | cyclization with maltodextrin as substrate | Paenibacillus campinasensis | ? | - |
? | |
| 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 | ? | - |
? | |
| additional information | cyclization with maltodextrin as substrate | Paenibacillus campinasensis H69-3 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 70000, SDS-PAGE | Paenibacillus campinasensis |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| CGTase | - |
Paenibacillus campinasensis |
| More | the enzyme is a member of the alpha-amylase family, family 13, of glycosyl hydrolases | Paenibacillus campinasensis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 65 | - |
- |
Paenibacillus campinasensis |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 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
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6.5 | - |
- |
Paenibacillus campinasensis |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 6 | 11.5 | purified enzyme, stable | Paenibacillus campinasensis |
pI Value
| Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|
| Paenibacillus campinasensis | isoelectric focusing | - |
5.3 |
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