Activating Compound | Comment | Organism | Structure |
---|---|---|---|
DTT | slight activation | Paenibacillus campinasensis |
Cloned (Comment) | Organism |
---|---|
phylogenetic tree | Paenibacillus campinasensis |
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 Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
1.65 | - |
maltodextrin | pH 6.5, 60°C | Paenibacillus campinasensis |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
extracellular | - |
Paenibacillus campinasensis | - |
- |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Ba2+ | activates | Paenibacillus campinasensis | |
Co2+ | activates | Paenibacillus campinasensis | |
Mn2+ | activates | Paenibacillus campinasensis |
Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
---|---|---|---|
70000 | - |
x * 70000, SDS-PAGE | Paenibacillus campinasensis |
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 | UniProt | Comment | Textmining |
---|---|---|---|
Paenibacillus campinasensis | - |
- |
- |
Paenibacillus campinasensis H69-3 | - |
- |
- |
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 Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
347.9 | - |
purified enzyme, substrate maltodextrin | Paenibacillus campinasensis |
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 | Comment | Organism |
---|---|---|
? | x * 70000, SDS-PAGE | Paenibacillus campinasensis |
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 Maximum [°C] | Comment | Organism |
---|---|---|---|
65 | - |
- |
Paenibacillus campinasensis |
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
6.5 | - |
- |
Paenibacillus campinasensis |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
6 | 11.5 | purified enzyme, stable | Paenibacillus campinasensis |
Organism | Comment | pI Value Maximum | pI Value |
---|---|---|---|
Paenibacillus campinasensis | isoelectric focusing | - |
5.3 |