Protein Variants | Comment | Organism |
---|---|---|
H49V/H539V | the mutant enzyme dissociates into dimers faster than the wild-type enzyme at both pH 6.0 and 7.0 | Bacillus sp. (in: Bacteria) |
H49V/H89V/H539V | the mutant enzyme dissociates into dimers faster than the wild-type enzyme at both pH 6.0 and 7.0 | Bacillus sp. (in: Bacteria) |
KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
0.454 | - |
beta-cyclodextrin | pH 7.0 | Bacillus sp. (in: Bacteria) | |
0.889 | - |
beta-cyclodextrin | pH 6.0 | Bacillus sp. (in: Bacteria) |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Bacillus sp. (in: Bacteria) | - |
I-5 | - |
Bacillus sp. (in: Bacteria) I-5 | - |
I-5 | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
beta-cyclodextrin + H2O | - |
Bacillus sp. (in: Bacteria) | ? | - |
? | |
beta-cyclodextrin + H2O | - |
Bacillus sp. (in: Bacteria) I-5 | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dodecamer | exists exclusively as dodecamer at pH 7.0, forming an assembly of six 3D domain-swapped dimeric subunit. At pH 5.0-6.0 the enzyme is present as a dimer. Above pH 6.5 the dodecameric form is predominant. No dissociation of the dodecamer at pH 7.0 and above. Dissociation of wild-type CDase I-5 proceeds very fast at pH 7.0 in presence of 0.2-1.0 M of KCl. The mutant enzyme H49V/H89V/H539V dissociates into dimers faster than the wild-type enzyme at both pH 6.0 and 7.0 | Bacillus sp. (in: Bacteria) |
Synonyms | Comment | Organism |
---|---|---|
CDase I-5 | - |
Bacillus sp. (in: Bacteria) |
Turnover Number Minimum [1/s] | Turnover Number Maximum [1/s] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|
3 | - |
beta-cyclodextrin | pH 7.0 | Bacillus sp. (in: Bacteria) | |
8.5 | - |
beta-cyclodextrin | pH 6.0 | Bacillus sp. (in: Bacteria) | |
78.2 | - |
beta-cyclodextrin | pH 7.0 | Bacillus sp. (in: Bacteria) |