Any feedback?
Literature summary for 2.4.1.19 extracted from
- Role of Phe283 in enzymatic reaction of cyclodextrin glycosyltransferase from alkalophilic Bacillus sp.1011: Substrate binding and arrangement of the catalytic site (2004), Protein Sci., 13, 457-465.
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| hanging-drop vapour-diffusion method, crystal structure of native and acarbose-complexed mutant CGTase F283L and F283Y | Bacillus sp. (in: Bacteria) |
Protein Variants
| Protein Variants | Comment | Organism |
|---|---|---|
| F283L | starch degrading activity is similar to that of wild-type enzyme between the acidic and neutral pH ranges but decreases to 10% at pH 10.0. The pH-value of half-maximal activity at basic pH side is shifted to 8.6 from 10.0 of the wild-type. 23%-67% decrease in KM-value for 3-ketobutylidene-beta-2-chloro-4-nitrophenylmalto-pentaoside in the disproportionation reaction. The turnover-number for the disproportionating reaction at various pH conditions decreases to 1.6% to 4.4% compared with those of wild-type enzyme | Bacillus sp. (in: Bacteria) |
| F283Y | mutation decreases the enzymatic activity in the basic pH range | Bacillus sp. (in: Bacteria) |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus sp. (in: Bacteria) | - |
1011 | - |
| Bacillus sp. (in: Bacteria) 1011 | - |
1011 | - |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 4 | - |
starch degrading activity, wild-type enzyme | Bacillus sp. (in: Bacteria) |
| 7 | - |
starch degrading activity, mutant enzyme F283L | Bacillus sp. (in: Bacteria) |
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
