Crystallization (Comment) | Organism |
---|---|
crystallographic analyses of DesB shows that gallate is recognized by several hydrogen bonds. Three groups of the hydrogen bonds recognize a substrate and place the substrate in a productive arrangement | Sphingobium sp. SYK-6 |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | the catalytic reaction of the extradiol dioxygenase DesB requires the shift of the Fe(II) ion, leading to the bidentate coordination of the substrate to the Fe(II) ion | Sphingobium sp. SYK-6 |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Sphingobium sp. SYK-6 | G2IKE5 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
3,4,5-trihydroxybenzoate + O2 | DesB has strict substrate specificity for 3,4,5-trihydroxybenzoate (gallate). Biochemical and structural study show the substrate recognition and catalytic mechanisms of extradiol dioxygenase DesB. Mutational analysis reveals that His124 and His192 in the active site are essential to the catalytic reaction of the extradiol dioxygenase DesB. His124, which interacts with OH(4) of the bound gallate, seems to contribute to proper positioning of the substrate in the active site. His192, which is located close to OH (3) of the gallate, is likely to serve as the catalytic base. Glu377' interacts with OH(5) of the gallate and seems to play a critical role in the substrate specificity | Sphingobium sp. SYK-6 | (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate | - |
? |
Synonyms | Comment | Organism |
---|---|---|
DesB | - |
Sphingobium sp. SYK-6 |
Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
---|---|---|---|
30 | - |
assay at | Sphingobium sp. SYK-6 |
pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
assay at | Sphingobium sp. SYK-6 |