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Literature summary extracted from
- Crystal structure of the alkylsulfatase AtsK insights into the catalytic mechanism of the Fe(II) alpha-ketoglutarate-dependent dioxygenase superfamily (2004), Biochemistry, 43, 3075-3088 .
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 1.14.11.77 | - |
Pseudomonas putida |
Crystallization (Commentary)
| EC Number | Crystallization (Comment) | Organism |
|---|---|---|
| 1.14.11.77 | structure of AtsK in the apo form and in complexes with the cosubstrate 2-oxoglutarate, with 2-oxoglutarate and iron, and with 2-oxoglutarate, iron, and an alkyl sulfate ester. The overall fold of the enzyme is closely related to that of the taurine/2-oxoglutarate dioxygenase TauD and is similar to the fold observed for other members of the enzyme superfamily | Pseudomonas putida |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 1.14.11.77 | Pseudomonas putida | Q9WWU5 | - |
- |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 1.14.11.77 | alpha-ketoglutarate-dependent sulfate ester dioxygenase | - |
Pseudomonas putida |
| 1.14.11.77 | AtsK | - |
Pseudomonas putida |
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Release 2023.1 (January 2023)
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