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Literature summary for 1.14.15.3 extracted from
- Molecular modelling and quantum biochemistry computations of a naturally occurring bioremediation enzyme Alkane hydroxylase from Pseudomonas putida P1 (2017), J. Mol. Graph. Model., 77, 232-239 .
Crystallization (Commentary)
| Crystallization (Comment) | Organism |
|---|---|
| homology miodeling of structure and docking of octane, octanol and 1-octyne. Residues Ala53, Trp55, Val15 and Tyr339 of AlkB are involved in the octane uptake/binding, octanol binding/exit, and the 1-octyne uptake/binding | Pseudomonas putida |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Pseudomonas putida | Q9WWW6 | - |
- |
| Pseudomonas putida P1 | Q9WWW6 | - |
- |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| AlkB | - |
Pseudomonas putida |
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Release 2023.1 (January 2023)
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