Organism | UniProt | Comment | Textmining |
---|---|---|---|
Pseudomonas syringae pv. syringae | Q9RBY6 | - |
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Pseudomonas syringae pv. syringae B301D | Q9RBY6 | - |
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Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | computational study of reaction at a model complex of the SyrB2 enzyme active site. The first step, alpha-ketoglutarate decarboxylation, is barrierless and exothermic, while the subsequent hydrogen abstraction step has an energetic barrier consistent with that accessible under biological conditions. The hydrogen abstraction and radical chlorination steps are strongly coupled: the barrier for the hydrogen abstraction step is reduced when carried out concomitantly with the exothermic chlorination step | Pseudomonas syringae pv. syringae | ? | - |
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additional information | computational study of reaction at a model complex of the SyrB2 enzyme active site. The first step, alpha-ketoglutarate decarboxylation, is barrierless and exothermic, while the subsequent hydrogen abstraction step has an energetic barrier consistent with that accessible under biological conditions. The hydrogen abstraction and radical chlorination steps are strongly coupled: the barrier for the hydrogen abstraction step is reduced when carried out concomitantly with the exothermic chlorination step | Pseudomonas syringae pv. syringae B301D | ? | - |
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General Information | Comment | Organism |
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metabolism | the enzyme is involved in the syringomycin E biosynthetic pathway | Pseudomonas syringae pv. syringae |