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Literature summary for 1.14.20.15 extracted from

  • Kulik, H.J.; Blasiak, L.C.; Marzari, N.; Drennan, C.L.
    First-principles study of non-heme Fe(II) halogenase SyrB2 reactivity (2009), J. Am. Chem. Soc., 131, 14426-14433 .
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Pseudomonas syringae pv. syringae Q9RBY6
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Pseudomonas syringae pv. syringae B301D Q9RBY6
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Substrates and Products (Substrate)

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

General Information Comment Organism
metabolism the enzyme is involved in the syringomycin E biosynthetic pathway Pseudomonas syringae pv. syringae