EC Number   |
General Information |
Reference |
|---|
   1.14.20.15 | evolution |
the enzyme SyrB2 from Pseudomonas syringae B301D is the founding member of the Fe/2OG aliphatic halogenases. In SyrB2, the sequence position that normally provides the carboxylate of the canonical facial triad of protein ligands is occupied by an alanine (Ala118), and the co-substrate, chloride (Cl?), occupies the vacated site in the iron coordination sphere.32 Fe/2OG halogenases mechanistically parallel the hydroxylases in that both employ ferryl intermediates as the H-abstracting species |
-, 734033 |
| 1.14.20.15 | metabolism |
the enzyme is involved in syringomycin E biosynthesis |
-, 748759 |
| 1.14.20.15 | metabolism |
the enzyme is involved in the biosynthesis of syringomycin |
-, 747733 |
| 1.14.20.15 | metabolism |
the enzyme is involved in the syringomycin E biosynthetic pathway |
-, 746579, 748021 |
| 1.14.20.15 | metabolism |
the enzyme participates in syringomycin E biosynthesis |
-, 747063, 749157 |
| 1.14.20.15 | metabolism |
thr3 from Streptomyces sp. OH-5093 can replace the halogenase gene syrB2 in the biosynthesis of syringomycin, by functional complementation of the mutant Pseudomonas syringae pv. syringae strain BR135A1 inactivated in syrB2 |
747733 |
| 1.14.20.15 | more |
other factors might be involved in directing the halogenation outcome and the likelihood that proper substrate positioning is also essential to avoidance of hydroxylation in the other types of Fe/2OG-oxygenase reactivity, direct probing the positions of the various target C-H bonds relative to the iron center, coupling of NO, overview |
-, 734033 |
