1.14.20.15: L-threonyl-[L-threonyl-carrier protein] 4-chlorinase
This is an abbreviated version!
For detailed information about L-threonyl-[L-threonyl-carrier protein] 4-chlorinase, go to the full flat file.
Word Map on EC 1.14.20.15
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1.14.20.15
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non-heme
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ferryl
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rebound
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halide
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alphakg-dependent
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unactivated
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chemoselectivity
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alphakg
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ironii
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high-spin
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alpha-ketoglutarate-dependent
- 1.14.20.15
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non-heme
-
ferryl
-
rebound
- halide
-
alphakg-dependent
-
unactivated
-
chemoselectivity
-
alphakg
-
ironii
-
high-spin
-
alpha-ketoglutarate-dependent
Reaction
Synonyms
aliphatic halogenase, SyrB2, syringomycin biosynthesis enzyme 2, Thr3
ECTree
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General Information
General Information on EC 1.14.20.15 - L-threonyl-[L-threonyl-carrier protein] 4-chlorinase
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evolution
metabolism
additional information
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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
evolution
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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
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the enzyme is involved in syringomycin E biosynthesis
metabolism
the enzyme is involved in the biosynthesis of syringomycin
metabolism
the enzyme is involved in the syringomycin E biosynthetic pathway
metabolism
the enzyme participates in syringomycin E biosynthesis
metabolism
Streptomyces sp. OH-5093
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
metabolism
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the enzyme is involved in the syringomycin E biosynthetic pathway
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metabolism
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the enzyme participates in syringomycin E biosynthesis
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metabolism
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the enzyme is involved in syringomycin E biosynthesis
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metabolism
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the enzyme is involved in the biosynthesis of syringomycin
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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
additional information
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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
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