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Information on EC 1.14.20.15 - L-threonyl-[L-threonyl-carrier protein] 4-chlorinase
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1.14.20.15 L-threonyl-[L-threonyl-carrier protein] 4-chlorinaseIUBMB Comments
The enzyme, characterized from the bacterium Pseudomonas syringae, participates in syringomycin E biosynthesis. The enzyme is a specialized iron(II)/2-oxoglutarate-dependent oxygenase that catalyses the chlorination of its substrate in a reaction that requires oxygen, chloride ions, ferrous iron and 2-oxoglutarate.
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Word Map
- 1.14.20.15
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non-heme
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ferryl
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rebound
- 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
The enzyme appears in viruses and cellular organisms
Reaction Schemes
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=
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an L-threonyl-[L-threonyl-carrier protein]
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+
=
a 4-chloro-L-threonyl-[L-threonyl-carrier protein]
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Synonyms
syrb2, aliphatic halogenase, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
aliphatic halogenase
SyrB2
syringomycin biosynthesis enzyme 2
SyrB2
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SyrB2
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
an L-threonyl-[L-threonyl-carrier protein] + 2-oxoglutarate + O2 + Cl- = a 4-chloro-L-threonyl-[L-threonyl-carrier protein] + succinate + CO2 + H2O
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SYSTEMATIC NAME
IUBMB Comments
L-threonyl-[L-threonyl-carrier protein],2-oxoglutarate:oxygen oxidoreductase (4-halogenating)
The enzyme, characterized from the bacterium Pseudomonas syringae, participates in syringomycin E biosynthesis. The enzyme is a specialized iron(II)/2-oxoglutarate-dependent oxygenase that catalyses the chlorination of its substrate in a reaction that requires oxygen, chloride ions, ferrous iron and 2-oxoglutarate.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-threonyl-[L-threonyl-carrier protein SyrB1] + 2-oxoglutarate + O2 + 2 Cl-
4,4-dichloro-L-threonyl-[L-threonyl-carrier protein SyrB1] + succinate + CO2 + H2O
L-threonyl-[L-threonyl-carrier protein SyrB1] + 2-oxoglutarate + O2 + Br-
4-bromo-L-threonyl-[L-threonyl-carrier protein SyrB1] + succinate + CO2 + H2O
L-threonyl-[L-threonyl-carrier protein SyrB1] + 2-oxoglutarate + O2 + Cl-
4-chloro-L-threonyl-[L-threonyl-carrier protein SyrB1] + succinate + CO2 + H2O
L-threonyl-[L-threonyl-carrier protein SyrB1] + 2-oxoglutarate + O2 + 2 Cl-
4,4-dichloro-L-threonyl-[L-threonyl-carrier protein SyrB1] + succinate + CO2 + H2O
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-
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?
L-threonyl-[L-threonyl-carrier protein SyrB1] + 2-oxoglutarate + O2 + 2 Cl-
4,4-dichloro-L-threonyl-[L-threonyl-carrier protein SyrB1] + succinate + CO2 + H2O
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-
-
?
L-threonyl-[L-threonyl-carrier protein SyrB1] + 2-oxoglutarate + O2 + Br-
4-bromo-L-threonyl-[L-threonyl-carrier protein SyrB1] + succinate + CO2 + H2O
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-
-
?
L-threonyl-[L-threonyl-carrier protein SyrB1] + 2-oxoglutarate + O2 + Br-
4-bromo-L-threonyl-[L-threonyl-carrier protein SyrB1] + succinate + CO2 + H2O
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-
-
?
L-threonyl-[L-threonyl-carrier protein SyrB1] + 2-oxoglutarate + O2 + Cl-
4-chloro-L-threonyl-[L-threonyl-carrier protein SyrB1] + succinate + CO2 + H2O
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?
L-threonyl-[L-threonyl-carrier protein SyrB1] + 2-oxoglutarate + O2 + Cl-
4-chloro-L-threonyl-[L-threonyl-carrier protein SyrB1] + succinate + CO2 + H2O
the enzyme participates in syringomycin E biosynthesis
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-
?
L-threonyl-[L-threonyl-carrier protein SyrB1] + 2-oxoglutarate + O2 + Cl-
4-chloro-L-threonyl-[L-threonyl-carrier protein SyrB1] + succinate + CO2 + H2O
substrate positioning controls the partition between halogenation and hydroxylation
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-
?
L-threonyl-[L-threonyl-carrier protein SyrB1] + 2-oxoglutarate + O2 + Cl-
4-chloro-L-threonyl-[L-threonyl-carrier protein SyrB1] + succinate + CO2 + H2O
the enzyme can not chlorinate free L-Thr or the small molecule surrogate for L-Thr-S-SyrB1, L-Thr-S-N-acetylcysteamine
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?
L-threonyl-[L-threonyl-carrier protein SyrB1] + 2-oxoglutarate + O2 + Cl-
4-chloro-L-threonyl-[L-threonyl-carrier protein SyrB1] + succinate + CO2 + H2O
the substrate consists of L-Thr tethered via thioester linkage to a covalently bound phosphopantetheine cofactor of a carrier protein, SyrB1. Without an appended amino acid, SyrB1 does not trigger formation of the chloroferryl intermediate state in SyrB2, even in the presence of free L-Thr or its analogues, but SyrB1 charged either by L-Thr or by any of several non-native amino acids does trigger the reaction by as much as 8000fold (for L-Thr-S-SyrB1). Triggering efficacy is sensitive to the structures of both the amino acid and the carrier protein, being diminished by 5-20fold when the native L-Thr is replaced by another amino acid and by about 40fold when SyrB1 is replaced by a heterologous carrier protein, CytC2. The SyrB2 chloroferryl state exhibits unprecedented stability (t1/2 = 30-110 min at 0°C), can be trapped in high concentration and purity by manual freezing without a cryosolvent, and represents an ideal target for structural characterization
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?
L-threonyl-[L-threonyl-carrier protein SyrB1] + 2-oxoglutarate + O2 + Cl-
4-chloro-L-threonyl-[L-threonyl-carrier protein SyrB1] + succinate + CO2 + H2O
the enzyme participates in syringomycin E biosynthesis
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-
?
L-threonyl-[L-threonyl-carrier protein SyrB1] + 2-oxoglutarate + O2 + Cl-
4-chloro-L-threonyl-[L-threonyl-carrier protein SyrB1] + succinate + CO2 + H2O
the substrate consists of L-Thr tethered via thioester linkage to a covalently bound phosphopantetheine cofactor of a carrier protein, SyrB1. Without an appended amino acid, SyrB1 does not trigger formation of the chloroferryl intermediate state in SyrB2, even in the presence of free L-Thr or its analogues, but SyrB1 charged either by L-Thr or by any of several non-native amino acids does trigger the reaction by as much as 8000fold (for L-Thr-S-SyrB1). Triggering efficacy is sensitive to the structures of both the amino acid and the carrier protein, being diminished by 5-20fold when the native L-Thr is replaced by another amino acid and by about 40fold when SyrB1 is replaced by a heterologous carrier protein, CytC2. The SyrB2 chloroferryl state exhibits unprecedented stability (t1/2 = 30-110 min at 0°C), can be trapped in high concentration and purity by manual freezing without a cryosolvent, and represents an ideal target for structural characterization
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?
L-threonyl-[L-threonyl-carrier protein SyrB1] + 2-oxoglutarate + O2 + Cl-
4-chloro-L-threonyl-[L-threonyl-carrier protein SyrB1] + succinate + CO2 + H2O
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?
L-threonyl-[L-threonyl-carrier protein SyrB1] + 2-oxoglutarate + O2 + Cl-
4-chloro-L-threonyl-[L-threonyl-carrier protein SyrB1] + succinate + CO2 + H2O
the enzyme participates in syringomycin E biosynthesis
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-
?
L-threonyl-[L-threonyl-carrier protein SyrB1] + 2-oxoglutarate + O2 + Cl-
4-chloro-L-threonyl-[L-threonyl-carrier protein SyrB1] + succinate + CO2 + H2O
the enzyme can not chlorinate free L-Thr or the small molecule surrogate for L-Thr-S-SyrB1, L-Thr-S-N-acetylcysteamine
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?
additional information
?
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the enzyme catalyzes chlorination of the C4 position of L-threonine appended via a thioester linkage to the phosphopantetheine arm of the companion aminoacyl carrier protein, SyrB1. The native substrate of SyrB2, Thr, is almost exclusively chlorinated, although non-native substrates undergo hydroxylation as well as chlorination. SyrB2 represents an intriguing case in which two different reaction outcomes catalyzed by this enzyme family (hydroxylation and halogenation) are observed
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?
additional information
?
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non-native substrates undergo hydroxylation as well as chlorination. The cis-chloroferryl complex in enzyme SyrB2 reacts more rapidly with SyrB1 presenting L-aminobutyric acid or L-norvaline than with L-threonine. Selectivity for chlorination is also strongly modulated: L-threonine is almost exclusively chlorinated, L-aminobutyric acid is chlorinated and hydroxylated at C4 to similar extents, and L-norvaline is predominately hydroxylated at the C5 position. The differential reactivity observed for the different substrates might arise primarily from substrate-protein interactions that impact the partition between the axial and equatorial coordination isomers of the ferryl complex rather than from substrate positioning per se
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?
additional information
?
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the enzyme catalyzes chlorination of the C4 position of L-threonine appended via a thioester linkage to the phosphopantetheine arm of the companion aminoacyl carrier protein, SyrB1. The native substrate of SyrB2, Thr, is almost exclusively chlorinated, although non-native substrates undergo hydroxylation as well as chlorination. SyrB2 represents an intriguing case in which two different reaction outcomes catalyzed by this enzyme family (hydroxylation and halogenation) are observed
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?
additional information
?
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non-native substrates undergo hydroxylation as well as chlorination. The cis-chloroferryl complex in enzyme SyrB2 reacts more rapidly with SyrB1 presenting L-aminobutyric acid or L-norvaline than with L-threonine. Selectivity for chlorination is also strongly modulated: L-threonine is almost exclusively chlorinated, L-aminobutyric acid is chlorinated and hydroxylated at C4 to similar extents, and L-norvaline is predominately hydroxylated at the C5 position. The differential reactivity observed for the different substrates might arise primarily from substrate-protein interactions that impact the partition between the axial and equatorial coordination isomers of the ferryl complex rather than from substrate positioning per se
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additional information
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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
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additional information
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mechanism of the chlorination reaction of SyrB2 is studied with computational methods. The structure of the SyrB2-substrate complex is modeled with the use of molecular docking procedures. DFT calculations performed with a model involving all first-shell and several second-shell ligands of iron provide energy profiles, which suggest that the two forms of the oxoferryl species can both participate in the reaction. Relative energies of transition states for C-H bond cleavage by these two reactive oxoferryl species dictate the product specificity. The identity of the two oxoferryl species observed in the experimental works is proposed and confirmed by theoretical calculations of their Mössbauer isomer shifts and quadrupole splittings. CASPT2 energy calculations for the oxoferryl species in the quintet, triplet, and septet spin states, together with the DFT results for the reaction pathway, suggest that once the Fe(IV)-O species is formed, the reaction proceeds exclusively on the quintet potential energy surface
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additional information
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the ability of an Fe(IV)-O intermediate in SyrB2 to perform chlorination vs. hydroxylation is computationally evaluated for different substrates. Differential contribution of the two frontier molecular orbitals to chlorination vs. hydroxylation selectivity in SyrB2 is related to a reaction mechanism that involves two asynchronous transfers: electron transfer from the substrate radical to the iron center followed by late ligand (Cl- or OH-) transfer to the substrate
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?
additional information
?
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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
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?
additional information
?
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mechanism of the chlorination reaction of SyrB2 is studied with computational methods. The structure of the SyrB2-substrate complex is modeled with the use of molecular docking procedures. DFT calculations performed with a model involving all first-shell and several second-shell ligands of iron provide energy profiles, which suggest that the two forms of the oxoferryl species can both participate in the reaction. Relative energies of transition states for C-H bond cleavage by these two reactive oxoferryl species dictate the product specificity. The identity of the two oxoferryl species observed in the experimental works is proposed and confirmed by theoretical calculations of their Mössbauer isomer shifts and quadrupole splittings. CASPT2 energy calculations for the oxoferryl species in the quintet, triplet, and septet spin states, together with the DFT results for the reaction pathway, suggest that once the Fe(IV)-O species is formed, the reaction proceeds exclusively on the quintet potential energy surface
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?
additional information
?
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the ability of an Fe(IV)-O intermediate in SyrB2 to perform chlorination vs. hydroxylation is computationally evaluated for different substrates. Differential contribution of the two frontier molecular orbitals to chlorination vs. hydroxylation selectivity in SyrB2 is related to a reaction mechanism that involves two asynchronous transfers: electron transfer from the substrate radical to the iron center followed by late ligand (Cl- or OH-) transfer to the substrate
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
L-threonyl-[L-threonyl-carrier protein SyrB1] + 2-oxoglutarate + O2 + Cl-
4-chloro-L-threonyl-[L-threonyl-carrier protein SyrB1] + succinate + CO2 + H2O
L-threonyl-[L-threonyl-carrier protein SyrB1] + 2-oxoglutarate + O2 + Cl-
4-chloro-L-threonyl-[L-threonyl-carrier protein SyrB1] + succinate + CO2 + H2O
the enzyme participates in syringomycin E biosynthesis
-
-
?
L-threonyl-[L-threonyl-carrier protein SyrB1] + 2-oxoglutarate + O2 + Cl-
4-chloro-L-threonyl-[L-threonyl-carrier protein SyrB1] + succinate + CO2 + H2O
the enzyme participates in syringomycin E biosynthesis
-
-
?
L-threonyl-[L-threonyl-carrier protein SyrB1] + 2-oxoglutarate + O2 + Cl-
4-chloro-L-threonyl-[L-threonyl-carrier protein SyrB1] + succinate + CO2 + H2O
-
the enzyme participates in syringomycin E biosynthesis
-
-
?
additional information
?
-
-
the enzyme catalyzes chlorination of the C4 position of L-threonine appended via a thioester linkage to the phosphopantetheine arm of the companion aminoacyl carrier protein, SyrB1. The native substrate of SyrB2, Thr, is almost exclusively chlorinated, although non-native substrates undergo hydroxylation as well as chlorination. SyrB2 represents an intriguing case in which two different reaction outcomes catalyzed by this enzyme family (hydroxylation and halogenation) are observed
-
-
?
additional information
?
-
-
the enzyme catalyzes chlorination of the C4 position of L-threonine appended via a thioester linkage to the phosphopantetheine arm of the companion aminoacyl carrier protein, SyrB1. The native substrate of SyrB2, Thr, is almost exclusively chlorinated, although non-native substrates undergo hydroxylation as well as chlorination. SyrB2 represents an intriguing case in which two different reaction outcomes catalyzed by this enzyme family (hydroxylation and halogenation) are observed
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?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Fe2+
Iron
the enzyme employs an Fe(IV)-oxo species to achieve selective C-H halogenation of L-threonine. Combined quantum mechanical/molecular mechanical (QM/MM) calculations show the presence of three Cl-Fe(IV)-oxo isomers which interconvert. The one having its oxo ligand pointing toward the target C-H bond is active during the hydrogen atom abstraction (H-abstraction) process. The fate of the formed Cl-FeIII-OH/R radical intermediate is determined by a hydrogenbonding interaction between the Arg254 residue and the OH ligand of Cl-Fe(III)-OH
Fe2+
non-haem Fe(II)-dependent enzyme, mononuclear iron enzyme. Crystallographic data confirm that halide ions bind directly to iron, before decarboxylation of 2-oxoglutarate and formation of a reactive ferryl-oxo species
Fe2+
the chloroferryl intermediate state of the enzyme presents opportunities for structural characterization
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
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UniProt
brenda
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UniProt
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
additional information
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
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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metabolism
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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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
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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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
structure of SyrB2 with both a chloride ion and 2-oxoglutarate coordinated to the iron ion at 1.6 A resolution
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A118D
A118E
mutant enzyme binds Fe(II), but the mutations completely abrogates chlorination activity
A118Q
suppressed H-bonding interaction of Arg254 with Cl-Fe(III)-OH and suppressed chlorination activity
E102A
mutation abolishes the production of syringomycin, as shown by a lack of antifungal activity
F121A
mutation abolishes the production of syringomycin, as shown by a lack of antifungal activity
F195A
mutation abolishes the production of syringomycin, as shown by a lack of antifungal activity
N123A
strong decrease in antifungal activity. The residual activity is approximately 26-30%
A118D
A118E
-
mutant enzyme binds Fe(II), but the mutations completely abrogates chlorination activity
-
A118Q
-
suppressed H-bonding interaction of Arg254 with Cl-Fe(III)-OH and suppressed chlorination activity
-
E102A
-
mutation abolishes the production of syringomycin, as shown by a lack of antifungal activity
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E105A
Streptomyces sp. OH-5093
mutation abolishes the production of syringomycin, as shown by a lack of antifungal activity
F124A
Streptomyces sp. OH-5093
mutation abolishes the production of syringomycin, as shown by a lack of antifungal activity
F195A
Streptomyces sp. OH-5093
mutation abolishes the production of syringomycin, as shown by a lack of antifungal activity
N126A
Streptomyces sp. OH-5093
strong decrease in antifungal activity. The residual activity is approximately 26-30%
A118D
mutant enzyme binds Fe(II), but the mutations completely abrogates chlorination activity
A118D
suppressed H-bonding interaction of Arg254 with Cl-Fe(III)-OH and suppressed chlorination activity
A118D
-
suppressed H-bonding interaction of Arg254 with Cl-Fe(III)-OH and suppressed chlorination activity
-
A118D
-
mutant enzyme binds Fe(II), but the mutations completely abrogates chlorination activity
-
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
autooxidative destruction after a small number of turnovers, the enzyme catalyze 7 turnovers before inactivation
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expression in Escherichia coli
expression in Escherichia coli as His-tagged fusion protein
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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Martinie, R.J.; Livada, J.; Chang, W.C.; Green, M.T.; Krebs, C.; Bollinger, J.M.; Silakov, A.
Experimental correlation of substrate position with reaction outcome in the aliphatic halogenase, SyrB2
J. Am. Chem. Soc.
137
6912-6919
2015
Pseudomonas syringae, Pseudomonas syringae B301D
brenda
Huang, J.; Li, C.; Wang, B.; Sharon, D.; Wu, W.; Shaik, S.
Selective chlorination of substrates by the halogenase SyrB2 is controlled by the protein according to a combined quantum mechanics/molecular mechanics and molecular dynamics study
ACS Catal.
6
2694-2704
2016
Pseudomonas syringae pv. syringae (Q9RBY6), Pseudomonas syringae pv. syringae B301D (Q9RBY6)
-
brenda
Matthews, M.L.; Krest, C.M.; Barr, E.W.; Vaillancourt, F.H.; Walsh, C.T.; Green, M.T.; Krebs, C.; Bollinger, J.M.
Substrate-triggered formation and remarkable stability of the C-H bond-cleaving chloroferryl intermediate in the aliphatic halogenase, SyrB2
Biochemistry
48
4331-4343
2009
Pseudomonas syringae pv. syringae (Q9RBY6), Pseudomonas syringae pv. syringae B301D (Q9RBY6)
brenda
Vaillancourt, F.; Vosburg, D.; Walsh, C.
Dichlorination and bromination of a threonyl-S-carrier protein by the non-heme FeII halogenase SyrB2
ChemBioChem
7
748-752
2006
Pseudomonas syringae pv. syringae (Q9RBY6), Pseudomonas syringae pv. syringae B301D (Q9RBY6)
brenda
Fullone, M.R.; Paiardini, A.; Miele, R.; Marsango, S.; Gross, D.C.; Omura, S.; Ros-Herrera, E.; Bonaccorsi di Patti, M.C.; Lagana, A.; Pascarella, S.; Grgurina, I.
Insight into the structure-function relationship of the nonheme iron halogenases involved in the biosynthesis of 4-chlorothreonine --Thr3 from Streptomyces sp. OH-5093 and SyrB2 from Pseudomonas syringae pv. syringae B301DR
FEBS J.
279
4269-4282
2012
Streptomyces sp. OH-5093 (H6SG30), Pseudomonas syringae pv. syringae (Q9RBY6), Pseudomonas syringae pv. syringae B301DR (Q9RBY6)
brenda
Kulik, H.J.; Blasiak, L.C.; Marzari, N.; Drennan, C.L.
First-principles study of non-heme Fe(II) halogenase SyrB2 reactivity
J. Am. Chem. Soc.
131
14426-14433
2009
Pseudomonas syringae pv. syringae (Q9RBY6), Pseudomonas syringae pv. syringae B301D (Q9RBY6)
brenda
Borowski, T.; Noack, H.; Radon, M.; Zych, K.; Siegbahn, P.E.
Mechanism of selective halogenation by SyrB2 a computational study
J. Am. Chem. Soc.
132
12887-12898
2010
Pseudomonas syringae pv. syringae (Q9RBY6), Pseudomonas syringae pv. syringae B301D (Q9RBY6)
brenda
Srnec, M.; Solomon, E.I.
Frontier molecular orbital contributions to Chlorination versus hydroxylation selectivity in the non-heme iron halogenase SyrB2
J. Am. Chem. Soc.
139
2396-2407
2017
Pseudomonas syringae pv. syringae (Q9RBY6), Pseudomonas syringae pv. syringae B301D (Q9RBY6)
brenda
Blasiak, L.C.; Vaillancourt, F.H.; Walsh, C.T.; Drennan, C.L.
Crystal structure of the non-haem iron halogenase SyrB2 in syringomycin biosynthesis
Nature
440
368-371
2006
Pseudomonas syringae pv. syringae (Q9RBY6), Pseudomonas syringae pv. syringae B301D (Q9RBY6)
brenda
Vaillancourt, F.H.; Yin, J.; Walsh, C.T.
SyrB2 in syringomycin E biosynthesis is a nonheme FeII alpha-ketoglutarate- and O2-dependent halogenase
Proc. Natl. Acad. Sci. USA
102
10111-10116
2005
Pseudomonas syringae pv. syringae (Q9RBY6), Pseudomonas syringae pv. syringae B301D (Q9RBY6), Pseudomonas syringae pv. syringae B301D
brenda
Matthews, M.L.; Neumann, C.S.; Miles, L.A.; Grove, T.L.; Booker, S.J.; Krebs, C.; Walsh, C.T.; Bollinger, J.M.
Substrate positioning controls the partition between halogenation and hydroxylation in the aliphatic halogenase, SyrB2
Proc. Natl. Acad. Sci. USA
106
17723-17728
2009
Pseudomonas syringae pv. syringae (Q9RBY6)
brenda
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