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
-
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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Natural Substrates Products
Natural Substrates Products on EC 1.14.20.15 - L-threonyl-[L-threonyl-carrier protein] 4-chlorinase
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REACTION DIAGRAM
L-threonyl-[L-threonyl-carrier protein SyrB1] + 2-oxoglutarate + O2 + Cl-
4-chloro-L-threonyl-[L-threonyl-carrier protein SyrB1] + succinate + CO2 + H2O
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 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
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the enzyme participates in syringomycin E biosynthesis
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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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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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?