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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Engineering
Engineering on EC 1.14.20.15 - L-threonyl-[L-threonyl-carrier protein] 4-chlorinase
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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
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mutant enzyme binds Fe(II), but the mutations completely abrogates chlorination activity
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A118Q
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suppressed H-bonding interaction of Arg254 with Cl-Fe(III)-OH and suppressed chlorination activity
-
E102A
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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%
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
-
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
-