1.14.14.11: styrene monooxygenase
This is an abbreviated version!
For detailed information about styrene monooxygenase, go to the full flat file.
Word Map on EC 1.14.14.11
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1.14.14.11
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epoxidation
-
enantioselective
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two-component
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s-styrene
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synthesis
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phenylacetic
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solvent-tolerant
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enantiopure
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phenylacetaldehyde
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two-liquid
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opacus
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s-epoxides
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taiwanensis
- 1.14.14.11
-
epoxidation
-
enantioselective
-
two-component
-
s-styrene
- synthesis
-
phenylacetic
-
solvent-tolerant
-
enantiopure
- phenylacetaldehyde
-
two-liquid
- opacus
-
s-epoxides
- taiwanensis
Reaction
Synonyms
FAD-specific styrene epoxidase, NSMOA, SMO, SmoA, StyA, StyA1, StyA1/StyA2B, StyA2B, StyAB
ECTree
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Cofactor
Cofactor on EC 1.14.14.11 - styrene monooxygenase
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FAD
incorporation of reduced FAD into StyA enzymes is attended with significant conformational rearrangements
FADH2
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direct electrochemical regeneration of FADH2 to substitute for the complex native regeneration cycle including StyB and NADH
FADH2
flavin binding and redox equilibria are tightly coupled such that reduced FAD binds apo NSMOA about 8000times more tightly than the oxidized coenzyme
FADH2
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no epoxidation activity is observed for the StyAB system when FAD is replaced by FMN or riboflavin. At a FAD concentration exceeding 0.015 mM, the styrene oxide formation rate decreases
FADH2
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NSMOA binds tightly to reduced FAD. FAD C(4a)-peroxide is the oxygen atom donor
FADH2
StyA1 is not active with free FADH2 and recognizes StyA2B as its natural partner. FADH2-induced activation of StyA1 requires interprotein communication with StyA2B. StyA1/StyA2B is a member of the family of two-component flavin-dependent monooxygenases. StyA1 is the major monooxygenase, and StyA2B functions mainly as a FAD reductase with little oxygenating side activity
FADH2
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the enzyme is specific for FADH2. No activity with FADH2-dependent monooxygenase (in this case StyA) can be regenerated directly by means of non-native redox catalysts such as [Cp*Rh(bpy)-(H2O)]2+