1.14.13.84: 4-hydroxyacetophenone monooxygenase
This is an abbreviated version!
For detailed information about 4-hydroxyacetophenone monooxygenase, go to the full flat file.
Word Map on EC 1.14.13.84
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1.14.13.84
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baeyer-villiger
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fluorescens
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ketones
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bvmos
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acetophenones
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cyclohexanone
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nadph-dependent
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biocatalytic
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putida
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enantioselectivity
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resin
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base-catalysed
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stabilised
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ring-substituted
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characterise
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fad
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flavoproteins
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synthesis
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4-fluorophenol
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fluorophenyl
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fluoride
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flavin-containing
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synthons
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4-fluorocatechol
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sulfides
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lactones
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fluorinated
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noncovalent
- 1.14.13.84
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baeyer-villiger
- fluorescens
- ketones
-
bvmos
- acetophenones
- cyclohexanone
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nadph-dependent
-
biocatalytic
- putida
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enantioselectivity
- resin
-
base-catalysed
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stabilised
-
ring-substituted
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characterise
- fad
- flavoproteins
- synthesis
- 4-fluorophenol
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fluorophenyl
- fluoride
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flavin-containing
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synthons
- 4-fluorocatechol
- sulfides
- lactones
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fluorinated
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noncovalent
Reaction
Synonyms
4-hydroxyacetophenone monooxygenase, arylketone monooxygenase, Baeyer-Villiger monooxygenase, hAPA, HAPMO, More, oxygenase, 4-hydroxyacetophenone mono-
ECTree
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Cofactor
Cofactor on EC 1.14.13.84 - 4-hydroxyacetophenone monooxygenase
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FAD
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contains one molecule of FAD per enzyme molecule, FAD is reduced specifically by NADPH and not by NADH
FAD
FAD-dependent, each subunit contains a noncovalently bound FAD molecule, both molecules participate in the reduction reaction, molecular oxygen is able to reoxidize the flavin cofactor
FAD
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required for activity, each subunit contains a non-covalently, tightly bound FAD cofactor, binding of FAD is important for the octameric conformation
NADPH
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specific for NADPH as coenzyme, Arg-339 and Lys-439 are involved in coenzyme recognition, Arg-440 not, Lys-439 plays a role in recognizing the 2-phosphate of NADPH, 700fold preference for NADPH over NADH
additional information
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complex formation between the cofactors NADPH or 3-aminopyridine adenine dinucleotide phosphate
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