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
-
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
1.14.13.84 4-hydroxyacetophenone monooxygenaseAdvanced search results
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results (Engineering
Engineering on EC 1.14.13.84 - 4-hydroxyacetophenone monooxygenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
G490A
strictly conserved glycine, dramatic effect of mutation on binding and oxidation of NADPH
H61T
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the H61T mutant is purified as apo-enzyme and mainly exists as a dimeric species, the binding of FAD to the enzyme restores the octameric conformation
K439A
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mutant with 100fold decrease in catalytic efficiency with NADPH, mainly caused by increased Km, 4fold increased efficiency with NADH
K439F
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mutant with higher activity with NADH compared to wild-type HAPMO
K439N
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mutant with higher activity with NADH compared to wild-type HAPMO
K439P
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mutant with higher activity with NADH compared to wild-type HAPMO
R339A
R440A
G490A
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strictly conserved glycine, dramatic effect of mutation on binding and oxidation of NADPH
-
H61T
-
the H61T mutant is purified as apo-enzyme and mainly exists as a dimeric species, the binding of FAD to the enzyme restores the octameric conformation
-
K439A
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mutant with 100fold decrease in catalytic efficiency with NADPH, mainly caused by increased Km, 4fold increased efficiency with NADH
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K439F
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mutant with higher activity with NADH compared to wild-type HAPMO
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K439N
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mutant with higher activity with NADH compared to wild-type HAPMO
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R339A
R440A
R339A
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mutant with largely decreased affinity for NADPH and decreased catalytic efficiency with NADH
R339A
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site-directed mutagenesiss, the mutant shows decreased activity and affinity to NADPH compared to the wild-type enzyme, the mutant only weakly interacts with 3-aminopyridine adenine dinucleotide phosphate
R440A
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totally inactive mutant, Arg-440 is crucial for completing the catalytic cycle
R440A
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site-directed mutagenesiss, inactive mutant, the mutant shows highly increased affinity to NADPH compared to the wild-type enzyme
R339A
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mutant with largely decreased affinity for NADPH and decreased catalytic efficiency with NADH
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R339A
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site-directed mutagenesiss, the mutant shows decreased activity and affinity to NADPH compared to the wild-type enzyme, the mutant only weakly interacts with 3-aminopyridine adenine dinucleotide phosphate
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R440A
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totally inactive mutant, Arg-440 is crucial for completing the catalytic cycle
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R440A
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site-directed mutagenesiss, inactive mutant, the mutant shows highly increased affinity to NADPH compared to the wild-type enzyme
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