1.14.13.92: phenylacetone monooxygenase
This is an abbreviated version!
For detailed information about phenylacetone monooxygenase, go to the full flat file.
Word Map on EC 1.14.13.92
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1.14.13.92
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baeyer-villiger
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ketone
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enantioselectivity
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bvmos
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thermobifida
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biocatalytic
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cyclohexanone
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fusca
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synthesis
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sulfoxidations
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biocatalyst
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phosphite
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cyclopentanone
- 1.14.13.92
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baeyer-villiger
- ketone
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enantioselectivity
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bvmos
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thermobifida
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biocatalytic
- cyclohexanone
- fusca
- synthesis
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sulfoxidations
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biocatalyst
- phosphite
- cyclopentanone
Reaction
Synonyms
4-hydroxyacetophenone monooxygenase, Baeyer-Villiger monooxygenase, BVMO, EtaA, HAPMO, M-PAMO, More, PAMO, phenylacetone monooxygenase, Tf PAMO
ECTree
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KM Value
KM Value on EC 1.14.13.92 - phenylacetone monooxygenase
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0.25
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mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
0.25
2-Octanone
recombinant mutant P253F/G254A/R258M/L443F, pH 7.4, 25°C
0.8
2-phenylcyclohexanone
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mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
0.8
2-phenylcyclohexanone
recombinant mutant P253F/G254A/R258M/L443F, pH 7.4, 25°C
44
2-phenylcyclohexanone
recombinant wild-type enzyme, pH 7.4, 25°C
0.266
cyclohexanone
pH 8.0, 25°C, recombinant mutant S441G/A442P/L443T/S444Q
1000
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mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
1000
Cyclopentanone
recombinant mutant P253F/G254A/R258M/L443F, pH 7.4, 25°C
0.04
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mutant enzyme P253F/G254A/R258M/L443F, at pH 7.5 and 37°C
0.28
phenylacetone
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25°C, pH 8.5, in the presence of 0.006 mM bovine serum albumin
1.4
phenylacetone
recombinant mutant P253F/G254A/R258M/L443F, pH 7.4, 25°C
additional information
additional information
Michaelis-Menten kinetics
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additional information
additional information
steady-state kinetics of wild-type and mutant enzymes
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additional information
additional information
steady-state kinetics of wild-type and mutant enzymes
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additional information
additional information
detailed steady-state and pre-steady-state kinetic analysis of the reductive and the oxidative half-reaction of wild-type and mutant enzymes, overview
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additional information
additional information
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detailed steady-state and pre-steady-state kinetic analysis of the reductive and the oxidative half-reaction of wild-type and mutant enzymes, overview
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additional information
additional information
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steady-state kinetics with NADPH and NADH cofactors, overview
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additional information
additional information
steady-state kinetic analysis of wild-type and mutant enzymes
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