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Literature summary for 1.14.13.92 extracted from

  • Rioz-Martinez, A.; De Gonzal, D.G.; Torres Pazmino, D.; Fraaije, M.; Gotor, V.
    Enzymatic Baeyer-Villiger oxidation of benzo-fused ketones: Formation of regiocomplementary lactones (2009), Eur. J. Org. Chem., 2009, 2526-2532.
No PubMed abstract available

Activating Compound

Activating Compound Comment Organism Structure
hexane enzyme activity is highest at concentrations of hexane between 5% and 30% Pseudomonas fluorescens

Cloned(Commentary)

Cloned (Comment) Organism
overexpressed in Escherichia coli Thermobifida fusca
overexpressed via plasmid in Escherichia coli Pseudomonas fluorescens

Protein Variants

Protein Variants Comment Organism
M446G enzyme has altered activity and substrate specificity Thermobifida fusca

Inhibitors

Inhibitors Comment Organism Structure
hexane enzyme activity is markedly reduced at concentrations of hexane below 5% and over 30% Pseudomonas fluorescens

Organism

Organism UniProt Comment Textmining
Pseudomonas fluorescens
-
-
-
Thermobifida fusca
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Pseudomonas fluorescens
-
Thermobifida fusca

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-bromo-indanone + NADPH + O2 substrate was only accepted by phenylacetone monooxygenase of Pseudomonas fluorescens but not of Thermobifida fusca, reaction was performed in presence of 10 U glucose-6-phosphate dehydrogenase and glucose-6-phosphate to recover NADPH Pseudomonas fluorescens 6-bromoisochroman-1-one + NADP+ + H2O
-
?
1-indanone + NADPH + H+ + O2 substrate was only accepted by phenylacetone monooxygenase of Pseudomonas fluorescens but not of Thermobifida fusca, reaction was performed in presence of 10 U glucose-6-phosphate dehydrogenase and glucose-6-phosphate to recover NADPH Pseudomonas fluorescens 3,4-dihydrocoumarin + NADP+ + H2O
-
?
1-indanone + NADPH + H+ + O2 reaction product is only synthesized by the mutant M446G of phenylacetone monooxygenase of Thermobifida fusca, reaction is performed in presence of 10 U glucose-6-phosphate dehydrogenase and glucose-6-phosphate to recover NADPH Thermobifida fusca 1-isochromanone + NADP+ + H2O
-
?
1-tetralone + NADPH + O2 substrate was accepted by phenylacetone monooxygenase of Pseudomonas fluorescens but not of Thermobifida fusca, reaction was performed in presence of 10 U glucose-6-phosphate dehydrogenase and glucose-6-phosphate to recover NADPH Pseudomonas fluorescens 4,5-dihydro-1-benzoxepin-2(3H)-one + NADP+ + H2O
-
?
2-indanone + NADPH + H+ + O2 substrate is only accepted by the mutant M446G of phenylacetone monooxygenase of Thermobifida fusca, reaction is performed in presence of 10 U glucose-6-phosphate dehydrogenase and glucose-6-phosphate to recover NADPH Thermobifida fusca 3-isochromanone + NADP+ + H2O
-
?
6-methoxy-1-indanone + NADPH + O2 substrate was only accepted by phenylacetone monooxygenase of Pseudomonas fluorescens but not of Thermobifida fusca, reaction was performed in presence of 10 U glucose-6-phosphate dehydrogenase and glucose-6-phosphate to recover NADPH Pseudomonas fluorescens ? + NADP+ + H2O
-
?
benzocyclobutanone + NADPH + O2 reaction is performed in presence of 10 U glucose-6-phosphate dehydrogenase and glucose-6-phosphate to recover NADPH Thermobifida fusca 2-coumaranone + NADP+ + H2O
-
?
benzocyclobutanone + NADPH + O2 reaction was performed in presence of 10 U glucose-6-phosphate dehydrogenase and glucose-6-phosphate to recover NADPH Pseudomonas fluorescens 2-coumaranone + NADP+ + H2O
-
?
phenylacetone + NADPH + O2 reaction is performed in presence of 10 U glucose-6-phosphate dehydrogenase and glucose-6-phosphate to recover NADPH Thermobifida fusca benzyl acetate + NADP+ + H2O
-
?
phenylacetone + NADPH + O2 reaction was performed in presence of 10 U glucose-6-phosphate dehydrogenase and glucose-6-phosphate to recover NADPH Pseudomonas fluorescens benzyl acetate + NADP+ + H2O
-
?

Synonyms

Synonyms Comment Organism
4-hydroxyacetophenone monooxygenase
-
Pseudomonas fluorescens
Baeyer-Villiger monooxygenase
-
Thermobifida fusca
BVMO
-
Thermobifida fusca
HAPMO
-
Pseudomonas fluorescens
M-PAMO mutant M446G of phenylacetone monooxygenase, phenylacetone monooxygenase mutein Thermobifida fusca
PAMO
-
Thermobifida fusca
phenylacetone monooxygenase
-
Thermobifida fusca

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
9
-
enzyme activity is high from pH 9 to pH 10.5 Thermobifida fusca
9
-
enzyme activity is highest from pH 9 to pH 10.5 Pseudomonas fluorescens