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Literature summary extracted from

  • Torres Pazmino, D.E.; Baas, B.J.; Janssen, D.B.; Fraaije, M.W.
    Kinetic mechanism of phenylacetone monooxygenase from Thermobifida fusca (2008), Biochemistry, 47, 4082-4093.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.13.92 expression of His-tagged wild-type and mutant enzymes in Escherichia coli Thermobifida fusca

Protein Variants

EC Number Protein Variants Comment Organism
1.14.13.92 R337A site-directed mutagenesis, the mutant is still able to form and stabilize the C4a-peroxyflavin intermediate, but loses the ability to convert phenylacetone or benzyle methylsulfide Thermobifida fusca
1.14.13.92 R337K site-directed mutagenesis, the mutant is still able to form and stabilize the C4a-peroxyflavin intermediate, but loses the ability to convert phenylacetone or benzyle methylsulfide Thermobifida fusca

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.13.92 Benzyl acetate product inhibition Thermobifida fusca
1.14.13.92 NADP+ product inhibition, remains bound during catalysis Thermobifida fusca

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.13.92 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 Thermobifida fusca

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.13.92 phenylacetone + NADPH + H+ + O2 Thermobifida fusca
-
 benzyl acetate + NADP+ + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.13.92 Thermobifida fusca Q47PU3
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.13.92 recombinant His-tagged wild-type and mutant enzymes from Escherichia coli Thermobifida fusca

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.13.92 phenylacetone + NADPH + H+ + O2 = benzyl acetate + NADP+ + H2O reaction mechanism and catalytic cycle, rapid binding of NADPH is followed by a transfer of the (4R)-hydride from NADPH to the FAD cofactor. The reduced PAMO is rapidly oxygenated by molecular oxygen, yielding a C4a-peroxyflavin. The peroxyflavin enzyme intermediate, possibly a Criegee intermediate or a C4a-hydroxyflavin form, reacts with phenylacetone to form benzylacetate, residue R337 is important in catalysis, overview Thermobifida fusca
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.13.92 additional information PAMO is an FAD-containing Baeyer-Villiger monooxygenase Thermobifida fusca ?
-
 ?
1.14.13.92 phenylacetone + NADPH + H+ + O2
-
 Thermobifida fusca benzyl acetate + NADP+ + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.13.92 PAMO
-
 Thermobifida fusca

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.13.92 25
-
 assay at Thermobifida fusca

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.13.92 7.5
-
 assay at Thermobifida fusca

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.13.92 (R)-NADPD deuterated cofactor derivative, the overall rate of catalysis is largely determined by the rate of hydride transfer upon replacement of NADPH by (R)-NADPD as the coenzyme, overview Thermobifida fusca
1.14.13.92 FAD residue R337, which is conserved in other Baeyer-Villiger monooxygenases, is positioned close to the flavin cofactor Thermobifida fusca
1.14.13.92 NADPH
-
 Thermobifida fusca