Literature summary for 1.14.13.92 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.

Search for more literature for 1.14.13.92

Cloned(Commentary)

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

Protein Variants

Protein Variants	Comment	Organism
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
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

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

KM Value [mM]

KM Value [mM]	KM Value Maximum [mM]	Substrate	Comment	Organism	Structure
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)

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

Organism

Organism	UniProt	Comment	Textmining
Thermobifida fusca	Q47PU3	-	-

Purification (Commentary)

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

Reaction

Reaction	Comment	Organism	Reaction ID
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)

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

Synonyms

Synonyms	Comment	Organism
PAMO	-	Thermobifida fusca

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

Cofactor	Comment	Organism	Structure
(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
FAD	residue R337, which is conserved in other Baeyer-Villiger monooxygenases, is positioned close to the flavin cofactor	Thermobifida fusca
NADPH	-	Thermobifida fusca

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Release 2023.1 (January 2023)