phenylalanine N-monooxygenase;
phenylalanine N-hydroxylase;
CYP79A2

Oxidoreductases;
Acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen. The oxygen incorporated need not be derived from O2;
With NADH or NADPH as one donor, and incorporation of one atom of oxygen into the other donor

L-phenylalanine,NADPH:oxygen oxidoreductase (N-hydroxylating)

L-phenylalanine + 2 O2 + 2 NADPH + 2 H+ = (E)-phenylacetaldoxime + 2 NADP+ + CO2 + 3 H2O (overall reaction) [RN:R09578];
(1a) L-phenylalanine + O2 + NADPH + H+ = N-hydroxy-L-phenylalanine + NADP+ + H2O [RN:R09579];
(1b) N-hydroxy-L-phenylalanine + O2 + NADPH + H+ = N,N-dihydroxy-L-phenylalanine + NADP+ + H2O [RN:R09580];
(1c) N,N-dihydroxy-L-phenylalanine = (E)-phenylacetaldoxime + CO2 + H2O [RN:R09581]

R09578 R09579 R09580 R09581;
(other) R08652

L-phenylalanine [CPD:C00079];
O2 [CPD:C00007];
NADPH [CPD:C00005];
H+ [CPD:C00080];
N-hydroxy-L-phenylalanine [CPD:C19712];
N,N-dihydroxy-L-phenylalanine [CPD:C19715]

A heme-thiolate protein (P-450). This enzyme catalyses two successive N-hydroxylations of L-phenylalanine, the first committed steps in the biosynthesis of benzylglucosinolate. The product of the two hydroxylations, N,N-dihydroxy-L-phenylalanine, is extremely labile and dehydrates spontaneously.The dehydrated product is then subject to a decarboxylation that produces the oxime. It is still not known whether the decarboxylation is spontaneous or catalysed by the enzyme. The product, (E)-phenylacetaldoxime, undergoes a spontaneous isomerization to the (Z) form.

1  [PMID:10799553]

Wittstock U, Halkier BA.

Cytochrome P450 CYP79A2 from Arabidopsis thaliana L. Catalyzes the conversion of L-phenylalanine to phenylacetaldoxime in the biosynthesis of benzylglucosinolate.

J. Biol. Chem. 275 (2000) 14659-66.

Arabidopsis thaliana [GN:ath]