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Your query returned 1 entry. 
Printable version
| EC | 1.14.14.40 | ||||
| Accepted name: | phenylalanine N-monooxygenase | ||||
| Reaction: | L-phenylalanine + 2 [reduced NADPH—hemoprotein reductase] + 2 O2 = (E)-phenylacetaldoxime + 2 [oxidized NADPH—hemoprotein reductase] + CO2 + 3 H2O (overall reaction) (1a) L-phenylalanine + [reduced NADPH—hemoprotein reductase] + O2 = N-hydroxy-L-phenylalanine + [oxidized NADPH—hemoprotein reductase] + H2O (1b) N-hydroxy-L-phenylalanine + [reduced NADPH—hemoprotein reductase] + O2 = N,N-dihydroxy-L-phenylalanine + [oxidized NADPH—hemoprotein reductase] + H2O (1c) N,N-dihydroxy-L-phenylalanine = (E)-phenylacetaldoxime + CO2 + H2O |
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| Other name(s): | phenylalanine N-hydroxylase; CYP79A2 (gene name); CYP79D16 (gene name) | ||||
| Systematic name: | L-phenylalanine,[reduced NADPH—hemoprotein reductase]:oxygen oxidoreductase (N-hydroxylating) | ||||
| Comments: | This cytochrome P-450 (heme-thiolate) enzyme, found in plants, catalyses two successive N-hydroxylations of L-phenylalanine, a committed step in the biosynthesis of benzylglucosinolate and the cyanogenic glucosides (R)-prunasin and (R)-amygdalin. The product of the two hydroxylations, N,N-dihydroxy-L-phenylalanine, is labile and undergoes dehydration followed by decarboxylation, producing an oxime. It is still not known whether the decarboxylation is spontaneous or catalysed by the enzyme. | ||||
| Links to other databases: | BRENDA, EXPASY, Gene, KEGG, MetaCyc | ||||
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