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In enzymology, a 4-hydroxyphenylacetaldehyde oxime monooxygenase (EC 1.14.13.68) is an enzyme that catalyzes the chemical reaction

(Z)-4-hydroxyphenylacetaldehyde oxime + NADPH + H + O₂ ${\displaystyle \rightleftharpoons }$ (S)-4-hydroxymandelonitrile + NADP + 2 H₂O

The 4 substrates of this enzyme are (Z)-4-hydroxyphenylacetaldehyde oxime, NADPH, H, and O₂, whereas its 3 products are (S)-4-hydroxymandelonitrile, NADP, and H₂O.

This enzyme belongs to the family of oxidoreductases, specifically those 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 o oxygen into the other donor. The systematic name of this enzyme class is (Z)-4-hydroxyphenylacetaldehyde oxime,NADPH:oxygen oxidoreductase. Other names in common use include 4-hydroxybenzeneacetaldehyde oxime monooxygenase, cytochrome P450II-dependent monooxygenase, NADPH-cytochrome P450 reductase (CYP71E1), CYP71E1, and 4-hydroxyphenylacetaldehyde oxime,NADPH:oxygen oxidoreductase. This enzyme participates in tyrosine metabolism.

References

• MacFarlane IJ, Lees EM, Conn EE (1975). "The in vitro biosynthesis of dhurrin, the cyanogenic glycoside of Sorghum bicolor". J. Biol. Chem. 250 (12): 4708–13. doi:10.1016/S0021-9258(19)41359-8. PMID 237909.
• Shimada M, Conn EE (1977). "The enzymatic conversion of p-hydroxyphenylacetaldoxime to p-hydroxymandelonitrile". Arch. Biochem. Biophys. 180 (1): 199–207. doi:10.1016/0003-9861(77)90026-1. PMID 193443.
• Busk PK, Moller BL (2002). "Dhurrin synthesis in sorghum is regulated at the transcriptional level and induced by nitrogen fertilization in older plants". Plant Physiol. 129 (3): 1222–31. doi:10.1104/pp.000687. PMC 166516. PMID 12114576.
• BL, Bak S; Morant, M; Olsen, CE; Ekstrøm, CT; Galbraith, DW; Møller, BL; Bak, S (2005). "Metabolic engineering of dhurrin in transgenic Arabidopsis plants with marginal inadvertent effects on the metabolome and transcriptome". Proc. Natl. Acad. Sci. U.S.A. 102 (5): 1779–84. Bibcode:2005PNAS..102.1779K. doi:10.1073/pnas.0409233102. PMC 545087. PMID 15665094.

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