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In enzymology, a reticuline oxidase (EC 1.21.3.3) is an enzyme that catalyzes the chemical reaction

(S)-reticuline + O₂ ${\displaystyle \rightleftharpoons }$ (S)-scoulerine + H₂O₂

Thus, the two substrates of this enzyme are (S)-reticuline and O₂, whereas its two products are (S)-scoulerine and H₂O₂.

This enzyme belongs to the family of oxidoreductases, specifically those acting on X-H and Y-H to form an X-Y bond with oxygen as acceptor. The systematic name of this enzyme class is (S)-reticuline:oxygen oxidoreductase (methylene-bridge-forming). Other names in common use include BBE, berberine bridge enzyme, berberine-bridge-forming enzyme, and tetrahydroprotoberberine synthase. This enzyme participates in alkaloid biosynthesis i.

References

• Steffens P, Nagakura N, Zenk MH (1984). "The berberine bridge forming enzyme in tetrahydroprotoberberine biosynthesis". Tetrahedron Lett. 25 (9): 951–952. doi:10.1016/S0040-4039(01)80070-8.
• Dittrich H, Kutchan TM (1991). "Molecular cloning, expression, and induction of berberine bridge enzyme, an enzyme essential to the formation of benzophenanthridine alkaloids in the response of plants to pathogenic attack". Proc. Natl. Acad. Sci. U.S.A. 88 (22): 9969–73. doi:10.1073/pnas.88.22.9969. PMC 52848. PMID 1946465.
• Kutchan TM, Dittrich H (1995). "Characterization and mechanism of the berberine bridge enzyme, a covalently flavinylated oxidase of benzophenanthridine alkaloid biosynthesis in plants". J. Biol. Chem. 270 (41): 24475–81. doi:10.1074/jbc.270.41.24475. PMID 7592663.

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