Contains FAD. The enzyme from the plant Eschscholtzia californica binds the cofactor covalently . Acts on (S)-reticuline and related compounds, converting the N-methyl group into the methylene bridge (’berberine bridge’) of (S)-tetrahydroprotoberberines. The product of the reaction, (S)-scoulerine, is a precursor of protopine, protoberberine and benzophenanthridine alkaloid biosynthesis in plants.
Steffens, P., Nagakura, N. and Zenk, M.H. The berberine bridge forming enzyme in tetrahydroprotoberberine biosynthesis. Tetrahedron Lett.25 (1984) 951–952.
Dittrich, H. and Kutchan, T.M. Molecular cloning, expression and induction of the berberine bridge enzyme, an enzyme essential to the formation of benzophenanthridine alkaloids in the response of plants to pathogenic attack. Proc. Natl. Acad. Sci. USA88 (1991) 9969–9973. [DOI] [PMID: 1946465]
Kutchan, T.M. and Dittrich, H. Characterization and mechanism of the berberine bridge enzyme, a covalently flavinylated oxidase of benzophenanthridine alkaloid biosynthesis in higher plants. J. Biol. Chem.270 (1995) 24475–24481. [DOI] [PMID: 7592663]
[EC 22.214.171.124 created 1989 as EC 126.96.36.199, transferred 2002 to EC 188.8.131.52]