A concerted mechanism for berberine bridge enzyme

Andreas Winkler, Andrzej Łyskowski, Sabrina Riedl, Martin Puhl, Toni M. Kutchan, Peter Macheroux, Karl Gruber

Research output: Contribution to journalArticlepeer-review

101 Scopus citations


Berberine bridge enzyme catalyzes the conversion of (S)-reticuline to (S)-scoulerine by formation of a carbon-carbon bond between the N-methyl group and the phenolic ring. We elucidated the structure of berberine bridge enzyme from Eschscholzia californica and determined the kinetic rates for three active site protein variants. Here we propose a catalytic mechanism combining base-catalyzed proton abstraction with concerted carbon-carbon coupling accompanied by hydride transfer from the N-methyl group to the N5 atom of the FAD cofactor.

Original languageEnglish
Pages (from-to)739-741
Number of pages3
JournalNature Chemical Biology
Issue number12
StatePublished - Dec 2008


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