Brief Communication abstract
Nature Chemical Biology 4, 739 - 741 (2008)
Published online: 26 October 2008 | doi:10.1038/nchembio.123
A concerted mechanism for berberine bridge enzyme
Andreas Winkler1,
Andrzej 
yskowski2,4,
Sabrina Riedl1,4,
Martin Puhl1,
Toni M Kutchan3,
Peter Macheroux1
&
Karl Gruber2
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.
- Institute of Biochemistry, Graz University of Technology, Petersgasse 12/II, 8010 Graz, Austria.
-
Institute of Molecular Biosciences, University of Graz, Humboldtstra
e 50/III, 8010 Graz, Austria. - Donald Danforth Plant Science Center, 975 North Warson Road, St. Louis, Missouri 63132, USA
-
Present addresses: Institute of Biotechnology, PO Box 65, Viikinkaari 1, FIN-00014 University of Helsinki, Finland (A.L.) and Institute of Biophysics and Nanosystems Research, Austrian Academy of Sciences, Schmiedlstrae 6, 8042 Graz, Austria (S.R.).
Correspondence to: Sabrina Riedl1,4 e-mail: peter.macheroux@tugraz.at
Correspondence to: Karl Gruber2 e-mail: karl.gruber@uni-graz.at
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