A concerted mechanism for berberine bridge enzyme

Andreas Winkler; Andrzej Lyskowski; Sabrina Riedl; Martin Puhl; Toni M. Kutchan; Peter Macheroux; Karl Gruber

doi:10.1038/nchembio.123

A concerted mechanism for berberine bridge enzyme

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

^*Corresponding author for this work

Institute of Biochemistry (6480)

Research output: Contribution to journal › Article › peer-review

Abstract

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 language	English
Pages (from-to)	739-741
Journal	Nature Chemical Biology
Volume	4
Issue number	12
DOIs	https://doi.org/10.1038/nchembio.123
Publication status	Published - 2008

Treatment code (Nähere Zuordnung)

Basic - Fundamental (Grundlagenforschung)

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10.1038/nchembio.123

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abstract = "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.",

author = "Andreas Winkler and Andrzej Lyskowski and Sabrina Riedl and Martin Puhl and Kutchan, {Toni M.} and Peter Macheroux and Karl Gruber",

note = "Nature Chemical Biology",

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AU - Winkler, Andreas

AU - Lyskowski, Andrzej

AU - Riedl, Sabrina

AU - Puhl, Martin

AU - Kutchan, Toni M.

AU - Macheroux, Peter

AU - Gruber, Karl

N1 - Nature Chemical Biology

PY - 2008

Y1 - 2008

N2 - 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.

AB - 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.

U2 - 10.1038/nchembio.123

DO - 10.1038/nchembio.123

M3 - Article

SN - 1552-4469

VL - 4

SP - 739

EP - 741

JO - Nature Chemical Biology

JF - Nature Chemical Biology

IS - 12

ER -

A concerted mechanism for berberine bridge enzyme

Abstract

Treatment code (Nähere Zuordnung)

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