flavin-adenine-dinucleotide and discretamine

flavin-adenine-dinucleotide has been researched along with discretamine* in 1 studies

Other Studies

1 other study(ies) available for flavin-adenine-dinucleotide and discretamine

Article	Year
A concerted mechanism for berberine bridge enzyme. Nature chemical biology, 2008, Volume: 4, Issue:12 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. Topics: Alkaloids; Berberine Alkaloids; Catalysis; Catalytic Domain; Eschscholzia; Flavin-Adenine Dinucleotide; Kinetics; Oxidoreductases, N-Demethylating; Oxygen; Protons	2008

Article

Year

A concerted mechanism for berberine bridge enzyme.

Nature chemical biology, 2008, Volume: 4, Issue:12

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.

Topics: Alkaloids; Berberine Alkaloids; Catalysis; Catalytic Domain; Eschscholzia; Flavin-Adenine Dinucleotide; Kinetics; Oxidoreductases, N-Demethylating; Oxygen; Protons

2008