Chemo-enzymatic access to novel berbine derivatives employing the berberine bridge enzyme

JOERG H. SCHRITTWIESER; VERENA RESCH; EVA FISCHEREDER; ALEJANDRO ORDEN; JOHANN SATTLER; WOLF-DIETER LIENHART; SILVIA WALLNER; KARL GRUBER; PETER MACHEROUX ; WOLFGANG KROUTIL

Flavins and Flavoproeteins 2011 Proceedings of the 17th International Symposium on Flavins and Flavoproteins

S. Miller, R. Hille, B. Palfey (Eds.), Lulu, Raleigh/USA

Año: 2013; p. 129 - 132

Berberine  bridge  enzyme  (BBE),  first  identified  in  1963 catalyzes in  vivo  an  outstanding  oxidative  intramolecular  C-C bond  formation  by bridging a phenol  moiety  to  an N-methyl  group  of (S)-reticuline yielding (S)-scoulerine  at  the  expense  of molecular oxygen. A bicovalently bonded  flavin  is  responsible  for  this  reaction  involving aerobic  oxidative  C-H  activation  coupled  to  C-C  bond  formation.Recently,  BBE  from  Eschscholzia  californica  (California  poppy)  was expressed in  Pichia  pastoris yielding  a sufficient  quantity  of the enzyme  for  crystallization  to  solve  the  structure  and  for  investigation  of the  mechanism.