Crystal structure and catalytic mechanism of leucoanthocyanidin reductase from Vitis vinifera.

@article{Maug2010CrystalSA,
  title={Crystal structure and catalytic mechanism of leucoanthocyanidin reductase from Vitis vinifera.},
  author={Chlo{\'e} Maug{\'e} and Thierry Granier and B{\'e}atrice Langlois d'Estaintot and Mahmoud Gargouri and Claude Manigand and Jean-Marie Schmitter and Jean Chaudi{\`e}re and Bernard Gallois},
  journal={Journal of molecular biology},
  year={2010},
  volume={397 4},
  pages={1079-91}
}
Leucoanthocyanidin reductase (LAR) catalyzes the NADPH-dependent reduction of 2R,3S,4S-flavan-3,4-diols into 2R,3S-flavan-3-ols, a subfamily of flavonoids that is important for plant survival and for human nutrition. LAR1 from Vitis vinifera has been co-crystallized with or without NADPH and one of its natural products, (+)-catechin. Crystals diffract to a resolution between 1.75 and 2.72 A. The coenzyme and substrate binding pocket is preformed in the apoprotein and not markedly altered upon… CONTINUE READING

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