Crystallization and preliminary x-ray analysis of porcine aldehyde reductase in complex with coenzyme and quercetin

Title:Crystallization and preliminary x-ray analysis of porcine aldehyde reductase in complex with coenzyme and quercetin

Volume: 7 Issue: 3

Author(s): Ossama EI-Kabbani and Roland P.-T. Chung

Affiliation:

Abstract: Aldehyde reductase, member of the aldo-keto reductase superfamily, catalyzes the reduction of a variety of aldehydes and ketones to their corresponding alcohols. Hexagonal crystals of porcine aldehyde reductase in complex with NADPH and the flavonoid inhibitor quercetin have been grown using the hanging-drop vapour­ diffusion method with ammonium sulfate as precipitant. The binding of quercetin into the active site of aldehyde reductase was revealed from a difference electron density map. This is the first crystallization report of an aldo-keto reductase in complex with a flavonoid.

Cite this article as:

EI-Kabbani Ossama and Chung P.-T. Roland, Crystallization and preliminary x-ray analysis of porcine aldehyde reductase in complex with coenzyme and quercetin, Protein & Peptide Letters 2000; 7 (3) . https://dx.doi.org/10.2174/092986650703221206130114