Aldehyde reductase YqhD

Storage Conditions:

2 °C to 8 °C

YqhD from E. coli is a homodimeric protein, localized in the cytoplasm. Each monomer has a two-domain structure, one domain that binds the cofactor NADPH and the other the catalytic metal Zn²⁺. This enzyme belongs to the aldo-keto reductase superfamily, a group of enzymes responsible for a wide array of biological functions.

Availability

On Demand

Details

YqhD from E. coli is a homodimeric protein, localized in the cytoplasm, which coordinates of the 3D structure have been deposited in the RCSB Protein Data Bank as entry 1Oj7 (Sulzenbacher et al., 2004). Each monomer has a two-domain structure, one domain that binds the cofactor NADPH and the other the catalytic metal Zn²⁺. This enzyme belongs to the aldo-keto reductase superfamily, a group of enzymes responsible for a wide array of biological functions. Pérez et al. (2008) showed that YqhD is an aldehyde reductase involved in the cellular resistance to Reactive Oxygen Species (ROS)-generating compounds and “reactive aldehydes”. YqhD catalyses the NADPH-dependent reduction of various membrane peroxidation derived aldehydes, including acetaldehyde, propanaldehyde, butanaldehyde, acrolein and malondialdehyde (MDA). It was suggested that YqhD is part of a specific defense mechanism against reactive aldehydes generated by membrane peroxidation in E. coli (Pérez et al., 2008). The enzyme is provided in 3.2 M ammonium sulphate.

Quantity: 2.0 mg

Temperature and pH optimum/stability: The optimum pH and temperature are 7.0 and 25 °C, respectively.