AKR1A1 Protein, Human (His)

AKR1A1, a versatile enzyme, catalyzes the NADPH-dependent reduction of a broad spectrum of carbonyl-containing compounds to their respective alcohols. Exhibiting enzymatic activity towards endogenous metabolites such as aromatic and aliphatic aldehydes, ketones, monosaccharides, and bile acids, AKR1A1 demonstrates a preference for negatively charged substrates like glucuronate and succinic semialdehyde. Functioning as a detoxifying enzyme, it plays a crucial role in reducing toxic aldehydes, including methylglyoxal and 3-deoxyglucosone, which accumulate under hyperglycemic conditions and exert cytotoxic effects. Additionally, AKR1A1 contributes to the detoxification of lipid-derived aldehydes, such as acrolein. The enzyme is implicated in the activation of procarcinogens, including polycyclic aromatic hydrocarbon trans-dihydrodiols, and participates in the metabolism of various xenobiotics and drugs, such as the anthracyclines doxorubicin (DOX) and daunorubicin (DAUN). Notably, AKR1A1 does not exhibit reductase activity towards retinoids. This diverse substrate specificity underscores its pivotal role in cellular detoxification processes and its potential relevance in therapeutic interventions.