RDH7 Inhibitors

Chemical inhibitors of RDH7 can exert their inhibitory effects through various biochemical mechanisms. Retinal, for example, serves as a competitive antagonist by binding to the same site on RDH7 that normally binds retinol, which is RDH7's natural substrate. This binding prevents RDH7 from converting retinol into retinaldehyde, essentially blocking the enzyme's primary function. Similarly, Citral forms a reaction with the alcohol group of retinol, reducing the pool of substrate available for RDH7 to act upon. This reaction alters retinol so that it cannot be recognized and processed by RDH7. Farnesol, by integrating into cellular membranes, can influence the function of membrane-bound enzymes like RDH7. This integration disrupts the normal activity of RDH7, leading to decreased enzymatic action. Bisphenol A also associates with cellular membranes and can disturb the function of membrane-associated enzymes such as RDH7, leading to a reduction in the enzyme's catalytic activity.

Furthermore, Methotrexate indirectly inhibits RDH7 by interfering with the cellular uptake and metabolism of retinol, limiting the availability of the enzyme's substrate. Benzo[a]pyrene forms adducts with retinol, which prevents RDH7 from accessing and processing its substrate. Synthetic derivatives of retinol, such as 4-Hydroxyphenyl retinamide and analogues like Isotretinoin and Tretinoin, can occupy the active site of RDH7, which directly impedes the enzyme's ability to metabolize retinol. N-Ethylmaleimide can modify cysteine residues on RDH7, potentially altering the enzyme's structure and function, leading to inhibition. Oleanolic acid alters membrane fluidity and permeability, which can affect the activity of RDH7. Lastly, Ellagic acid can bind to RDH7, potentially modifying its structure or directly blocking its active site, which results in the inhibition of the enzyme's function. Each of these chemicals, through their distinct interactions with RDH7 or its substrate, can effectively inhibit the enzymatic activity of RDH7.