ALDH3B1 Inhibitors

ALDH3B1 inhibitors encompass a range of compounds that can interfere with the enzymatic activity of the ALDH3B1 protein through various mechanisms. Disulfiram and cyanamide function by directly interacting with the active site of ALDH3B1, either by binding to the aldehyde substrate-binding site or by covalently modifying the active site cysteine, leading to the enzyme's inhibition. Compounds like daidzin, gossypol, 4-diethylamino benzaldehyde, and ferulic acid exhibit competitive inhibition by contesting the aldehyde substrates for the enzyme's active site. This competitive mechanism ensures that the presence of these inhibitors in the enzyme's vicinity will decrease ALDH3B1's functional activity by preventing the physiological substrates from accessing the catalytic site.

In addition to competitive inhibition, other mechanisms are also at play with different chemical compounds. For example, benomyl and aldicarb inhibit ALDH3B1 by interacting with essential residues within the active site, which are crucial for enzyme-substrate interaction and catalysis. Omeprazole, through the formation of adducts with cysteine residues, can modify the active site and disrupt normal enzyme activity. In contrast, acetaldehyde and chloral hydrate utilize a mechanism of substrate inhibition, where high concentrations of these substrates can lead to an inhibitory effect, reducing the overall activity of ALDH3B1.