AFMID Inhibitors

AFMID inhibitors generally target various points of the kynurenine pathway or related metabolic processes, which can lead to altered AFMID activity.Compounds such as 1-Methyl-D-tryptophan act through competitive inhibition mechanisms within the kynurenine pathway, potentially leading to the accumulation of substrates that compete with AFMID's activity. Others, like Chloroquine, affect the lysosomal pH, which can lead to a less optimal environment for AFMID's function if it is localized to the lysosome. Metabolites such as 3-Hydroxyanthranilic acid and kynurenine itself could engage in feedback inhibition, a common regulatory mechanism in metabolic pathways.

Several compounds, including Methotrexate and Allopurinol, affect the availability of precursors or cofactors required for NAD+ synthesis, which can indirectly influence AFMID's role in this pathway. Nicotinamide, as the end product of NAD+ synthesis, may exert feedback inhibition on enzymes involved in its production, potentially including AFMID. Benserazide and Minocycline modulate the availability of tryptophan or its catabolism, respectively, which can have downstream effects on AFMID activity.