CYP2AB1 Activators

CYP2AB1, a cytochrome P450 enzyme, is predicted to possess heme binding activity, oxidoreductase activity, acting on paired donors with incorporation or reduction of molecular oxygen, and steroid hydroxylase activity. It is involved in organic acid metabolic processes and xenobiotic metabolic processes, active in the cytoplasm and intracellular membrane-bounded organelle, and is orthologous to the pseudogene CYP2AB1P in humans.

Activation of CYP2AB1 involves a multifaceted interplay of direct and indirect mechanisms influenced by various chemicals. For example, the antimalarial Amodiaquine and the glucocorticoid Dexamethasone may directly induce CYP2AB1 by modulating cytochrome P450 enzymes or activating nuclear receptors, respectively. Additionally, compounds like the thiazolidinedione Troglitazone and the protease inhibitor Nelfinavir may indirectly upregulate CYP2AB1 by influencing PPAR signaling or modulating cytochrome P450 enzymes. The activation of CYP2AB1 is intricately linked to its role in xenobiotic metabolism and steroid hydroxylation, providing insights into potential interactions with drugs and foreign compounds. Understanding these activation mechanisms contributes to the broader understanding of CYP2AB1 function and its impact on drug metabolism.