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Cytochrome P450 130 (CYP130) is a heme-containing monooxygenase enzyme produced by Mycobacterium tuberculosis (Mtb) [2]. It is one of the 20 P450 enzymes encoded in the Mtb genome and is notable for its high affinity for antifungal azole drugs, such as econazole and clotrimazole, which inhibit its activity by coordinating with the heme iron [1, 4]. Although its exact endogenous substrate and physiological role are not yet fully understood, its absence in the closely related Mycobacterium bovis suggests it may be specifically involved in the infection of human hosts or Mtb virulence [1, 4, 5]. Structural studies have revealed that CYP130 undergoes a dramatic conformational change from an open to a closed state upon ligand binding, which reshapes the protein surface and active site [1, 11]. Given its potential role in Mtb survival and its susceptibility to existing drug classes, CYP130 is considered a viable therapeutic target for developing novel treatments against tuberculosis, including multidrug-resistant strains [4, 5, 12].
Inhibition of the enzyme's catalytic activity by binding to the heme iron and active site, preventing the processing of endogenous substrates essential for Mycobacterium tuberculosis physiology or virulence [1, 4, 5].
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