ActVA-Orf6 monooxygenase (ActVA-Orf6)

ActVA-Orf6 monooxygenase is a small enzyme (113 amino acids) with a unique ferredoxin-like fold and dimeric assembly, found in Streptomyces coelicolor and other actinobacteria[1][8]. It plays a key role in the biosynthetic pathway leading to actinorhodin, an antibiotic compound, by oxidizing large three-ring aromatic substrates during secondary metabolite production. The enzyme’s active site consists of conserved residues (notably Asn62 and Trp66), and it functions without a metal ion or prosthetic group, distinguishing it from many other monooxygenases. While not a direct therapeutic target, its structural and mechanistic characterization informs biotechnological research in antibiotic development[1][8][5].

Other names

ActVA-Orf6Monooxygenase ActVA-Orf6ActVA monooxygenaseActVA6

Catalyzes monooxygenation reactions on large aromatic intermediates in actinorhodin biosynthesis