Violacein biosynthesis protein VioB (VioB)

Violacein biosynthesis protein VioB is a critical enzyme in the biosynthetic pathway of violacein, a bis-indole pigment produced by various bacteria, most notably Chromobacterium violaceum [1, 2]. As a heme-dependent oxidase, VioB catalyzes the dimerization of two indole-3-pyruvic acid (IPA) imine molecules, a key step in constructing the complex pyrrolidone-containing scaffold of violacein [2, 31]. This enzyme is of significant interest in biotechnology and medicine due to the potent biological activities of its product, violacein, which exhibits antibacterial, antifungal, and antitumoral properties [3, 35]. VioB is considered a therapeutic target for anti-virulence strategies aimed at reducing the toxicity of C. violaceum, an opportunistic human pathogen, as its inhibition leads to the depletion of violacein and a subsequent decrease in bacterial virulence [5]. Additionally, VioB is a primary focus for metabolic engineering efforts to enhance the microbial production of violacein for pharmaceutical applications [2, 35].

Other names

Iminophenyl-pyruvate dimer synthaseIPA imine dimer synthaseL-tryptophan 2-aminotransferase (misnomer)VioB protein

Catalyzes the oxidative coupling and dimerization of two molecules of indole-3-pyruvic acid (IPA) imine to form a precursor of violacein.