Tryptophan 2-monooxygenase (TMO)

Tryptophan 2-monooxygenase is a flavin adenine dinucleotide (FAD)-dependent oxidoreductase enzyme, primarily found in plant-associated bacteria such as *Pseudomonas savastanoi*. It catalyzes the oxidative decarboxylation of L-tryptophan to indole-3-acetamide (IAM), carbon dioxide, and water, using molecular oxygen as a co-substrate. This reaction is the initial step in the synthesis of indole-3-acetic acid (IAA), the main plant growth hormone known as auxin. The enzyme plays a key role in plant-pathogen interactions resulting in gall formation (crown gall disease) and is of significant interest in metabolic engineering for biosynthesis of auxins and related compounds. Structurally, TMO is closely related to the monoamine oxidase family of flavoenzymes and is characterized by conserved residues important for substrate binding and catalysis[1][2][3][4][5][6].

Other names

L-tryptophan:oxygen 2-oxidoreductase (decarboxylating)iaaM (gene name)TMOtryptophan monooxygenase

Catalyzes oxidative decarboxylation of L-tryptophan, producing indole-3-acetamide, a precursor in the auxin (IAA) biosynthetic pathway[1][2][3][4][5].