The enzyme, characterized from the ascomycete fungus Aspergillus flavus, is specific for L-tyrosine. It contains three domains - an adenylation domain, a peptidyl-carrier protein (PCP) domain, and a reductase domain, and requires activation by attachment of a phosphopantetheinyl group. The enzyme activates its substrate to an adenylate form, followed by a transfer to the PCP domain. The resulting thioester is subsequently transferred to the reductase domain, where it is reduced to the aldehyde.
