The enzyme contains an adenylation domain, a phosphopantetheinyl binding 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 phosphopantetheinyl binding domain. The resulting thioester is subsequently transferred to the reductase domain, where it is reduced to an aldehyde and released.
[Reduction of aromatic acids to aldehydes and alcohols in the cell-free system. 1. Purification and properties of aryl-aldehyde: NADP-oxidoreductase from Neurospora crassa]
