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Multiple alternatively spliced transcript variants encoding different isoforms have been described for this gene, but some of their full-length sequences are not yet known., this process relies on a copper cofactor.

Dopamine beta-hydroxylase, also a copper-containing enzyme, effects a similar transformation.

Very low amounts of activity were present in the cerebellum and pineal gland.

When the linker region was present between the monooxygenase and lyase domains, monofunctional soluble enzymes were generated from bifunctional PAM proteins; without the linker region, bifunctional enzymes were generated.

Soluble forms of PAM expressed in At T-20 cells and soluble proteins generated through selective endoproteolysis of membrane-associated PAM were secreted in an active form into the medium; secretion of the transfected proteins and endogenous hormone were stimulated in parallel by secretagogues.

Alternative splicing of the single PAM gene gives rise to m RNAs generating PAM proteins with and without a putative transmembrane domain, with and without a linker region between the two enzymes, and forms containing only the monooxygenase domain.

The expression, endoproteolytic processing, storage, and secretion of this secretory granule-associated protein were examined after stable transfection of At T-20 mouse pituitary cells with naturally occurring and truncated PAM proteins.