Peptidyl amidating enzyme

This enzyme belongs to the family of oxidoreductases, specifically those acting on paired donors, with O2 as oxidant and incorporation or reduction of oxygen.

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I]d-Tyr-Val-Gly as substrate, a peptidyl-glycine α-amidating monooxygenase (PAM) was detected in islet secretory granule lysates.

The enzyme is active between p H 6.0 and 8.5 and exhibits maximal activity near p H 7.0.

Many peptide hormones and neuropeptides require an amidated carboxy terminal for full biological activity.

This reaction is carried out in two steps: hydroxylation of a C-terminal glycine and cleavage of the C N bond with the release of glyoxylate.

Other divalent metal ions and redox cofactors were tested and found to be inactive in the assay.


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