Peptidylglycine α-Amidating Monooxygenase and Other Processing Enzymes in the Neurointermediate Pituitary

• Published in: Annals of the New York Academy of Sciences 1993-05, Vol.680 (1), p.147-160
• Main Authors: EIPPER, BETTY A., BLOOMQUIST, BRIAN T., HUSTEN, E. JEAN, MILGRAM, SHARON L., MAINS, RICHARD E.
• Format: Article
• Language: English
• Subjects: Amino Acid Sequence; Animals; Gene Expression Regulation; Melanocyte-Stimulating Hormones - genetics; Melanocyte-Stimulating Hormones - metabolism; Mixed Function Oxygenases - genetics; Mixed Function Oxygenases - metabolism; Models, Structural; Molecular Sequence Data; Multienzyme Complexes; Pituitary Gland - enzymology; Pro-Opiomelanocortin - metabolism; Proprotein Convertase 2; Proprotein Convertases; Protein Processing, Post-Translational; Protein Structure, Secondary; Rats; RNA, Messenger - metabolism; Serine Endopeptidases - genetics; Serine Endopeptidases - metabolism; Substrate Specificity; Subtilisins - genetics; Subtilisins - metabolism
• ISSN: 0077-8923; 1749-6632
• DOI: 10.1111/j.1749-6632.1993.tb19681.x

Studies on the mRNAs encoding PAM and on the various PAM proteins have begun to reveal some of the intricate mechanisms used to optimize the ability of this enzyme to carry out the alpha-amidation of peptides. Comparison of the regulatory elements governing expression of the various enzymes involved in peptide processing should reveal common elements. Knowledge of the processing enzymes themselves should help us to understand how these enzymes function in the secretory granule environment. In addition to their catalytic domains, other processing enzymes, like PAM, may well have processing domains and routing domains designed to optimize their ability to function in secretory granules.