title: The 108-kDA peptidylglycine alpha-amidating monooxygenase precursor contains two separable enzymatic activities involved in peptide amidation.
abstract: A 43-kDa protein factor that increases the ability of purified bovine peptidylglycine alpha-amidating monooxygenase (PAM)-A and -B to produce alpha-amidated peptides at physiological pH was purified to homogeneity from bovine neurointermediate pituitary. At each step of the purification, the amount of activity correlated with the amount of protein detected on Western blots by antibody to bovine PAM(561-579). In the bovine neurointermediate pituitary the 108-kDa PAM precursor protein is cleaved to form a peptidylglycine alpha-hydroxylating monooxygenase and a peptidyl-alpha-hydroxyglycine alpha-amidating lyase, which function sequentially in the 2-step formation of alpha-amidated peptides.
authors.affiliation: Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205.
authors.forename: S N
authors.initials: SN
authors.lastname: Perkins
authors.forename: E J
authors.initials: EJ
authors.lastname: Husten
authors.forename: B A
authors.initials: BA
authors.lastname: Eipper
mesh_terms: D019760:Amidine-Lyases; D000818:Animals; D015153:Blotting, Western; D002417:Cattle; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange; D004792:Enzyme Precursors / Q000302:isolation & purification* / Q000378:metabolism; D006836:Hydro-Lyases / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D007700:Kinetics; D006899:Mixed Function Oxygenases / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D008970:Molecular Weight; D009097:Multienzyme Complexes; D010902:Pituitary Gland / Q000201:enzymology*; D011499:Protein Processing, Post-Translational
chemical_list: D004792:Enzyme Precursors; D009097:Multienzyme Complexes; D006899:Mixed Function Oxygenases; C035189:peptidylglycine monooxygenase; D006836:Hydro-Lyases; D019760:Amidine-Lyases; C068521:peptidylamidoglycolate lyase