Peptidylglycine alpha-amidating monooxygenase activity in spinal cord, dorsal roots, and dorsal root ganglia of Macaca fascicularis.
Several peptides synthesized by primary sensory neurons are alpha-amidated at the C-terminal residue, including vasoactive intestinal polypeptide, neurokinin A and substance P, which is also abundant in spinal cord. In pituitary and other tissues, the C-terminal amidation is catalyzed by peptidylglycine alpha-amidating monooxygenase (PAM). In the present study, soluble PAM activity in spinal cord and in primary sensory neurons is quantified and characterized as to cofactor and cosubstrate requirements and substrate specificity.
Laboratory of Human Biochemistry, Children's Hospital, Boston, MA 02115.
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Graham
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Gallop
D000818:Animals; D005727:Ganglia, Spinal / Q000201:enzymology*; D008251:Macaca / Q000378:metabolism*; D006899:Mixed Function Oxygenases; D009097:Multienzyme Complexes; D009479:Neuropeptides / Q000378:metabolism; D000587:Oxidoreductases Acting on CH-NH Group Donors / Q000378:metabolism*; D013116:Spinal Cord / Q000201:enzymology*; D013126:Spinal Nerve Roots / Q000201:enzymology*
D009097:Multienzyme Complexes; D009479:Neuropeptides; D006899:Mixed Function Oxygenases; C035189:peptidylglycine monooxygenase; D000587:Oxidoreductases Acting on CH-NH Group Donors