Ontology highlight
ABSTRACT:
SUBMITTER: McIntyre NR
PROVIDER: S-EPMC4801743 | biostudies-literature | 2016 Aug
REPOSITORIES: biostudies-literature
McIntyre Neil R NR Lowe Edward W EW Battistini Matthew R MR Leahy James W JW Merkler David J DJ
Journal of enzyme inhibition and medicinal chemistry 20150529 4
Peptidylglycine α-amidating monooxygenase (PAM) is a bifunctional enzyme that catalyzes the final reaction in the maturation of α-amidated peptide hormones. Peptidylglycine α-hydroxylating monooxygenase (PHM) is the PAM domain responsible for the copper-, ascorbate- and O2-dependent hydroxylation of a glycine-extended peptide. Peptidylamidoglycolate lyase is the PAM domain responsible for the Zn(II)-dependent dealkylation of the α-hydroxyglycine-containing precursor to the final α-amidated pepti ...[more]