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Peptidyl-glycine alpha-amidating monooxygenase
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AMD_HUMAN
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1.14.17.3, 4.3.2.5, PAL, PAM, PHM, Peptidyl-alpha-hydroxyglycine alpha-amidating lyase, Peptidylamidoglycolate lyase, Peptidylglycine alpha-hydroxylating monooxygenase
http://www.biopax.org/relea...
FUNCTION: Bifunctional enzyme that catalyzes 2 sequential steps in C-terminal alpha-amidation of peptides. The monooxygenase part produces an unstable peptidyl(2-hydroxyglycine) intermediate that is dismutated to glyoxylate and the corresponding desglycine peptide amide by the lyase part. C-terminal amidation of peptides such as neuropeptides is essential for full biological activity. CATALYTIC ACTIVITY: Peptidylglycine + ascorbate + O(2) = peptidyl(2-hydroxyglycine) + dehydroascorbate + H(2)O. CATALYTIC ACTIVITY: Peptidylamidoglycolate = peptidyl amide + glyoxylate. COFACTOR: Zinc; for the lyase reaction. COFACTOR: Binds 2 copper ions per subunit; For the monoxygenase reaction. ENZYME REGULATION: Inhibited by EDTA, phenylglyoxal and diethyl pyrocarbonate. SUBUNIT: Monomer. Interacts with RASSF9 (By similarity). SUBCELLULAR LOCATION: Isoform 1: Membrane; Single-pass type I membrane protein. SUBCELLULAR LOCATION: Isoform 2: Membrane; Single-pass type I membrane protein. SUBCELLULAR LOCATION: Isoform 3: Secreted. Note=Secreted from secretory granules. SUBCELLULAR LOCATION: Isoform 4: Secreted. Note=Secreted from secretory granules. ALTERNATIVE PRODUCTS: Event=Alternative splicing; Named isoforms=5; Comment=Additional isoforms seem to exist; Name=1; IsoId=P19021-1; Sequence=Displayed; Name=2; IsoId=P19021-2; Sequence=VSP_001227; Name=3; IsoId=P19021-3; Sequence=VSP_001228; Name=4; IsoId=P19021-4; Sequence=VSP_001229; Name=5; IsoId=P19021-5; Sequence=VSP_038691; SIMILARITY: In the C-terminal section; belongs to the peptidyl- alpha-hydroxyglycine alpha-amidating lyase family. SIMILARITY: In the N-terminal section; belongs to the copper type II ascorbate-dependent monooxygenase family. SIMILARITY: Contains 5 NHL repeats. SEQUENCE CAUTION: Sequence=AAD01439.1; Type=Erroneous initiation; COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License.
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