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ENZYME

ENZYME entry: EC 1.14.17.3

PURL: https://purl.expasy.org/enzyme/EC/1.14.17.3
Accepted Name
peptidylglycine monooxygenase
Alternative Name(s)
PAM
peptidyl alpha-amidating enzyme
peptidylglycine 2-hydroxylase
peptidylglycine alpha-amidating monooxygenase
Reaction catalysed
a [peptide]-C-terminal glycine + 2 L-ascorbate + O2 = a [peptide]-C-terminal (2S)-2-hydroxyglycine + 2 monodehydro-L-ascorbate radical + H2O
Comment(s)
  • A copper protein.
  • The enzyme binds two copper ions with distinct roles during catalysis.
  • Peptidylglycines with a neutral amino acid residue in the penultimate position are the best substrates for the enzyme.
  • The product is unstable and dismutates to glyoxylate and the corresponding desglycine peptide amide, a reaction catalyzed by EC 4.3.2.5.
  • In mammals, the two activities are part of a bifunctional protein.
  • Involved in the final step of biosynthesis of alpha-melanotropin and related biologically active peptides.
Cross-references
BRENDA1.14.17.3
EC2PDB1.14.17.3
ExplorEnz1.14.17.3
KEGG Ligand Database for Enzyme Nomenclature1.14.17.3
IUBMB Enzyme Nomenclature1.14.17.3
MEDLINEFind literature relating to 1.14.17.3
MetaCyc1.14.17.3
Rhea expert-curated reactions1.14.17.3
UniProtKB/Swiss-Prot
P08478, AMDA_XENLAP12890, AMDB_XENLAP83388, AMDL_CAEEL
P10731, AMD_BOVINP19021, AMD_HUMANP97467, AMD_MOUSE
P14925, AMD_RATQ95XM2, PHM_CAEELO01404, PHM_DROME

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