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Literature summary extracted from

  • Abad, E.; Rommel, J.B.; Kaestner, J.
    Reaction mechanism of the bicopper enzyme peptidylglycine alpha-hydroxylating monooxygenase (2014), J. Biol. Chem., 289, 13726-13738 .
    View publication on PubMedView publication on EuropePMC

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.17.3 Cu2+ a bicopper enzyme, two noninteracting copper atoms, involved in reaction mechanism, detailed overview Rattus norvegicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.14.17.3 calcitonin + ascorbate + O2 Rattus norvegicus
-
 ? + dehydroascorbate + H2O
-
 ?
1.14.17.3 oxytoxin + ascorbate + O2 Rattus norvegicus
-
 ? + dehydroascorbate + H2O
-
 ?
1.14.17.3 peptidylglycine + ascorbate + O2 Rattus norvegicus
-
 peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
 ?
1.14.17.3 substance P + ascorbate + O2 Rattus norvegicus
-
 ? + dehydroascorbate + H2O
-
 ?
1.14.17.3 thyrotropin + ascorbate + O2 Rattus norvegicus
-
 ? + dehydroascorbate + H2O
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.14.17.3 Rattus norvegicus P14925
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.17.3 [peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O reaction mechanism simulation using quantum mechanics/molecular mechanics calculations, molecular dynamics simulations, and the enzyme crystal structure, PDB 1SDW, detailed overview. The overall reaction of PHM consists of a stereospecific hydroxylation of the pro-S hydrogen using molecular O2 as oxygen source. Two electrons and two protons are consumed during the reaction. Ascorbate is the best (but not the only possible) reductant. In the protein resting state, both copper atoms are in the +2 oxidation state and are reduced by ascorbate to +1. Molecular oxygen then binds to CuM as the substrate binds to the protein. first and rate-limiting step is hydrogen abstraction, second step is OH rebinding via double protonated intermediate and transition state (TS2) Rattus norvegicus
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.17.3 calcitonin + ascorbate + O2
-
 Rattus norvegicus ? + dehydroascorbate + H2O
-
 ?
1.14.17.3 oxytoxin + ascorbate + O2
-
 Rattus norvegicus ? + dehydroascorbate + H2O
-
 ?
1.14.17.3 peptidylglycine + ascorbate + O2
-
 Rattus norvegicus peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
 ?
1.14.17.3 substance P + ascorbate + O2
-
 Rattus norvegicus ? + dehydroascorbate + H2O
-
 ?
1.14.17.3 thyrotropin + ascorbate + O2
-
 Rattus norvegicus ? + dehydroascorbate + H2O
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.17.3 PAM
-
 Rattus norvegicus
1.14.17.3 peptidylglycine alpha-hydroxylating monooxygenase
-
 Rattus norvegicus
1.14.17.3 PHM
-
 Rattus norvegicus

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.17.3 ascorbate
-
 Rattus norvegicus

General Information

EC Number General Information Comment Organism
1.14.17.3 additional information solvent-exposed active site of enzyme PHM Rattus norvegicus
1.14.17.3 physiological function peptidylglycine alpha-hydroxylating monooxygenase catalyzes the generation of C-terminal carboxamides of peptide hormones, neurotransmitters, and growth factors for biological activation. The enzyme is a noninteracting bicopper enzyme that stereospecifically hydroxylates the terminal glycine of small peptides for its later amidation. Neuroendocrine messengers, such as oxytocin, rely on the biological activity of this enzyme. Each catalytic turnover requires one oxygen molecule, two protons from the solvent, and two electrons Rattus norvegicus