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Literature summary for 1.14.17.3 extracted from

  • Takahashi, K.; Onami, T.; Noguchi, M.
    Kinetic isotope effects of peptidylglycine a-hydroxylating mono-oxygenase reaction (1998), Biochem. J., 336, 131-137.
No PubMed abstract available

Cloned(Commentary)

Cloned (Comment) Organism
expression in Spodoptera fugiperda cells via baculovirus vector, amino acid sequence analysis Xenopus laevis

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+
-
Xenopus laevis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
peptidylglycine + ascorbate + O2 Xenopus laevis
-
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
?

Organism

Organism UniProt Comment Textmining
Xenopus laevis
-
peptidylglycine alpha-hydroxylating monooxygenase activity
-

Purification (Commentary)

Purification (Comment) Organism
native wild-type and recombinant from Spodoptera frugiperda cell expression system Xenopus laevis

Reaction

Reaction Comment Organism Reaction ID
[peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O mechanism Xenopus laevis
[peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O ping-pong-mechanism Xenopus laevis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-Tyr-Val-Gly + ascorbate + O2
-
Xenopus laevis D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
?
additional information EC 1.14.17.3 is often called peptidylglycine alpha-amidating monooxygenase (PAM) and the alpha-amidated product is mentioned as the product of the reaction, but the alpha-amidation of glycine-extended peptides is a two-step process catalyzed by 2 enzymes: 1. EC 1.14.17.3: production of peptidyl(2-hydroxyglycine) by a copper, molecular oxygen and ascorbate-dependent peptidyl-glycine alpha-hydroxylating monooxygenase (PMH) and 2. conversion of the peptidyl-alpha-hydroxyglycine derivative into an alpha-amidated product at physiological pH by peptidyl-alpha-hydroxyglycine alpha-amidating lyase Xenopus laevis ?
-
?
peptidylglycine + ascorbate + O2
-
Xenopus laevis peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
?
peptidylglycine + ascorbate + O2 COOH-terminal glycine Xenopus laevis peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
?

Synonyms

Synonyms Comment Organism
More EC 1.14.17.3 is often called peptidylglycine alpha-amidating monooxygenase (PAM) and the alpha-amidated product is mentioned as the product of the reaction, but the alpha-amidation of glycine-extended peptides is a two-step process catalyzed by 2 enzymes: 1. EC 1.14.17.3: production of peptidyl(2-hydroxyglycine) by a copper, molecular oxygen and ascorbate-dependent peptidyl-glycine alpha-hydroxylating monooxygenase (PHM), 2. conversion of the peptidyl-alpha-hydroxyglycine derivative into an alpha-amidated product at physiological pH by peptidyl-alpha-hydroxyglycine alpha-amidating lyase (PHL) Xenopus laevis

Cofactor

Cofactor Comment Organism Structure
ascorbate dependent on Xenopus laevis