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Literature summary extracted from

  • Suzuki, K.; Shimoi, H.; Iwasaki, Y.; Kawahara, T.; Matsuura, Y.; Nishikawa, Y.
    Elucidation of amidating reaction mechanism by frog amidating enzyme, peptidylglycine alpha-hydroxylating monooxygenase, expressed in insect cell culture (1990), EMBO J., 9, 4259-4265.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.17.3 expression in Spodoptera fugiperda cells via baculovirus vector, amino acid sequence analysis Xenopus laevis
4.3.2.5 expression in cultured Sf9 insect cells Xenopus laevis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.17.3 EDTA
-
 Xenopus laevis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.17.3 0.0032
-
 N-dansyl-Tyr-Phe-Gly + 2 mM L-ascorbate Xenopus laevis
1.14.17.3 0.28
-
 L-ascorbate + 0.02 mM N-dansyl-Tyr-Phe-Gly Xenopus laevis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.17.3 Cu2+ a copper protein Xenopus laevis
1.14.17.3 Cu2+ Cu2+ is absolutely required for optimal activity Xenopus laevis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.17.3 39000
-
 SDS-PAGE, gel filtration Xenopus laevis
1.14.17.3 39000
-
 native wild-type enzyme Xenopus laevis
1.14.17.3 43000
-
 recombinant wild-type enzyme, SDS-PAGE, gel filtration Xenopus laevis

Natural Substrates/ Products (Substrates)

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

Organism

EC Number Organism UniProt Comment Textmining
1.14.17.3 Xenopus laevis
-
-
-
4.3.2.5 Xenopus laevis
-
-
-

Purification (Commentary)

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

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.17.3 [peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O mechanism Xenopus laevis
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.17.3 skin
-
 Xenopus laevis
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.14.17.3 16
-
 purified recombinant enzyme Xenopus laevis
4.3.2.5 16000000
-
 Mono Q fraction Xenopus laevis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.17.3 Ala-Ile-Gly-Val-Gly-Ala-Pro-Gly + ascorbate + O2
-
 Xenopus laevis Ala-Ile-Gly-Val-Gly-Ala-Pro-2-hydroxyglycine + dehydroascorbate + H2O
-
 ?
1.14.17.3 dansyl-D-Tyr-Val-Gly + ascorbate + O2
-
 Xenopus laevis dansyl-D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
 ?
1.14.17.3 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 ?
-
 ?
1.14.17.3 N-dansyl-L-Tyr-L-Phe-Gly + ascorbate + O2
-
 Xenopus laevis N-dansyl-L-Tyr-L-Phe-2-hydroxyglycine + dehydroascorbate + H2O
-
 r
1.14.17.3 peptidylglycine + ascorbate + O2
-
 Xenopus laevis peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
 ?
1.14.17.3 peptidylglycine + ascorbate + O2 COOH-terminal glycine Xenopus laevis peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
 ?
4.3.2.5 alpha-hydroxyglycine-extended peptide
-
 Xenopus laevis peptidyl amide + glyoxylate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
1.14.17.3 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

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.14.17.3 30
-
 assay at Xenopus laevis

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.14.17.3 5.4
-
 assay at, recombinant enzyme Xenopus laevis
1.14.17.3 5.5 6
-
 Xenopus laevis

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.17.3 ascorbate dependent on Xenopus laevis