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Literature summary extracted from

  • Suzuki, K.; Ohta, M.; Okamoto, M.; Nishikawa, Y.
    Functional expression and characterization of a Xenopus laevis peptidylglycine alpha-amidating monooxygenase, AE-II, in insect-cell culture (1993), Eur. J. Biochem., 213, 93-98.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.17.3 expression in Spodoptera fugiperda cells via baculovirus vector of membrane-associated, bifunctional enzyme form 2, AE-II, wild-type and truncated mutant, N-terminal amino acid sequence analysis Xenopus laevis

Protein Variants

EC Number Protein Variants Comment Organism
1.14.17.3 additional information construction of a truncated form of AE-II, lacking the transmembrane domain and leading to solubility of the fully active, truncated enzyme being secreted into the culture medium from Spodoptera frugiperda cells Xenopus laevis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.17.3 D-Tyr-Val-Gly inhibition above 20 mM of hydroxylation Xenopus laevis

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.14.17.3 3.5
-
 N-dansyl-L-Tyr-L-Phe-Gly recombinant mutant AE-II, form 2 Xenopus laevis
1.14.17.3 3.5
-
 N-dansyl-L-Tyr-L-Phe-Gly reaction product of step 1, substrate of step 2 Xenopus laevis
1.14.17.3 4.5
-
 N-dansyl-L-Tyr-L-Phe-Gly recombinant mutant AE-II, form 2 Xenopus laevis

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.17.3 membrane transmembranal protein Xenopus laevis 16020
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.17.3 Cu2+
-
 Xenopus laevis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.17.3 74000
-
 1 * 74000, recombinant mutant AE-II, form 2, SDS-PAGE Xenopus laevis
1.14.17.3 78000
-
 recombinant mutant AE-II, form 2, 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
-
 3 genetic forms, 2 protein forms of amidating enzyme: protein form 1, gene AE-I, has only peptidylglycine alpha-hydroxylating activity, protein form 2, genes AE-III and AE-II, show peptidylglycine alpha-hydroxylating activity and peptidylhydroxylglycine N-C lyase activity
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.17.3 truncated mutant form 2 from gene AE-II, recombinant from Spodoptera frugiperda cell expression system Xenopus laevis

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.17.3 skin soluble enzyme with peptidylglycine alpha-hydroxylating activity or peptidylhydroxylglycine N-C lyase activity 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
-
 ?

Subunits

EC Number Subunits Comment Organism
1.14.17.3 monomer 1 * 74000, recombinant mutant AE-II, form 2, SDS-PAGE Xenopus laevis

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

Cofactor

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