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Literature summary for 1.14.17.3 extracted from

  • Shimoi, H.; Kawahara, T.; Suzuki, K.; Iwasaki, Y.; Jeng, A.Y.; Nishikawa, Y.
    Characterization of a Xenopus laevis skin peptidylglycine alpha-hydroxylating monooxygenase expressed in insect-cell culture (1992), Eur. J. Biochem., 209, 189-194.
    View publication on PubMed
Search for more literature for 1.14.17.3

Activating Compound

Activating Compound Comment Organism Structure
acetate form 1, AE-I, activates below pH 6.0 Xenopus laevis
chloride form 1, AE-I, activates below pH 6.0 Xenopus laevis
Iodide form 1, AE-I, activates below pH 6.0 Xenopus laevis

Cloned(Commentary)

Cloned (Comment) Organism
expression in Spodoptera fugiperda cells via baculovirus vector of soluble form 1, AE-I showing only peptidylglycine alpha-hydroxylating activity Xenopus laevis

General Stability

General Stability Organism
stabilized by salts like KI and KCl, recombinant form 1, AE-I Xenopus laevis

Inhibitors

Inhibitors Comment Organism Structure
additional information form 1, AE-I, competitive inhibition by tripeptides with C-terminal glycine, most effective is methione within these peptides Xenopus laevis

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+ Cu2+ is absolutely required for optimal activity 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
-
 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
-

Reaction

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

Source Tissue

Source Tissue Comment Organism Textmining
skin soluble enzyme with peptidylglycine alpha-hydroxylating activity, AE-I Xenopus laevis
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
dansyl-D-Tyr-Val-Gly + ascorbate + O2
-
 Xenopus laevis dansyl-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 requirement for 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

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
6
-
 MES buffer, recombinant from 1, AE-I Xenopus laevis
7
-
 phosphate buffer, recombinant form 1, AE-I Xenopus laevis

Cofactor

Cofactor Comment Organism Structure
ascorbate dependent on Xenopus laevis