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Literature summary for 1.14.17.3 extracted from

  • Iwasaki, Y.; Shimoi, H.; Saiki, H.; Nishikawa, Y.
    Tissue-specific molecular diversity of amidating enzymes (peptidylglycine alpha-hydroxylating monooxygenase and peptidylhydroxyglycine N-C lyase) in Xenopus laevis (1993), Eur. J. Biochem., 214, 811-818.
    View publication on PubMed
Search for more literature for 1.14.17.3

Cloned(Commentary)

Cloned (Comment) Organism
expression in Spodoptera fugiperda cells via baculovirus vector of membrane-associated, bifunctional enzyme form 2, AE-III Xenopus laevis

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasm peptidylglycine alpha-hydroxylating activity and peptidylhydroxylglycine N-C lyase activity Xenopus laevis 5737
-
membrane recombinant bifunctional enzyme form 2, uncleaved in insect cells Xenopus laevis 16020
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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
-
 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
-

Source Tissue

Source Tissue Comment Organism Textmining
brain predominantly membrane-associated, bifunctional enzyme Xenopus laevis
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heart predominantly membrane-associated, bifunctional enzyme Xenopus laevis
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heart atrium Xenopus laevis
-
heart ventricle Xenopus laevis
-
additional information tissue distribution, overview Xenopus laevis
-
skin soluble enzyme with peptidylglycine alpha-hydroxylating activity or peptidylhydroxylglycine N-C lyase activity Xenopus laevis
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.0124
-
 skin, peptidylhydroxylglycine N-C lyase, highest activity of all tissues Xenopus laevis
0.0206
-
 skin, peptidylglycine alpha-hydroxylating activity, highest activity of all tissues 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 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

Temperature Optimum [°C]

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

Cofactor

Cofactor Comment Organism Structure
ascorbate dependent on Xenopus laevis