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Literature summary extracted from

  • Merkler, D.J.; Kulathila, R.; Francisco, W.A.; Ash, D.E.; Bell, J.
    The irreversible inactivation of two copper-dependent monooxygenases by sulfite: peptidylglycine alpha-amidating enzyme and dopamine beta-monooxygenase (1995), FEBS Lett., 366, 165-169.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.14.17.3 medullary thyroid alpha-AE, type A, expression in chinese hamster ovary cells Rattus norvegicus

General Stability

EC Number General Stability Organism
1.14.17.3 substance-P, i.e. RPKPQQFFGLM-NH2, protects against inactivation by sulfite Rattus norvegicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.14.17.1 Na2SO3
-
Bos taurus
1.14.17.3 sulfite irreversible inactivation is Cu2+-dependent Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.14.17.3 extracellular recombinant enzyme secreted into medium Rattus norvegicus
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.14.17.1 Cu2+ a copper protein Bos taurus
1.14.17.3 Cu2+ Cu2+ is absolutely required for optimal activity Rattus norvegicus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.14.17.3 75000
-
recombinant form A, gel filtration and SDS-PAGE Rattus norvegicus

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 Rattus norvegicus
-
peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.14.17.1 Bos taurus
-
-
-
1.14.17.3 Rattus norvegicus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.14.17.3 type A alpha-AE, recombinant from chinese hamster ovary cells Rattus norvegicus

Reaction

EC Number Reaction Comment Organism Reaction ID
1.14.17.3 [peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O kinetic model for slow-binding inhibition Rattus norvegicus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.14.17.1 adrenal gland
-
Bos taurus
-
1.14.17.3 medullary thyroid carcinoma cell
-
Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.14.17.1 3,4-dihydroxyphenethylamine + ascorbate + O2
-
Bos taurus noradrenaline + dehydroascorbate + H2O
-
?
1.14.17.1 tyramine + ascorbate + O2
-
Bos taurus octopamine + dehydroascorbate + H2O
-
?
1.14.17.3 D-Tyr-Val-Gly + ascorbate + O2
-
Rattus norvegicus D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
?
1.14.17.3 dansyl-D-Tyr-Val-Gly + ascorbate + O2
-
Rattus norvegicus 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 Rattus norvegicus ?
-
?
1.14.17.3 peptidylglycine + ascorbate + O2
-
Rattus norvegicus peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
?
1.14.17.3 peptidylglycine + ascorbate + O2 COOH-terminal glycine Rattus norvegicus peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O semidehydroascorbate ?

Synonyms

EC Number Synonyms Comment Organism
1.14.17.3 alpha-AE
-
Rattus norvegicus
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) Rattus norvegicus

Cofactor

EC Number Cofactor Comment Organism Structure
1.14.17.3 ascorbate dependent on Rattus norvegicus