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Literature summary for 1.14.17.3 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
Search for more literature for 1.14.17.3

Cloned(Commentary)

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

General Stability

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

Inhibitors

Inhibitors Comment Organism Structure
sulfite irreversible inactivation is Cu2+-dependent Rattus norvegicus

Localization

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

Metals/Ions

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

Molecular Weight [Da]

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

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
peptidylglycine + ascorbate + O2 Rattus norvegicus
-
 peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
 ?

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Purification (Commentary)

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

Reaction

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

Source Tissue

Source Tissue Comment Organism Textmining
medullary thyroid carcinoma cell
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-Tyr-Val-Gly + ascorbate + O2
-
 Rattus norvegicus D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
 ?
dansyl-D-Tyr-Val-Gly + ascorbate + O2
-
 Rattus norvegicus 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 Rattus norvegicus ?
-
 ?
peptidylglycine + ascorbate + O2
-
 Rattus norvegicus peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
 ?
peptidylglycine + ascorbate + O2 COOH-terminal glycine Rattus norvegicus peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O semidehydroascorbate ?

Synonyms

Synonyms Comment Organism
alpha-AE
-
 Rattus norvegicus
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

Cofactor Comment Organism Structure
ascorbate dependent on Rattus norvegicus