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Literature summary for 1.14.17.3 extracted from

  • Bradbury, A.F.; Finnie, M.D.A.; Smyth, D.G.
    Mechanism of C-terminal amide formation by pituitary enzymes (1982), Nature, 298, 686-689.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
secretory granule
-
Sus scrofa 30141
-

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
60000
-
gel filtration Sus scrofa
60000
-
shows reversible aggregation with MW of 100000 Sus scrofa

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Reaction

Reaction Comment Organism Reaction ID
[peptide]-glycine + 2 ascorbate + O2 = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H2O mechanism Sus scrofa

Source Tissue

Source Tissue Comment Organism Textmining
pituitary gland
-
Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-Tyr-Val-Gly + ascorbate + O2
-
Sus scrofa D-Tyr-Val-2-hydroxyglycine + dehydroascorbate + H2O
-
?
additional information substrates are also physiologically relevant peptides related to alpha-melanotropine Sus scrofa ?
-
?
peptidylglycine + ascorbate + O2
-
Sus scrofa peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
?
peptidylglycine + ascorbate + O2 COOH-terminal glycine Sus scrofa peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
?

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Sus scrofa

Cofactor

Cofactor Comment Organism Structure
ascorbate dependent on Sus scrofa