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Literature summary for 1.14.17.3 extracted from

  • Gaier, E.D.; Miller, M.B.; Ralle, M.; Aryal, D.; Wetsel, W.C.; Mains, R.E.; Eipper, B.A.
    Peptidylglycine alpha-amidating monooxygenase heterozygosity alters brain copper handling with region specificity (2013), J. Neurochem., 127, 605-619.
    View publication on PubMedView publication on EuropePMC

Metals/Ions

Metals/Ions Comment Organism Structure
copper a cuproenzyme Mus musculus

Natural Substrates/ Products (Substrates)

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

Organism

Organism UniProt Comment Textmining
Mus musculus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
amygdala
-
Mus musculus
-
brain
-
Mus musculus
-
brain cortex
-
Mus musculus
-
hippocampus
-
Mus musculus
-
interneuron
-
Mus musculus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
peptidylglycine + ascorbate + O2
-
Mus musculus peptidyl(2-hydroxyglycine) + dehydroascorbate + H2O
-
?

Synonyms

Synonyms Comment Organism
PAM
-
Mus musculus
peptidylglycine alpha-amidating monooxygenase
-
Mus musculus

Cofactor

Cofactor Comment Organism Structure
ascorbate
-
Mus musculus

General Information

General Information Comment Organism
physiological function the enzyme is a regulator of copper homeostasis in neuroendocrine cells Mus musculus