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Literature summary for 1.14.17.3 extracted from

  • Chufan, E.E.; Prigge, S.T.; Siebert, X.; Eipper, B.A.; Mains, R.E.; Amzel, L.M.
    Differential reactivity between two copper sites in peptidylglycine alpha-hydroxylating monooxygenase (2010), J. Am. Chem. Soc., 132, 15565-15572.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
truncated version (residues 42-356) expressed in CHO cell Rattus norvegicus

Crystallization (Commentary)

Crystallization (Comment) Organism
hanging-drop diffusion method at 293 K Rattus norvegicus

Protein Variants

Protein Variants Comment Organism
additional information protein containing residues 42-356 Rattus norvegicus

Metals/Ions

Metals/Ions Comment Organism Structure
Cu2+
-
Rattus norvegicus

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
peptidylglycine + 2 ascorbate + O2
-
Rattus norvegicus peptidyl(2-hydroxyglycine) + 2 semidehydroascorbate + H2O
-
?

Synonyms

Synonyms Comment Organism
peptidylglycine alpha-hydroxylating monooxygenase
-
Rattus norvegicus