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CATH Superfamily 2.60.120.310

Copper type II, ascorbate-dependent monooxygenase, N-terminal domain

The name of this superfamily has been modified since the most recent official CATH+ release (v4_3_0). At the point of the last release, this superfamily was named:

"
Copper type II, ascorbate-dependent monooxygenase, N-terminal domain
".

Functional Families

Overview of the Structural Clusters (SC) and Functional Families within this CATH Superfamily. Clusters with a representative structure are represented by a filled circle.
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FunFam 5: Peptidylglycine alpha-hydroxylating monooxygenase

There are 1 EC terms in this cluster

Please note: EC annotations are assigned to the full protein sequence rather than individual protein domains. Since a given protein can contain multiple domains, it is possible that some of the annotations below come from additional domains that occur in the same protein, but have been classified elsewhere in CATH.

Note: The search results have been sorted with the annotations that are found most frequently at the top of the list. The results can be filtered by typing text into the search box at the top of the table.

EC Term Annotations Evidence
Peptidylglycine monooxygenase. [EC: 1.14.17.3]
[Peptide]-glycine + 2 ascorbate + O(2) = [peptide]-(2S)-2-hydroxyglycine + 2 monodehydroascorbate + H(2)O.
  • A copper protein.
  • The enzyme binds two copper ions with distinct roles during catalysis.
  • Peptidylglycines with a neutral amino acid residue in the penultimate position are the best substrates for the enzyme.
  • The product is unstable and dismutates to glyoxylate and the corresponding desglycine peptide amide, a reaction catalyzed by EC 4.3.2.5.
  • In mammals, the two activities are part of a bifunctional protein.
  • Involved in the final step of biosynthesis of alpha-melanotropin and related biologically active peptides.
 5 E2QCL8 E2QCL8 O01404 O01404 Q95XM2