Copper type II ascorbate-dependent monooxygenase

Copper type II ascorbate-dependent monooxygenase, N-terminal domain
reduced peptidylglycine alpha-hydroxylating monooxygenase in a new crystal form
Identifiers
Symbol	Cu2_monooxygen
Pfam	PF01082
InterPro	IPR000323
PROSITE	PDOC00080
SCOP	1phm
Available protein structures: Pfam structures PDB RCSB PDB; PDBe PDBsum structure summary

Copper type II ascorbate-dependent monooxygenase, C-terminal domain
reduced peptidylglycine alpha-hydroxylating monooxygenase in a new crystal form
Identifiers
Symbol	Cu2_monoox_C
Pfam	PF03712
PROSITE	PDOC00080
SCOP	1phm
Available protein structures: Pfam structures PDB RCSB PDB; PDBe PDBsum structure summary

In molecular biology, the copper type II ascorbate-dependent monooxygenases are a class of enzymes that require copper as a cofactor and which use ascorbate as an electron donor. This family contains two related enzymes, dopamine-beta-monooxygenase EC 1.14.17.1 and peptidylglycine alpha-amidating monooxygenase EC 1.14.17.3. There are a few regions of sequence similarities between these two enzymes, two of these regions contain clusters of conserved histidine residues which are most probably involved in binding copper.^[1]

References

1. ^ Southan C, Kruse LI (September 1989). "Sequence similarity between dopamine beta-hydroxylase and peptide alpha-amidating enzyme: evidence for a conserved catalytic domain". FEBS Lett. 255 (1): 116–20. doi:10.1016/0014-5793(89)81072-5. PMID 2792366. 

This article includes text from the public domain Pfam and InterPro IPR000323