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Copper type II ascorbate-dependent monooxygenase

From Wikipedia, the free encyclopedia

Copper type II ascorbate-dependent monooxygenase, N-terminal domain
reduced peptidylglycine alpha-hydroxylating monooxygenase in a new crystal form
Identifiers
SymbolCu2_monooxygen
PfamPF01082
InterProIPR000323
PROSITEPDOC00080
SCOP21phm / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary
Copper type II ascorbate-dependent monooxygenase, C-terminal domain
reduced peptidylglycine alpha-hydroxylating monooxygenase in a new crystal form
Identifiers
SymbolCu2_monoox_C
PfamPF03712
PROSITEPDOC00080
SCOP21phm / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure 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 Letters. 255 (1): 116–20. doi:10.1016/0014-5793(89)81072-5. PMID 2792366. S2CID 84464131.
This article incorporates text from the public domain Pfam and InterPro: IPR000323

External links

This page was last edited on 6 March 2023, at 01:19
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