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 | ||||||||
| SUPERFAMILY | 1phm | ||||||||
| |||||||||
| 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 | ||||||||
| SUPERFAMILY | 1phm | ||||||||
| |||||||||
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
- ↑ 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 incorporates text from the public domain Pfam and InterPro IPR000323
External links
- Eukaryotic Linear Motif resource motif class MOD_Cter_Amidation
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