Biology:Copper type II ascorbate-dependent monooxygenase
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Short description: Class of enzymes
Copper type II ascorbate-dependent monooxygenase, N-terminal domain | |||||||||
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reduced peptidylglycine alpha-hydroxylating monooxygenase in a new crystal form | |||||||||
Identifiers | |||||||||
Symbol | Cu2_monooxygen | ||||||||
Pfam | PF01082 | ||||||||
InterPro | IPR000323 | ||||||||
PROSITE | PDOC00080 | ||||||||
SCOP2 | 1phm / SCOPe / SUPFAM | ||||||||
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Copper type II ascorbate-dependent monooxygenase, C-terminal domain | |||||||||
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reduced peptidylglycine alpha-hydroxylating monooxygenase in a new crystal form | |||||||||
Identifiers | |||||||||
Symbol | Cu2_monoox_C | ||||||||
Pfam | PF03712 | ||||||||
PROSITE | PDOC00080 | ||||||||
SCOP2 | 1phm / SCOPe / SUPFAM | ||||||||
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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
- ↑ "Sequence similarity between dopamine beta-hydroxylase and peptide alpha-amidating enzyme: evidence for a conserved catalytic domain". FEBS Letters 255 (1): 116–20. September 1989. doi:10.1016/0014-5793(89)81072-5. PMID 2792366.
External links
- Eukaryotic Linear Motif resource motif class MOD_Cter_Amidation
Original source: https://en.wikipedia.org/wiki/Copper type II ascorbate-dependent monooxygenase.
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