This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
Monooxygenase
From Proteopedia
(Difference between revisions)
| Line 3: | Line 3: | ||
== Function == | == Function == | ||
| - | '''Monooxygenases''' (MO) catalyzes the incorporation of a hydroxyl group into a variety of substrates. MO catalyzes the reduction of | + | '''Monooxygenases''' (MO) catalyzes the incorporation of a hydroxyl group into a variety of substrates. MO catalyzes the reduction of O<sub/2/> to H2O while oxidating NADPH. |
=== Peptidylglycine α-Hydroxylating Monooxygenase (PHM)-coordination of peroxide to Cu<sub>M</sub> center. Structural and computational study <ref >doi 10.1007/s00775-012-0967-z</ref>=== | === Peptidylglycine α-Hydroxylating Monooxygenase (PHM)-coordination of peroxide to Cu<sub>M</sub> center. Structural and computational study <ref >doi 10.1007/s00775-012-0967-z</ref>=== | ||
Revision as of 08:30, 24 July 2017
| |||||||||||
3D structures of monooxygenase
Updated on 24-July-2017
Methane monooxygenase See Methane monooxygenase
Camphor 5-monooxygenase See Cytochrome P450
Luciferin 4-monooxygenase and Alkanal monooxygenase See Luciferase
References
- ↑ Rudzka K, Moreno DM, Eipper B, Mains R, Estrin DA, Amzel LM. Coordination of peroxide to the Cu(M) center of peptidylglycine alpha-hydroxylating monooxygenase (PHM): structural and computational study. J Biol Inorg Chem. 2012 Dec 18. PMID:23247335 doi:10.1007/s00775-012-0967-z
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Joel L. Sussman, Alexander Berchansky, Jaime Prilusky
