Monooxygenase
From Proteopedia
(Difference between revisions)
												
			
			| Line 5: | Line 5: | ||
'''Monooxygenases''' (MO) catalyzes the incorporation of a hydroxyl group into a variety of substrates.  MO catalyzes the reduction of O<sub>2</sub> to H<sub>2</sub>O while oxidating NADPH.  | '''Monooxygenases''' (MO) catalyzes the incorporation of a hydroxyl group into a variety of substrates.  MO catalyzes the reduction of O<sub>2</sub> to H<sub>2</sub>O while oxidating NADPH.  | ||
*'''ActVA-Orf6 monooxygenase''' catalyses the oxidation of an aromatic intermediate of the actinorhodin pathway <ref>PMID:12514126</ref>.  | *'''ActVA-Orf6 monooxygenase''' catalyses the oxidation of an aromatic intermediate of the actinorhodin pathway <ref>PMID:12514126</ref>.  | ||
| + | *'''Baeyer-Villigen monooxygenase''' is a bioanalytic tool which can catalyze reactions which are difficult to do via chemical means<ref>PMID:15599520</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>===  | === 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 09:24, 15 July 2024
  | |||||||||||
References
- ↑ Sciara G, Kendrew SG, Miele AE, Marsh NG, Federici L, Malatesta F, Schimperna G, Savino C, Vallone B. The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis. EMBO J. 2003 Jan 15;22(2):205-15. PMID:12514126 doi:http://dx.doi.org/10.1093/emboj/cdg031
 - ↑ Fraaije MW, Wu J, Heuts DP, van Hellemond EW, Spelberg JH, Janssen DB. Discovery of a thermostable Baeyer-Villiger monooxygenase by genome mining. Appl Microbiol Biotechnol. 2005 Jan;66(4):393-400. PMID:15599520 doi:10.1007/s00253-004-1749-5
 - ↑ 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

