Monooxygenase

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'''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>.
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*'''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

Glycosylated lytic polysaccharide monooxygenase complex with Cu(II) (orange) and peroxide (PDB code 5tkh)

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References

  1. 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
  2. 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
  3. 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

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