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Contents

   



(Top)
 


1 Classification  





2 Related structures  





3 Human proteins containing this domain  





4 See also  





5 References  





6 External links  














Monooxygenase






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From Wikipedia, the free encyclopedia
 


Monooxygenase
Structure of the TetX monooxygenase in complex with the substrate 7-Iodtetracycline.[1]
Identifiers
SymbolFAD_binding_3
PfamPF01494
InterProIPR002938
SCOP22phh / SCOPe / SUPFAM
Available protein structures:
Pfam  structures / ECOD  
PDBRCSB PDB; PDBe; PDBj
PDBsumstructure summary

Monooxygenases are enzymes that incorporate one hydroxyl group (−OH) into substrates in many metabolic pathways. In this reaction, the two atoms of dioxygen are reduced to one hydroxyl group and one H2O molecule by the concomitant oxidation of NAD(P)H.[2][3] One important subset of the monooxygenases, the cytochrome P450 omega hydroxylases, is used by cells to metabolize arachidonic acid (i.e. eicosatetraenoic acid) to the cell signaling molecules, 20-hydroxyeicosatetraenoic acid or to reduce or totally inactivate the activate signaling molecules for example by hydroxylating leukotriene B4 to 20-hydroxy-leukotriene B5, 5-hydroxyeicosatetraenoic acid to 5,20-dihydroxyeicosatetraenoic acid, 5-oxo-eicosatetraenoic acid to 5-oxo-20-hydroxyeicosatetraenoic acid, 12-hydroxyeicosatetraenoic acid to 12,20-dihydroxyeicosatetraenoic acid, and epoxyeicosatrienoic acids to 20-hydroxy-epoxyeicosatrienoic acids.

Classification[edit]

They are classified as oxidoreductase enzymes that catalyze an electron transfer.

Related structures[edit]

2XDO 2XYO 2Y6R

Human proteins containing this domain[edit]

COQ6; CYP450; MICAL1; MICAL2; MICAL2PV1; MICAL2PV2; MICAL3;

See also[edit]

References[edit]

  1. ^ PDB: 2Y6Q​; Volkers G, Palm GJ, Weiss MS, Wright GD, Hinrichs W (April 2011). "Structural basis for a new tetracycline resistance mechanism relying on the TetX monooxygenase". FEBS Lett. 585 (7): 1061–6. doi:10.1016/j.febslet.2011.03.012. PMID 21402075. S2CID 26967337.
  • ^ Harayama S, Kok M, Neidle EL (1992). "Functional and evolutionary relationships among diverse oxygenases". Annu. Rev. Microbiol. 46: 565–601. doi:10.1146/annurev.mi.46.100192.003025. PMID 1444267.
  • ^ Schreuder HA, van Berkel WJ, Eppink MH, Bunthol C (1999). "Phe161 and Arg166 variants of p-hydroxybenzoate hydroxylase. Implications for NADPH recognition and structural stability". FEBS Lett. 443 (3): 251–255. doi:10.1016/S0014-5793(98)01726-8. PMID 10025942. S2CID 21305517.
  • External links[edit]

    This article incorporates text from the public domain Pfam and InterPro: IPR002938

    Retrieved from "https://en.wikipedia.org/w/index.php?title=Monooxygenase&oldid=1170980511"

    Categories: 
    Protein domains
    Enzymes
    Hidden category: 
    Commons category link is on Wikidata
     



    This page was last edited on 18 August 2023, at 09:23 (UTC).

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