Monooxygenase

Monooxygenase

Structure of the Tetx Monooxygenase in complex with the substrate 7-Iodtetracycline.[1]
Identifiers
Symbol FAD_binding_3
Pfam PF01494
InterPro IPR002938
SCOP 2phh
SUPERFAMILY 2phh

Monooxygenases are enzymes that incorporate one hydroxyl group 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]

Classification

It is classified as an Oxidoreductase enzyme that catalyzes an electron transfer.

Related Structures

2XDO 2XYO 2Y6R

Human proteins containing this domain

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

References

  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.
  2. ↑ 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.
  3. ↑ 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.

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