IUBMB Enzyme Nomenclature


Accepted name: phenol 2-monooxygenase (FADH2)

Reaction: phenol + FADH2 + O2 = catechol + FAD + H2O

For diagram of reaction click here.

Other name(s): pheA1 (gene name)

Systematic name: phenol,FADH2:oxygen oxidoreductase (2-hydroxylating)

Comments: The enzyme catalyses the ortho-hydroxylation of simple phenols into the corresponding catechols. It accepts 4-methylphenol, 4-chlorophenol, and 4-fluorophenol [1] as well as 4-nitrophenol, 3-nitrophenol, and resorcinol [3]. The enzyme is part of a two-component system that also includes an NADH-dependent flavin reductase. It is strictly dependent on FADH2 and does not accept FMNH2 [1,3]. cf. EC, phenol 2-monooxygenase (NADPH).

Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, CAS registry number:


1. Kirchner, U., Westphal, A.H., Muller, R. and van Berkel, W.J. Phenol hydroxylase from Bacillus thermoglucosidasius A7, a two-protein component monooxygenase with a dual role for FAD. J. Biol. Chem. 278 (2003) 47545-47553. [PMID: 12968028]

2. van den Heuvel, R.H., Westphal, A.H., Heck, A.J., Walsh, M.A., Rovida, S., van Berkel, W.J. and Mattevi, A. Structural studies on flavin reductase PheA2 reveal binding of NAD in an unusual folded conformation and support novel mechanism of action. J. Biol. Chem. 279 (2004) 12860-12867. [PMID: 14703520]

3. Saa, L., Jaureguibeitia, A., Largo, E., Llama, M.J. and Serra, J.L. Cloning, purification and characterization of two components of phenol hydroxylase from Rhodococcus erythropolis UPV-1. Appl. Microbiol. Biotechnol. 86 (2010) 201-211. [PMID: 19787347]

[EC created 2016]

Return to EC 1.14.14 home page
Return to EC 1.14 home page
Return to EC 1 home page
Return to Enzymes home page
Return to IUBMB Biochemical Nomenclature home page