Reaction: 2-aminophenol + O2 = 2-aminomuconate 6-semialdehyde
Other name(s): amnA (gene name); amnB (gene name); 2-aminophenol:oxygen 1,6-oxidoreductase (decyclizing)
Systematic name: 2-aminophenol:oxygen 1,6-oxidoreductase (ring-opening)
Comments: The enzyme, a member of the nonheme-iron(II)-dependent dioxygenase family, is an extradiol-type dioxygenase that utilizes a non-heme ferrous iron to cleave the aromatic ring at the meta position (relative to the hydroxyl substituent). The enzyme also has some activity with 2-amino-5-methylphenol and 2-amino-4-methylphenol . The enzyme from the bacterium Comamonas testosteroni CNB-1 also has the activity of EC 188.8.131.52, 2-amino-5-chlorophenol 1,6-dioxygenase .
Links to other databases: BRENDA, EXPASY, KEGG, Metacyc, PDB, CAS registry number:
1. Takenaka, S., Murakami, S., Shinke, R., Hatakeyama, K., Yukawa, H. and Aoki, K. Novel genes encoding 2-aminophenol 1,6-dioxygenase from Pseudomonas species AP-3 growing on 2-aminophenol and catalytic properties of the purified enzyme. J. Biol. Chem. 272 (1997) 14727-14732. [PMID: 9169437]
2. Wu, J.F., Sun, C.W., Jiang, C.Y., Liu, Z.P. and Liu, S.J. A novel 2-aminophenol 1,6-dioxygenase involved in the degradation of p-chloronitrobenzene by Comamonas strain CNB-1: purification, properties, genetic cloning and expression in Escherichia coli. Arch. Microbiol. 183 (2005) 1-8. [PMID: 15580337]
3. Li, D.F., Zhang, J.Y., Hou, Y., Liu, L., Liu, S.J. and Liu, W. Crystallization and preliminary crystallographic analysis of 2-aminophenol 1,6-dioxygenase complexed with substrate and with an inhibitor. Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun. 68 (2012) 1337-1340. [PMID: 23143244]