The Enzyme Database

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EC 1.13.11.74     
Accepted name: 2-aminophenol 1,6-dioxygenase
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 [1]. The enzyme from the bacterium Comamonas testosteroni CNB-1 also has the activity of EC 1.13.11.76, 2-amino-5-chlorophenol 1,6-dioxygenase [2].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
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.J., Liu, L., Hu, Y., Liu, S.J., Wang da, C. and Liu, W. Structures of aminophenol dioxygenase in complex with intermediate, product and inhibitor. Acta Crystallogr. D Biol. Crystallogr. 69 (2013) 32–43. [PMID: 23275161]
[EC 1.13.11.74 created 2013]
 
 


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