| EC |
1.13.11.76 |
| Accepted name: |
2-amino-5-chlorophenol 1,6-dioxygenase |
| Reaction: |
2-amino-5-chlorophenol + O2 = 2-amino-5-chloromuconate 6-semialdehyde |
| Other name(s): |
cnbC (gene name); 2-amino-5-chlorophenol:oxygen 1,6-oxidoreductase (decyclizing) |
| Systematic name: |
2-amino-5-chlorophenol: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 from the bacterium Comamonas testosteroni CNB-1 also has the activity of EC 1.13.11.74, 2-aminophenol 1,6-dioxygenase. |
| Links to other databases: |
BRENDA, EXPASY, KEGG, MetaCyc, PDB |
| References: |
| 1. |
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. [DOI] [PMID: 15580337] |
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| [EC 1.13.11.76 created 2013] |
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