Structural highlights
Function
AMNA_COMTE Component of the 2-aminophenol 1,6-dioxygenase (APD) complex that catalyzes the ring fission of 2-aminophenol to produce 2-aminomuconic semialdehyde. CnbCa may have a role in the stability of the complex. The complex is also active on other substrates such as 2-amino-5-chlorophenol (68% activity), protocatechuate (33% activity) and catechol (5% activity). Both 2-aminophenol and 2-amino-5-cholorophenol are likely native substrates for this dioxygenase which is involved in the reductive degradation pathway of both nitrobenzene (NB) and 4-chloronitrobenzene (4-CNB), allowing C.testosteroni strain CNB-1 to grow on these compounds as sole source of carbon, nitrogen, and energy.[1] [2]
References
- ↑ Wu JF, Sun CW, Jiang CY, Liu ZP, Liu SJ. 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. 2005 Jan;183(1):1-8. Epub 2004 Dec 3. PMID:15580337 doi:http://dx.doi.org/10.1007/s00203-004-0738-5
- ↑ Wu JF, Jiang CY, Wang BJ, Ma YF, Liu ZP, Liu SJ. Novel partial reductive pathway for 4-chloronitrobenzene and nitrobenzene degradation in Comamonas sp. strain CNB-1. Appl Environ Microbiol. 2006 Mar;72(3):1759-65. PMID:16517619 doi:http://dx.doi.org/72/3/1759
