nBlog 2008-09-12

The first stucture of the N. farcinica protein comes from France.

F. Rodrigues-Lima's group (Université Paris Diderot-Paris) reported the first structure of the N. farcinica protein in the paper entitled "Functional and Structural Characterization of the Arylamine N-Acetyltransferase from the Opportunistic Pathogen Nocardia farcinica" in the Journal of Molecular Biology. In the work, they cloned an arylamine N-acetyltransferase (NAT) gene (nfa18420) in E. coli, purified the enzyme and characterized. The NAT of N. farcinica (NfNAT) was found to acetylate efficiently a broad range of aromatic substrates and considered to be the most efficient prokaryotic NAT enzyme. In particular, the NfNAT was able to acetylate isoniazid (INH), an anti-mycobacterial agent. The author said "NAT could contribute to INH insensivity in N. farcinica". We would like to investigate this point in the near future by making the deletion mutant of nfa18420.

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They also determined the crystal structure of NfNAT. The result indicated that the structure of NfNAT was almost identical to that of other prokaryotic NATs, especially to mycobacterial NATs. They conclude their remarks with the sentence "These data ... and may be exploited to design NAT antagonists for a range of clinical applications".