Abstract:
:The first structure of nicotine oxidoreductase (NicA2) was determined by X-ray crystallography. Pseudomonas putida has evolved nicotine-degrading activity to provide a source of carbon and nitrogen. The structure establishes NicA2 as a member of the monoamine oxidase family. Residues 1-50 are disordered and may play a role in localization. The nicotine-binding site proximal to the isoalloxazine ring of flavin shows an unusual composition of the classical aromatic cage (W427 and N462). The active site architecture is consistent with the proposed binding of the deprotonated form of the substrate and the flavin-dependent oxidation of the pyrrolidone C-N bond followed by nonenzymatic hydrolysis.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Tararina MA,Janda KD,Allen KNdoi
10.1021/acs.biochem.6b00963subject
Has Abstractpub_date
2016-12-06 00:00:00pages
6595-6598issue
48eissn
0006-2960issn
1520-4995journal_volume
55pub_type
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