Structural Analysis Provides Mechanistic Insight into Nicotine Oxidoreductase from Pseudomonas putida.

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

Biochemistry

journal_title

Biochemistry

authors

Tararina MA,Janda KD,Allen KN

doi

10.1021/acs.biochem.6b00963

subject

Has Abstract

pub_date

2016-12-06 00:00:00

pages

6595-6598

issue

48

eissn

0006-2960

issn

1520-4995

journal_volume

55

pub_type

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