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Title

Deciphering the genetic determinants for aerobic nicotinic acid degradation: the nic cluster from Pseudomonas putida KT2440

AuthorsJiménez, José Ignacio; Canales, Ángeles ; Jiménez-Barbero, Jesús ; Ginalski, K.; Rychlewski, L.; García, José Luis ; Díaz, Eduardo
KeywordsRing-cleavage dioxygenase
nicotinic acid hydroxylase
heterocyclic compounds
Issue Date12-Aug-2008
PublisherNational Academy of Sciences (U.S.)
CitationProceedings of the National Academy of Sciences, 105 (32) : 11329-11334 (2008)
AbstractThe aerobic catabolism of nicotinic acid (NA) is considered a model system for degradation of N-heterocyclic aromatic compounds, some of which are major environmental pollutants; however, the complete set of genes as well as the structural–functional relationships of most of the enzymes involved in this process are still unknown. We have characterized a gene cluster (nic genes) from Pseudomonas putida KT2440 responsible for the aerobic NA degradation in this bacterium and when expressed in heterologous hosts. The biochemistry of the NA degradation through the formation of 2,5-dihydroxypyridine and maleamic acid has been revisited, and some gene products become the prototype of new types of enzymes with unprecedented molecular architectures. Thus, the initial hydroxylation of NA is catalyzed by a two-component hydroxylase (NicAB) that constitutes the first member of the xanthine dehydrogenase family whose electron transport chain to molecular oxygen includes a cytochrome c domain. The Fe2+-dependent dioxygenase (NicX) converts 2,5-dihydroxypyridine into N-formylmaleamic acid, and it becomes the founding member of a new family of extradiol ring-cleavage dioxygenases. Further conversion of N-formylmaleamic acid to formic and maleamic acid is catalyzed by the NicD protein, the only deformylase described so far whose catalytic triad is similar to that of some members of the α/β-hydrolase fold superfamily. This work allows exploration of the existence of orthologous gene clusters in saprophytic bacteria and some pathogens, where they might stimulate studies on their role in virulence, and it provides a framework to develop new biotechnological processes for detoxification/biotransformation of N-heterocyclic aromatic compounds
Description6 páginas, 3 figuras -- PAGS nros. 11329-11334
Publisher version (URL)http://dx.doi.org/10.1073/pnas.0802273105
URIhttp://hdl.handle.net/10261/54055
DOI10.1073/pnas.0802273105
E-ISSN1091-6490
Appears in Collections:(CIB) Artículos
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