Present address: Center for Systems Biology, University of Iceland, Sturlugata 8, 101 Reykjavik, Iceland.
Unravelling the gallic acid degradation pathway in bacteria: the gal cluster from Pseudomonas putida
Article first published online: 16 NOV 2010
© 2010 Blackwell Publishing Ltd
Volume 79, Issue 2, pages 359–374, January 2011
How to Cite
Nogales, J., Canales, Á., Jiménez-Barbero, J., Serra, B., Pingarrón, J. M., García, J. L. and Díaz, E. (2011), Unravelling the gallic acid degradation pathway in bacteria: the gal cluster from Pseudomonas putida. Molecular Microbiology, 79: 359–374. doi: 10.1111/j.1365-2958.2010.07448.x
- Issue published online: 11 JAN 2011
- Article first published online: 16 NOV 2010
- Accepted manuscript online: 5 NOV 2010 04:58AM EST
- Accepted 25 October, 2010.
Gallic acid (3,4,5-trihydroxybenzoic acid, GA) is widely distributed in nature, being a major phenolic pollutant and a commonly used antioxidant and building-block for drug development. We have characterized the first complete cluster (gal genes) responsible for growth in GA in a derivative of the model bacterium Pseudomonas putida KT2440. GalT mediates specific GA uptake and chemotaxis, and highlights the critical role of GA transport in bacterial adaptation to GA consumption. The proposed GA degradation via the central intermediate 4-oxalomesaconic acid (OMA) was revisited and all enzymes involved have been identified. Thus, GalD is the prototype of a new subfamily of isomerases that catalyses a biochemical step that remained unknown, i.e. the tautomerization of the OMAketo generated by the GalA dioxygenase to OMAenol. GalB is the founding member of a new family of zinc-containing hydratases that converts OMAenol into 4-carboxy-4-hydroxy-2-oxoadipic acid (CHA). galC encodes the aldolase catalysing CHA cleavage to pyruvic and oxaloacetic acids. The presence of homologous gal clusters outside the Pseudomonas genus sheds light on the evolution and ecology of the gal genes in GA degraders. The gal genes were used for expanding the metabolic abilities of heterologous hosts towards GA degradation, and for engineering a GA cellular biosensor.