Enzymes
| UniProtKB help_outline | 1 proteins |
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- Name help_outline (1E)-4-oxobut-1-ene-1,2,4-tricarboxylate Identifier CHEBI:57471 (Beilstein: 1124055) help_outline Charge -3 Formula C7H3O7 InChIKeyhelp_outline ODTDYYZJDQGKQT-NSCUHMNNSA-K SMILEShelp_outline [O-]C(=O)\C=C(/CC(=O)C([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 4 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline 4-carboxy-2-hydroxy-cis,cis-muconate Identifier CHEBI:58142 Charge -3 Formula C7H3O7 InChIKeyhelp_outline QWLUKZXOQAQUFQ-DXLKSGPOSA-K SMILEShelp_outline O\C(=C\C(=C/C([O-])=O)C([O-])=O)C([O-])=O 2D coordinates Mol file for the small molecule Search links Involved in 2 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
| RHEA:28931 | RHEA:28932 | RHEA:28933 | RHEA:28934 | |
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| Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
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Publications
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Unravelling the gallic acid degradation pathway in bacteria: the gal cluster from Pseudomonas putida.
Nogales J., Canales A., Jimenez-Barbero J., Serra B., Pingarron J.M., Garcia J.L., Diaz E.
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 ... >> More
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. << Less
Mol. Microbiol. 79:359-374(2011) [PubMed] [EuropePMC]
This publication is cited by 6 other entries.