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Gene Review

paaG  -  1,2-epoxyphenylacetyl-CoA isomerase,...

Escherichia coli str. K-12 substr. MG1655

Synonyms: ECK1391, JW1389, ydbT
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Disease relevance of paaG


High impact information on paaG


Chemical compound and disease context of paaG

  • Evidence that the fadB gene of the fadAB operon of Escherichia coli encodes 3-hydroxyacyl-coenzyme A (CoA) epimerase, delta 3-cis-delta 2-trans-enoyl-CoA isomerase, and enoyl-CoA hydratase in addition to 3-hydroxyacyl-CoA dehydrogenase [7].
  • Moreover, the function of the ech gene product as an enoyl-CoA hydratase/aldolase suggests that ferulic acid degradation in Pseudomonas sp. strain HR199 proceeds via a similar pathway to that recently described for Pseudomonas fluorescens AN103 [6].
  • E. coli was metabolically engineered to produce vanillin by expression of the fcs and ech genes from Amycolatopsis sp. encoding feruloyl-CoA synthetase and enoyl-CoA hydratase/aldolase, respectively [8].

Biological context of paaG

  • The amino acid sequence deduced from ech exhibited 51% identity to the enoyl-CoA hydratase/aldolase from Pseudomonas sp. strain HR199, indicating that the enzyme from D. acidovorans represents a new lineage of this protein [3].
  • The recombinants harboring phaJ1(Pa) or phaJ2(Pa) showed high (R)-specific enoyl-CoA hydratase activity with different substrate specificities, that is, specific for short chain-length enoyl-CoA or medium chain-length enoyl-CoA, respectively [9].

Associations of paaG with chemical compounds


Analytical, diagnostic and therapeutic context of paaG


  1. Identification and characterization of a new enoyl coenzyme A hydratase involved in biosynthesis of medium-chain-length polyhydroxyalkanoates in recombinant Escherichia coli. Park, S.J., Lee, S.Y. J. Bacteriol. (2003) [Pubmed]
  2. The role of the fatty acid beta-oxidation multienzyme complex from Pseudomonas oleovorans in polyhydroxyalkanoate biosynthesis: molecular characterization of the fadBA operon from P. oleovorans and of the enoyl-CoA hydratase genes phaJ from P. oleovorans and Pseudomonas putida. Fiedler, S., Steinbüchel, A., Rehm, B.H. Arch. Microbiol. (2002) [Pubmed]
  3. The coenzyme A-dependent, non-beta-oxidation pathway and not direct deacetylation is the major route for ferulic acid degradation in Delftia acidovorans. Plaggenborg, R., Steinbüchel, A., Priefert, H. FEMS Microbiol. Lett. (2001) [Pubmed]
  4. 3-Hydroxyacyl-CoA epimerases of rat liver peroxisomes and Escherichia coli function as auxiliary enzymes in the beta-oxidation of polyunsaturated fatty acids. Yang, S.Y., Cuebas, D., Schulz, H. J. Biol. Chem. (1986) [Pubmed]
  5. Involvement of coenzyme A esters and two new enzymes, an enoyl-CoA hydratase and a CoA-transferase, in the hydration of crotonobetaine to L-carnitine by Escherichia coli. Elssner, T., Engemann, C., Baumgart, K., Kleber, H.P. Biochemistry (2001) [Pubmed]
  6. Biochemical and genetic analyses of ferulic acid catabolism in Pseudomonas sp. Strain HR199. Overhage, J., Priefert, H., Steinbüchel, A. Appl. Environ. Microbiol. (1999) [Pubmed]
  7. Evidence that the fadB gene of the fadAB operon of Escherichia coli encodes 3-hydroxyacyl-coenzyme A (CoA) epimerase, delta 3-cis-delta 2-trans-enoyl-CoA isomerase, and enoyl-CoA hydratase in addition to 3-hydroxyacyl-CoA dehydrogenase. Yang, S.Y., Li, J.M., He, X.Y., Cosloy, S.D., Schulz, H. J. Bacteriol. (1988) [Pubmed]
  8. Production of vanillin by metabolically engineered Escherichia coli. Yoon, S.H., Li, C., Kim, J.E., Lee, S.H., Yoon, J.Y., Choi, M.S., Seo, W.T., Yang, J.K., Kim, J.Y., Kim, S.W. Biotechnol. Lett. (2005) [Pubmed]
  9. Molecular cloning of two (R)-specific enoyl-CoA hydratase genes from Pseudomonas aeruginosa and their use for polyhydroxyalkanoate synthesis. Tsuge, T., Fukui, T., Matsusaki, H., Taguchi, S., Kobayashi, G., Ishizaki, A., Doi, Y. FEMS Microbiol. Lett. (2000) [Pubmed]
  10. Functional genomics by NMR spectroscopy. Phenylacetate catabolism in Escherichia coli. Ismail, W., El-Said Mohamed, M., Wanner, B.L., Datsenko, K.A., Eisenreich, W., Rohdich, F., Bacher, A., Fuchs, G. Eur. J. Biochem. (2003) [Pubmed]
  11. Genes coding for the benzoyl-CoA pathway of anaerobic aromatic metabolism in the bacterium Thauera aromatica. Breese, K., Boll, M., Alt-Mörbe, J., Schägger, H., Fuchs, G. Eur. J. Biochem. (1998) [Pubmed]
  12. Identification of Amycolatopsis sp. strain HR167 genes, involved in the bioconversion of ferulic acid to vanillin. Achterholt, S., Priefert, H., Steinbüchel, A. Appl. Microbiol. Biotechnol. (2000) [Pubmed]
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