Abstract
Pseudomonas aeruginosa is able to utilize leucine/isovalerate and acyclic terpenes as sole carbon sources. Key enzymes which play an important role in these catabolic pathways are 3-hydroxy-3-methylglutaryl-coenzyme A (CoA) lyase (EC 4.1.3.4; HMG-CoA lyase) and the 3-hydroxy-3-isohexenylglutaryl-CoA lyase (EC 4.1.2.26; HIHG-CoA lyase), respectively. HMG-CoA lyase is encoded by the liuE gene while the gene for HIHG-CoA lyase remains unidentified. A mutant in the liuE gene was unable to utilize both leucine/isovalerate and acyclic terpenes indicates an involvement of liuE in both catabolic pathways (Chávez-Avilés et al. 2009, FEMS Microbiol Lett 296:117–123). The LiuE protein was purified as a His-tagged recombinant protein and in addition to show HMG-CoA lyase activity (Chávez-Avilés et al. 2009, FEMS Microbiol Lett 296:117–123), also displays HIHG-CoA lyase activity, indicating a bifunctional role in both the leucine/isovalerate and acyclic terpenes catabolic pathways.
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Acknowledgments
This research was funded from grants CONACYT (P-46547-Z), C.I.C.-UMSNH 2.14, and COECyT CB070229-2 to JCG. M. Chávez-Avilés was supported by a fellowship from CONACYT.
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Chávez-Avilés, M., Díaz-Pérez, A.L. & Campos-García, J. The bifunctional role of LiuE from Pseudomonas aeruginosa, displays additionally HIHG-CoA lyase enzymatic activity. Mol Biol Rep 37, 1787–1791 (2010). https://doi.org/10.1007/s11033-009-9611-6
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DOI: https://doi.org/10.1007/s11033-009-9611-6