The bifunctional role of LiuE from Pseudomonas aeruginosa, displays additionally HIHG-CoA lyase enzymatic activity

Mol Biol Rep. 2010 Apr;37(4):1787-91. doi: 10.1007/s11033-009-9611-6. Epub 2009 Jul 14.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / metabolism*
  • Electrophoresis, Polyacrylamide Gel
  • Metabolic Networks and Pathways
  • Oxo-Acid-Lyases / metabolism*
  • Pseudomonas aeruginosa / enzymology*
  • Recombinant Proteins / metabolism

Substances

  • Bacterial Proteins
  • Recombinant Proteins
  • Oxo-Acid-Lyases