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Applied and Environmental Microbiology, June 2006, p. 4128-4135, Vol. 72, No. 6
0099-2240/06/$08.00+0     doi:10.1128/AEM.00080-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.

The Alkyl tert-Butyl Ether Intermediate 2-Hydroxyisobutyrate Is Degraded via a Novel Cobalamin-Dependent Mutase Pathway{dagger}

Thore Rohwerder,1* Uta Breuer,1 Dirk Benndorf,1 Ute Lechner,2 and Roland H. Müller1

UFZ-Center for Environmental Research Leipzig-Halle, Department of Environmental Microbiology, Permoserstr. 15, 04318 Leipzig, Germany,1 Martin-Luther-Universität Halle, Institut für Mikrobiologie, Kurt-Mothes-Str. 3, 06120 Halle, Germany2

Received 12 January 2006/ Accepted 24 March 2006

Fuel oxygenates such as methyl and ethyl tert-butyl ether (MTBE and ETBE, respectively) are degraded only by a limited number of bacterial strains. The aerobic pathway is generally thought to run via tert-butyl alcohol (TBA) and 2-hydroxyisobutyrate (2-HIBA), whereas further steps are unclear. We have now demonstrated for the newly isolated ß-proteobacterial strains L108 and L10, as well as for the closely related strain CIP I-2052, that 2-HIBA was degraded by a cobalamin-dependent enzymatic step. In these strains, growth on substrates containing the tert-butyl moiety, such as MTBE, TBA, and 2-HIBA, was strictly dependent on cobalt, which could be replaced by cobalamin. Tandem mass spectrometry identified a 2-HIBA-induced protein with high similarity to a peptide whose gene sequence was found in the finished genome of the MTBE-degrading strain Methylibium petroleiphilum PM1. Alignment analysis identified it as the small subunit of isobutyryl-coenzyme A (CoA) mutase (ICM; EC 5.4.99.13), which is a cobalamin-containing carbon skeleton-rearranging enzyme, originally described only in Streptomyces spp. Sequencing of the genes of both ICM subunits from strain L108 revealed nearly 100% identity with the corresponding peptide sequences from M. petroleiphilum PM1, suggesting a horizontal gene transfer event to have occurred between these strains. Enzyme activity was demonstrated in crude extracts of induced cells of strains L108 and L10, transforming 2-HIBA into 3-hydroxybutyrate in the presence of CoA and ATP. The physiological and evolutionary aspects of this novel pathway involved in MTBE and ETBE metabolism are discussed.

* Corresponding author. Mailing address: Department of Environmental Microbiology, UFZ, Permoserstr. 15, 04318 Leipzig, Germany. Phone: 49 341 235 2367. Fax: 49 341 235 2247. E-mail: thore.rohwerder{at}ufz.de.

{dagger} Supplemental material for this article may be found at http://aem.asm.org/.

Applied and Environmental Microbiology, June 2006, p. 4128-4135, Vol. 72, No. 6
0099-2240/06/$08.00+0     doi:10.1128/AEM.00080-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.



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