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Journal of Bacteriology, April 2009, p. 2899-2901, Vol. 191, No. 8
0021-9193/09/$08.00+0 doi:10.1128/JB.01756-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Institute for Biotechnology 1, Jülich Forschungszentrum, D-52425 Jülich, Germany,1 Université de Toulouse, INSA, LISBP, 135 Avenue de Rangueil, F-31077 Toulouse, France,2 INRA, UMR792 Ingénierie des Systèmes Biologiques et des Procédés, F-31400 Toulouse, France,3 CNRS, UMR5504, F-31400 Toulouse, France4
Received 16 December 2008/ Accepted 11 February 2009
Genome sequence information suggests that B12-dependent mutases are present in a number of bacteria, including members of the suborder Corynebacterineae like Mycobacterium tuberculosis and Corynebacterium glutamicum. We here functionally identify a methylmalonyl coenzyme A (CoA) mutase in C. glutamicum that is retained in all of the members of the suborder Corynebacterineae and is encoded by NCgl1471, NCgl1472, and NCgl1470. In addition, we observe the presence of methylmalonate in C. glutamicum, reaching concentrations of up to 757 nmol g (dry weight)–1 in propionate-grown cells, whereas in Escherichia coli no methylmalonate was detectable. As demonstrated with a mutase deletion mutant, the presence of methylmalonate in C. glutamicum is independent of mutase activity but possibly due to propionyl-CoA carboxylase activity. During growth on propionate, increased mutase activity has severe cellular consequences, resulting in growth arrest and excretion of succinate. The physiological context of the mutase present in members of the suborder Corynebacterineae is discussed.
Published ahead of print on 20 February 2009.
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