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Journal of Bacteriology, April 2009, p. 2112-2121, Vol. 191, No. 7
0021-9193/09/$08.00+0     doi:10.1128/JB.01523-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.

Different Biochemical Mechanisms Ensure Network-Wide Balancing of Reducing Equivalents in Microbial Metabolism{triangledown} ,{dagger}

Tobias Fuhrer and Uwe Sauer*

Institute of Molecular Systems Biology, ETH Zurich, CH-8093 Zurich, Switzerland

Received 28 October 2008/ Accepted 21 January 2009

To sustain growth, the catabolic formation of the redox equivalent NADPH must be balanced with the anabolic demand. The mechanisms that ensure such network-wide balancing, however, are presently not understood. Based on 13C-detected intracellular fluxes, metabolite concentrations, and cofactor specificities for all relevant central metabolic enzymes, we have quantified catabolic NADPH production in Agrobacterium tumefaciens, Bacillus subtilis, Escherichia coli, Paracoccus versutus, Pseudomonas fluorescens, Rhodobacter sphaeroides, Sinorhizobium meliloti, and Zymomonas mobilis. For six species, the estimated NADPH production from glucose catabolism exceeded the requirements for biomass synthesis. Exceptions were P. fluorescens, with balanced rates, and E. coli, with insufficient catabolic production, in which about one-third of the NADPH is supplied via the membrane-bound transhydrogenase PntAB. P. versutus and B. subtilis were the only species that appear to rely on transhydrogenases for balancing NADPH overproduction during growth on glucose. In the other four species, the main but not exclusive redox-balancing mechanism appears to be the dual cofactor specificities of several catabolic enzymes and/or the existence of isoenzymes with distinct cofactor specificities, in particular glucose 6-phosphate dehydrogenase. An unexpected key finding for all species, except E. coli and B. subtilis, was the lack of cofactor specificity in the oxidative pentose phosphate pathway, which contrasts with the textbook view of the pentose phosphate pathway dehydrogenases as being NADP+ dependent.

* Corresponding author. Mailing address: Institute of Molecular Systems Biology, ETH Zurich, CH-8093 Zurich, Switzerland. Phone: 41-44-633 3672. Fax: 41-44-633 1051. E-mail: sauer{at}imsb.biol.ethz.ch

{triangledown} Published ahead of print on 30 January 2009.

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

Journal of Bacteriology, April 2009, p. 2112-2121, Vol. 191, No. 7
0021-9193/09/$08.00+0     doi:10.1128/JB.01523-08
Copyright © 2009, American Society for Microbiology. All Rights Reserved.





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