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Journal of Bacteriology, July 2004, p. 4528-4534, Vol. 186, No. 14
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.14.4528-4534.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.

The Bacillus subtilis yqjI Gene Encodes the NADP+-Dependent 6-P-Gluconate Dehydrogenase in the Pentose Phosphate Pathway

Nicola Zamboni,1 Eliane Fischer,1 Dietmar Laudert,2 Stéphane Aymerich,3 Hans-Peter Hohmann,2 and Uwe Sauer1*

Institute of Biotechnology, ETH Zürich, Zürich,1 DSM Nutritional Products Inc., Basel, Switzerland,2 Génétique Moléculaire et Cellulaire, INRA-CNRS (URA1925), Thiverval-Grignon, France3

Received 1 February 2004/ Accepted 15 April 2004

Despite the importance of the oxidative pentose phosphate (PP) pathway as a major source of reducing power and metabolic intermediates for biosynthetic processes, almost no direct genetic or biochemical evidence is available for Bacillus subtilis. Using a combination of knockout mutations in known and putative genes of the oxidative PP pathway and 13C-labeling experiments, we demonstrated that yqjI encodes the NADP+-dependent 6-P-gluconate dehydrogenase, as was hypothesized previously from sequence similarities. Moreover, YqjI was the predominant isoenzyme during glucose and gluconate catabolism, and its role in the oxidative PP pathway could not be played by either of two homologues, GntZ and YqeC. This conclusion is in contrast to the generally held view that GntZ is the relevant isoform; hence, we propose a new designation for yqjI, gndA, the monocistronic gene encoding the principal 6-P-gluconate dehydrogenase. Although we demonstrated the NAD+-dependent 6-P-gluconate dehydrogenase activity of GntZ, gntZ mutants exhibited no detectable phenotype on glucose, and GntZ did not contribute to PP pathway fluxes during growth on glucose. Since gntZ mutants grew normally on gluconate, the functional role of GntZ remains obscure, as does the role of the third homologue, YqeC. Knockout of the glucose-6-P dehydrogenase-encoding zwf gene was primarily compensated for by increased glycolytic fluxes, but about 5% of the catabolic flux was rerouted through the gluconate bypass with glucose dehydrogenase as the key enzyme.

* Corresponding author. Mailing address: Institute of Biotechnology, ETH Zürich, Zürich, Switzerland. Phone: 41-1-633 3672. Fax: 41-1-633 1051. E-mail: sauer{at}biotech.biol.ethz.ch.

Journal of Bacteriology, July 2004, p. 4528-4534, Vol. 186, No. 14
0021-9193/04/$08.00+0     DOI: 10.1128/JB.186.14.4528-4534.2004
Copyright © 2004, American Society for Microbiology. All Rights Reserved.



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