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Applied and Environmental Microbiology, April 2003, p. 1959-1966, Vol. 69, No. 4
0099-2240/03/$08.00+0     DOI: 10.1128/AEM.69.4.1959-1966.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.

5-Keto-D-Gluconate Production Is Catalyzed by a Quinoprotein Glycerol Dehydrogenase, Major Polyol Dehydrogenase, in Gluconobacter Species

Kazunobu Matsushita,1* Yoshikazu Fujii,1 Yoshitaka Ano,1 Hirohide Toyama,1 Masako Shinjoh,2 Noribumi Tomiyama,2 Taro Miyazaki,2 Teruhide Sugisawa,2 Tatsuo Hoshino,2 and Osao Adachi1

Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University, Yamaguchi 753-8515,1 Department of Applied Microbiology, Nippon Roche Research Center, Kamakura, Kanagawa 247-8530, Japan2

Received 16 September 2002/ Accepted 7 January 2003

Acetic acid bacteria, especially Gluconobacter species, have been known to catalyze the extensive oxidation of sugar alcohols (polyols) such as D-mannitol, glycerol, D-sorbitol, and so on. Gluconobacter species also oxidize sugars and sugar acids and uniquely accumulate two different keto-D-gluconates, 2-keto-D-gluconate and 5-keto-D-gluconate, in the culture medium by the oxidation of D-gluconate. However, there are still many controversies regarding their enzyme systems, especially on D-sorbitol and also D-gluconate oxidations. Recently, pyrroloquinoline quinone-dependent quinoprotein D-arabitol dehydrogenase and D-sorbitol dehydrogenase have been purified from G. suboxydans, both of which have similar and broad substrate specificity towards several different polyols. In this study, both quinoproteins were shown to be identical based on their immuno-cross-reactivity and also on gene disruption and were suggested to be the same as the previously isolated glycerol dehydrogenase (EC 1.1.99.22). Thus, glycerol dehydrogenase is the major polyol dehydrogenase involved in the oxidation of almost all sugar alcohols in Gluconobacter sp. In addition, the so-called quinoprotein glycerol dehydrogenase was also uniquely shown to oxidize D-gluconate, which was completely different from flavoprotein D-gluconate dehydrogenase (EC 1.1.99.3), which is involved in the production of 2-keto-D-gluconate. The gene disruption experiment and the reconstitution system of the purified enzyme in this study clearly showed that the production of 5-keto-D-gluconate in G. suboxydans is solely dependent on the quinoprotein glycerol dehydrogenase.

* Corresponding author. Mailing address: Department of Biological Chemistry, Faculty of Agriculture, Yamaguchi University, Yamaguchi 753-8515, Japan. Phone: 81(83)933-5858. Fax: 81(83)933-5859. E-mail: kazunobu{at}agr.yamaguchi-u.ac.jp.

Applied and Environmental Microbiology, April 2003, p. 1959-1966, Vol. 69, No. 4
0099-2240/03/$08.00+0     DOI: 10.1128/AEM.69.4.1959-1966.2003
Copyright © 2003, American Society for Microbiology. All Rights Reserved.



This article has been cited by other articles:

  • Saichana, I., Moonmangmee, D., Adachi, O., Matsushita, K., Toyama, H. (2009). Screening of Thermotolerant Gluconobacter Strains for Production of 5-Keto-D-Gluconic Acid and Disruption of Flavin Adenine Dinucleotide-Containing D-Gluconate Dehydrogenase. Appl. Environ. Microbiol. 75: 4240-4247 [Abstract] [Full Text]  
  • Yang, X.-P., Wei, L.-J., Lin, J.-P., Yin, B., Wei, D.-Z. (2008). Membrane-Bound Pyrroloquinoline Quinone-Dependent Dehydrogenase in Gluconobacter oxydans M5, Responsible for Production of 6-(2-Hydroxyethyl) Amino-6-Deoxy-L-Sorbose. Appl. Environ. Microbiol. 74: 5250-5253 [Abstract] [Full Text]  
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