Membrane-bound glycerol dehydrogenase catalyzes oxidation of D-pentonates to 4-keto-D-pentonates, D-fructose to 5-keto-D-fructose, and D-psicose to 5-keto-D-psicose
A novel oxidation of D-pentonates to 4-keto-D-pentonates was analyzed with <i>Gluconobacter Thailandicus</i> NBRC 3258. D-Pentonate 4-dehydrogenase activity in the membrane fraction was readily inactivated by EDTA and it was reactivated by the addition of PQQ and Ca<sup>2+</sup&...
Guardado en:
| Autores principales: | , , , , , , |
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| Formato: | Articulo |
| Lenguaje: | Inglés |
| Publicado: |
2017
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| Materias: | |
| Acceso en línea: | http://sedici.unlp.edu.ar/handle/10915/87580 |
| Aporte de: |
| Sumario: | A novel oxidation of D-pentonates to 4-keto-D-pentonates was analyzed with <i>Gluconobacter Thailandicus</i> NBRC 3258. D-Pentonate 4-dehydrogenase activity in the membrane fraction was readily inactivated by EDTA and it was reactivated by the addition of PQQ and Ca<sup>2+</sup>. D-Pentonate 4-dehydrogenase was purified to two different subunits, 80 and 14 kDa. The absorption spectrum of the purified enzyme showed no typical absorbance over the visible regions. The enzyme oxidized D-pentonates to 4-keto-D-pentonates at the optimum pH of 4.0. In addition, the enzyme oxidized D-fructose to 5-keto-D-fructose, D-psicose to 5-keto-D-psicose, including the other polyols such as, glycerol, D-ribitol, D-arabitol, and D-sorbitol. Thus, D-pentonate 4-dehydrogenase was found to be identical with glycerol dehydrogenase (GLDH), a major polyol dehydrogenase in <i>Gluconobacter</i> species. The reaction versatility of quinoprotein GLDH was notified in this study. |
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