Enzymes involved in the formation of glycerol 3-phosphate and the by-products dihydroxyacetone and glycerol in Zymomonas mobilis |
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Authors: | Silke Horbach Joachim Strohhäcker Roland Welle Albert de Graaf Hermann Sahm |
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Institution: | Institut für Biotechnologie I, Forschungszentrum Jülich GmbH, 52425 Jülich, FRG |
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Abstract: | Abstract In Zymomonas mobilis a novel pathway for the formation of glycerol 3-phosphate was identified by enzymatic studies and nuclear magnetic resonance spectroscopy. This pathway branches off from the Entner-Doudoroff pathway at the intermediate glyceraldehyde 3-phosphate and proceedes via dihydroxyacetone phosphate, dihydroxyacetone, glycerol to glycerol 3-phosphate. The reaction sequence is catalyzed by the enzymes triosephosphate isomerase (0.4 U (mg protein)−1), dihydroxyacetone phosphatase (0.31 U (mg protein)−1), dihydroxyacetone reductase (0.25 U (mg protein)−1), and glycerokinase (0.08 mU (mg protein)−1), respectively. The action of a postulated aldolase catalyzing the cleavage of fructose 6-phosphate to dihydroxyacetone and glyceraldehyde 3-phosphate could be excluded. |
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Keywords: | Zymomonas mobilis Glycerol 3-phosphate Dihydroxyacetone Glycerol NMR spectroscopy |
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