Plant Physiol.
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Plant Physiology 53:628-631 (1974)
© 1974 American Society of Plant Biologists

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Articles

Isolation, Characterization, and Partial Purification of a Reduced Nicotinamide Adenine Dinucleotide Phosphate-dependent Dihydroxyacetone Reductase from the Halophilic Alga Dunaliella parva

Ami Ben-Amotz and Mordhay Avron

Department of Biochemistry, Weizmann Institute of Science, Rehovoth, Israel

An NADP+-dependent dihydroxyacetone reductase, which catalyzes specifically the reduction of dihydroxyacetone to glycerol, has been isolated from the halophilic alga Dunaliella parva. The enzyme has been purified about 220-fold. It has a molecular weight of about 65,000 and is highly specific for NADPH. The pH optima for dihydroxyacetone reduction and for glycerol oxidation are 7.5 and 9.2, respectively. The enzyme has a very narrow substrate specificity and will not catalyze the reduction of glyceraldehyde or dihydroxyacetone phosphate. It is suggested that this enzyme functions physiologically as a dihydroxyacetone reductase in the path of glycerol synthesis and accumulation in Dunaliella.






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ASPB Publications PLANT PHYSIOLOGY® THE PLANT CELL
Copyright © 1974 by the American Society of Plant Biologists