Isolation, characterization, and partial purification of a reduced nicotinamide adenine dinucleotide phosphate-dependent dihydroxyacetone reductase from the halophilic alga Dunaliella parva

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 NA...

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Published inPlant physiology (Bethesda) Vol. 53; no. 4; pp. 628 - 631
Main Authors Ben Amotz, A, Avron, M
Format Journal Article
LanguageEnglish
Published United States American Society of Plant Physiologists 01.04.1974
Subjects
Alcohols
Algae
Dehydrogenases
Dunaliella
Enterobacter aerogenes
Enzymes
Oxidation
plant biochemistry
plant physiology
Quaternary ammonium compounds
Sulfates
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Summary: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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ISSN:0032-0889
1532-2548
DOI:10.1104/pp.53.4.628