NADP Specific dihydroxyacetone reductase fromDunaliella parva
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چکیده
منابع مشابه
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 NADPH. The pH optima for dihydroxyacetone reduction and for glycerol oxidation are 7.5 and 9.2, r...
متن کاملDihydroxyacetone Phosphate Reductase in Plants ' Received
on either DEAE cellulose or Sephacryl S-200. About 80% of the reductase was one form in the chloroplast and the rest was a second form in the cytosol as determined by chromatography and by fractionation of subcellular organelles. The amount of activity detectable in the chloroplast fraction was 10.7 micromoles of dihydroxyacetone phosphate reductase per hour per milligram chlorophyll from spina...
متن کاملThionicotinamide-NADP, a nucleotide analog interfering with ferredoxin-NADP reductase-ferredoxin interaction.
1 7 W . K R E U T Z U. W . MENKE, Z . N a t u r f o r s c h . 1 7 b , 6 7 5 [1962], 18 W. KREUTZ, Z. Naturforsch. 18 b, 1098 [1963] ; 19 b, 441 [1964], 19 W. MENKE, in: Photosynthesis Mechanisms in green Plants, Publ. 1145, Nat. Acad. Sci.-Nat. Res. Council, Publ. 1963, p. 537. 20 W. MENKE, in: Biochemistry of Chloroplasts, Vol. I, (ed. T. GOODWIN), p. 3, Acad. Press, London and New York 1967. ...
متن کاملTwo isozymes of dihydroxyacetone phosphate reductase in dunaliella.
Two isoforms of dihydroxyacetone phosphate reductase were present in Dunaliella tertiolecta. The major form was located in the chloroplast and the minor form in the cytosol. The chloroplastic reductase eluted first from a DEAE cellulose column followed immediately by the cytosolic form. Both forms were unstable and cold labile. Addition of 5 millimolar dithiothreitol helped to stabilize the enz...
متن کاملA novel NADPH:(bound) NADP+ reductase and NADH:(bound) NADP+ transhydrogenase function in bovine liver catalase.
Many catalases have the shared property of containing bound NADPH and being susceptible to inactivation by their own substrate, H2O2. The presence of additional (unbound) NADPH effectively prevents bovine liver and human erythrocytic catalase from becoming compound II, the reversibly inactivated state of catalase, and NADP+ is known to be generated in the process. The function of the bound NADP...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1973
ISSN: 0014-5793
DOI: 10.1016/0014-5793(73)80548-4