Differential Inhibition and Activation of Two Leaf Dihydroxyacetone Phosphate Reductases
نویسندگان
چکیده
منابع مشابه
Exclusive localization in peroxisomes of dihydroxyacetone phosphate acyltransferase and alkyl-dihydroxyacetone phosphate synthase in rat liver.
Dihydroxyacetone phosphate acyl transferase (DHAP-AT), alkyl dihydroxyacetone phosphate synthase (alkyl-DHAP-synthase), and glycerol-3-phosphate acyltransferase (GPAT) activities were investigated under optimal assay conditions using highly purified organelle preparations. The data presented clearly indicate that GPAT activity was mainly localized in mitochondria and microsomes, whereas DHAP-AT...
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 کاملAcyl dihydroxyacetone phosphate: precursor of alkyl ethers.
1-0-Alkyl dihydroxyacetone phosphate is biosynthesised in guinea pig liver mitochondria and in rat brain microsomes by direct reaction of a long chain alcohol and acyl dihydroxyacetone phosphate. ATP and Mg* are stimulatory but coenzyme A is not necessary for the reaction. 1-0-Alkyl dihydroxyacetone phosphate (alkyl DHAP)l was shown to be biosynthesized from long chain alcohol and DHAP with ATP...
متن کاملPhosphate inhibition of spinach leaf sucrose phosphate synthase as affected by glucose-6-phosphate and phosphoglucoisomerase.
The inhibition patterns of inorganic phosphate (Pi) on sucrose phosphate synthase activity in the presence and absence of the allosteric activator glucose-6-P was studied, as well as the effects of phosphoglucoisomerase on fructose-6-P saturation kinetics with and without Pi. In the presence of 5 millimolar glucose-6-P, Pi was a partial competitive inhibitor with respect to both substrates, fru...
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...
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ژورنال
عنوان ژورنال: Plant Physiology
سال: 1988
ISSN: 0032-0889,1532-2548
DOI: 10.1104/pp.87.2.379