Department of Biochemistry, Weizmann Institute of Science, Rehovoth, Israel.
Plant Physiol. 1974 Apr;53(4):628-31. doi: 10.1104/pp.53.4.628.
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.
已从嗜盐藻类小球藻中分离出一种依赖 NADP(+)的二羟丙酮还原酶,它能特异性地将二羟丙酮还原为甘油。该酶已被纯化约 220 倍,分子量约为 65000,对 NADPH 具有高度特异性。二羟丙酮还原和甘油氧化的最适 pH 值分别为 7.5 和 9.2。该酶具有非常狭窄的底物特异性,不能催化甘油醛或二羟丙酮磷酸的还原。据认为,该酶在小球藻中甘油合成和积累的途径中作为二羟丙酮还原酶发挥生理作用。