Lerner H R, Sussman I, Avron M
Biochim Biophys Acta. 1980 Sep 9;615(1):1-9. doi: 10.1016/0005-2744(80)90002-9.
Dihydroxyacetone kinase from Dunaliella salina is stabilized against inactivation by maintainance in the presence of 2 M glycerol. In the stabilized form a two-step purification procedure resulted in an enzyme preparation of about 440-fold purity which gave three bands (78 000--100 000 daltons) in the absence of denaturing agents on a polyacrylamide gel. The enzyme is specific for dihydroxyacetone and Mg2+-ATP complex as its substrates. It has sharp pH activity curve with pH optimum around 7.5 and little activity below 6. It is suggested that dihydroxyacetone kinase plays a central role in the mechanism of osmoregulation via glycerol in Dunaliella.
盐生杜氏藻的二羟基丙酮激酶在2 M甘油存在的情况下得以维持稳定，从而防止失活。以稳定形式通过两步纯化程序得到了纯度约为440倍的酶制剂，该制剂在聚丙烯酰胺凝胶上，于不存在变性剂的情况下产生了三条带（78 000 - 100 000道尔顿）。该酶对二羟基丙酮和Mg2+-ATP复合物作为其底物具有特异性。它具有尖锐的pH活性曲线，最适pH约为7.5，在pH低于6时活性很低。有人提出，二羟基丙酮激酶在盐生杜氏藻中通过甘油进行渗透调节的机制中起核心作用。
