Characterization and partial purification of dihydroxyacetone kinase in Dunaliella salina.
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.
D055598:Chemical Phenomena; D002627:Chemistry, Physical; D000460:Chlorophyta / Q000201:enzymology*; D004098:Dihydroxyacetone / Q000302:isolation & purification / Q000378:metabolism; D005990:Glycerol; D006863:Hydrogen-Ion Concentration; D008274:Magnesium; D008970:Molecular Weight; D010770:Phosphotransferases / Q000302:isolation & purification* / Q000378:metabolism; D017853:Phosphotransferases (Alcohol Group Acceptor)
D010770:Phosphotransferases; D017853:Phosphotransferases (Alcohol Group Acceptor); C023132:glycerone kinase; D008274:Magnesium; D004098:Dihydroxyacetone; D005990:Glycerol