| pubmed-article:2635863 | pubmed:abstractText | A novel phospholipid analogue, di (triethyleneglycol-n-tetradecylether) phosphate was synthesized and its activation ability for a phospholipid-requiring enzyme, Mycobacterium smegmatis malate dehydrogenase, was examined. The results showed that the newly-synthesized phospholipid analogue a high ability, nearly equal to that of natural beef heart cardiolipin, for the activation of the lipid-depleted inactive enzyme; whereas both simple di-n-octylphosphate and di-n-tetradecylphosphate were found to have poor activation abilities. These results strongly suggest that a slightly hydrophilic region between the phosphate group and the two alkyl chains of an anionic phospholipid is important for the best activation of M. smegmatis malate dehydrogenase. | lld:pubmed |
