FAD-dependent malate dehydrogenase from Mycobacterium smegmatis: activation of the lipid-depleted inactive enzyme by a phospholipid analogue, di (triethyleneglycoltetradecylether) phosphate.
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.
Imai
T
T
Department of Chemistry, Rikkyo (St. Paul's) University, Tokyo, Japan.
Murata
T
T
D000818:Animals; D002308:Cardiolipins / Q000494:pharmacology; D002417:Cattle; D004789:Enzyme Activation; D005182:Flavin-Adenine Dinucleotide / Q000494:pharmacology*; D008291:Malate Dehydrogenase / Q000378:metabolism*; D009161:Mycobacterium / Q000201:enzymology*; D010755:Organophosphates / Q000494:pharmacology; D010743:Phospholipids / Q000494:pharmacology*
D002308:Cardiolipins; D010755:Organophosphates; D010743:Phospholipids; C063696:di(triethyleneglycoltetradecylether) phosphate; D005182:Flavin-Adenine Dinucleotide; C063695:dioctyl phosphate; D008291:Malate Dehydrogenase; C063697:ditetradecyl phosphate