Abstract
An enzyme which catalyzes the conversion of phosphatidyl glycerol to cardiolipin (diphosphatidyl glycerol) has been found to reside solely in the membrane of Micrococcus lysodeikticus. This enzyme has been tentatively designated as “cardiolipin synthetase”, since its reaction mechanism has not been defined. It appears to synthesize one molecule of cardiolipin from two molecules of phosphatidyl glycerol and the conversion has been followed by using an assay employing 32P-labelled phosphatidyl glycerol as the only added substrate. Higher than 90% conversion of phosphatidyl glycerol to cardiolipin has been achieved with isolated membranes as the enzyme source and by stimulation with Triton X-100. A low-density, small particle fraction bearing “cardiolipin synthetase” activity has been released from whole membranes. Such preparations exhibit activity in the absence of detergent and are devoid of phosphatidic acid cytidyltransferase activity found in whole membranes. In contrast to several other phospholipid synthesizing enzymes reported 1–4, the synthesis of cardiolipin by this enzyme(s) is not dependent upon added Mg 2+ or K +. Cardiolipin synthesis proceeds in the absence of detectable CDP-diglyceride and without significant degradation of phosphatidyl glycerol to phosphatidic acid.
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Schedule a callMore From: Biochimica et Biophysica Acta (BBA)/Lipids and Lipid Metabolism
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