Now, Jeremy M. Baskin and co-workers from Cornell University report the directed evolution of an enzyme to enable the efficient conversion of phosphatidylcholine (PC) — the most abundant cellular membrane lipid — to a range of natural and unnatural lipids with diverse structures and functionalities. The work is based on a microbial phospholipase D (PLD) that can catalyse the exchange of phospholipid head groups by transphosphatidylation of PC with exogenous alcohols — to yield phosphatidyl alcohol (PAlc) lipids — or by hydrolysis with water — to yield the natural signalling lipid phosphatidic acid (PA) (pictured; BODIPY, boron dipyrromethene) — however, with limited activity and substrate scope.
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