By Moseley Waite (auth.)
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They calculated that the turnover number for the enzyme in vitro was five times lower than that of the activity in situ. While the reason for this higher estimated activity of the enzyme in the membrane is not obvious, it appears evident that diffusion of phospholipid within the membrane is not rate limiting. It remains a problem, however, to define the regulation of this enzyme within the cell and indeed to determine how much of the turnover of cellular phospholipid is the result of this particular phospholipase.
From these data, it was suggested that the transacylase and lysophospholipase L2 activities could be catalyzed by a single enzyme. The plasmid responsible for lysophospholipase L2 activity, pK01, was identified and used to transform an E. , 1983). This resulted in a transformed cell that then overproduced lysophospholipase L 2 • This hybrid plasmid also contained the pldA gene, leading to the conclusion that the pldB gene, coding for lysophospholipase L 2 , is between the pldA and metE genes. While the functions of these phospholipases Al are not fully understood, in all probability this class of enzyme should play a significant function in bacterial membrane metabolism especially under conditions subject to stress.
1978). Sundler et at. (1978) carried out more detailed studies on this enzyme in order to define its interaction with micelles. They used phosphatidylinositol diluted with phosphatidylcholine and Triton X-I 00 as substrate to determine the specificity of binding and the effect of surface dilution or two-dimensional concentration on the enzyme activity. 5:4 gave optimal activity, some 8- to lO-fold higher than that obtained with pure phosphatidylinositol sonicated in buffer. Higher ratios of Triton X-I00:phosphatidylinositol resulted in lowered activity, an observation interpreted by Roberts et al.