The involvement of guanosine 5-diphosphate-3-diphosphate in the regulation of phospholipid biosynthesis in Escherichia coli. Lack of ppGpp inhibition of acyltransfer from acyl-ACP to sn-glycerol 3-phosphate.
作者： D R Lueking , H Goldfine
DOI: 10.1016/S0021-9258(19)41255-6
关键词:
摘要: The response of the Escherichia coli sn-glycerol-3-phosphate acyltransferase to guanosine 5-diphosphate-3-diphosphate (ppGpp) has been determined in vitro employing palmityl coenzyme A (CoA) and acyl carrier protein as substrates. Levels ppGpp which cause significant inhibition enzyme activity with palmityl-CoA substrate have no effect on when is employed donor. observed was dependent upon relative concentrations MgCl2 (MgCl2 ratio) employed. With donor, PPGpp inhibited production lysophosphatidic acid but not phosphatidic acid. substrate, had influence distribution reaction products.
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