Hawrot E, Kennedy E P
Proc Natl Acad Sci U S A. 1975 Mar;72(3):1112-6. doi: 10.1073/pnas.72.3.1112.
Phosphatidylserine decarboxylase catalyzes the last step in the pathway leading to phosphatidylethanolamine, the principal membrane lipid of E. coli. Mutants of E. coli have now been isolated in which this enzyme is theramolabile. The structural gene for phosphatidylserine decarboxylase (psd gene) is closely linked to the pur A locus at about 83 min on the standard map of the E. coli chromosome. When a mutant with thermolabile decarboxylase is incubated at 42 degrees, growth ceases, but only after a substantial fraction (20-40%) of the total phospholipid of the cell has been replaced by phosphatidylserine. Examination of such mutants with altered content of phospholipids may shed light on the role of specific phospholipids in membrane function.
磷脂酰丝氨酸脱羧酶催化通向磷脂酰乙醇胺的途径中的最后一步反应，磷脂酰乙醇胺是大肠杆菌的主要膜脂。现已分离出大肠杆菌的突变体，其中这种酶不耐热。磷脂酰丝氨酸脱羧酶的结构基因（psd基因）在大肠杆菌染色体标准图谱上约83分钟处与pur A位点紧密连锁。当具有不耐热脱羧酶的突变体在42摄氏度下培养时，生长停止，但只有在细胞总磷脂的很大一部分（20%-40%）被磷脂酰丝氨酸取代后才会停止。对这种磷脂含量改变的突变体进行研究，可能会揭示特定磷脂在膜功能中的作用。
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